|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-492 |
4.95e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH---DRHQLLTETCDLKTKVAVLEGDLKQQQK 318
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 319 SIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmVRHQESLQAKQRTLLQ 398
Cdd:COG1196 338 ELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 399 QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLE 478
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250
....*....|....
gi 148708515 479 ELKERERLLVAFPD 492
Cdd:COG1196 495 LLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-542 |
1.28e-12 |
|
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: 71.24 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEHDRHQ 294
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 295 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQLEEQVqllagRLDGASQQIRWASTEL 372
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLER-----RIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 373 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellQSL 452
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR--------------SEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 453 QQEKQDLEQVTTDLQLTISELRQQLEELKER-----ERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQA----NAIRIQ 523
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIE 993
|
330
....*....|....*....
gi 148708515 524 VLQEENKRLQSMLTKIREV 542
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDL 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-553 |
3.28e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 321
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAEL------EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 322 AMEAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLL 397
Cdd:COG1196 292 ELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 398 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQL 477
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708515 478 EELKERERLLVAfpdLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKMVPQ 553
Cdd:COG1196 452 AELEEEEEALLE---LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-538 |
1.08e-10 |
|
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: 65.09 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 321
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 322 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 388
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 389 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQE 455
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 456 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPdlhqPEEAQIQSSSNVTQDMERQVQA----NAIRIQVLQEENKR 531
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP----EEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKR 987
|
....*..
gi 148708515 532 LQSMLTK 538
Cdd:TIGR02169 988 LDELKEK 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-545 |
7.13e-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: 62.38 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 301 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 380
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 381 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 460
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 461 QVTTDLQLTISELRQQLEELKER-ERLLVAFPDLhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEE----NKRLQSM 535
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQiEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEAlallRSELEEL 899
|
250
....*....|
gi 148708515 536 LTKIREVAQQ 545
Cdd:TIGR02168 900 SEELRELESK 909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-435 |
2.10e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 298
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 299 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 378
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148708515 379 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 435
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-516 |
2.64e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 220 EQSKDLTRLNKHVGA--LTQLVG---PLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQ 294
Cdd:TIGR02168 217 ELKAELRELELALLVlrLEELREeleELQEELKEAEEELEELTAELQELEEKL-----------EELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 295 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGE----RRAAAERQVQQLeeqvqllagrldgaSQQIRWAST 370
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEelesKLDELAEELAEL--------------EEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 371 ELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQ 450
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708515 451 SLQQEKQ-----DLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQ 516
Cdd:TIGR02168 432 EAELKELqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-485 |
2.82e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 318
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 319 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 383
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 384 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVT 463
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 148708515 464 TDLQLTISELRQQLEELKERER 485
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
312-553 |
7.87e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 312 DLKQQQKSIQAmEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIrwasTELDKEKARVDsmvRHQESLQA 391
Cdd:TIGR02168 217 ELKAELRELEL-ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELE---EEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 392 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELlqslqqeKQDLEQVTTDLQLTIS 471
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK-------LEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 472 ELRQQLEELKERERLLvafpdlhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKMV 551
Cdd:TIGR02168 362 ELEAELEELESRLEEL----------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
..
gi 148708515 552 PQ 553
Cdd:TIGR02168 432 EA 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-485 |
4.27e-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: 56.60 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 220 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLL 296
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 297 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE---GERRAAAERQvqqleeqvqllagRLDGASQQIRWASTELD 373
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALRE-------------ALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 374 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQeqcqlqaqqellqslq 453
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS---------------- 884
|
250 260 270
....*....|....*....|....*....|..
gi 148708515 454 qekqdleqvttdLQLTISELRQQLEELKERER 485
Cdd:TIGR02168 885 ------------LEEALALLRSELEELSEELR 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
244-485 |
4.66e-08 |
|
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: 55.54 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 244 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAM 323
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-----------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 324 EAKAQQLEEEGERRAAAerqvqqleeqvqlLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCL 403
Cdd:COG4942 89 EKEIAELRAELEAQKEE-------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 404 DQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 483
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 148708515 484 ER 485
Cdd:COG4942 236 AA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
305-485 |
1.36e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 305 KVAVLEGDLKQQQKSIQAMEAKAQQLEEEgeRRAAAERQVQqleeqvqllAGRLDGAS-QQIRWAST-----ELDKEKAR 378
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAE--LDALQERREA---------LQRLAEYSwDEIDVASAereiaELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 379 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 458
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*..
gi 148708515 459 LEQVTTDLQLTISELRQQLEELKERER 485
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-435 |
2.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAegqkdglRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQ 321
Cdd:COG4913 240 AHEALEDA-------REQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 322 AMEAKAQQLEEegERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQ 390
Cdd:COG4913 306 RLEAELERLEA--RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148708515 391 AKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 435
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-473 |
2.90e-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: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLL-- 296
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDel 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 297 -TETCDLKTKVAVLEGDLKQQQKSI----QAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTE 371
Cdd:TIGR02168 809 rAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 372 LDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQS 451
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148708515 452 LQQE------------------------------------KQDLEQVTTDLQLTISEL 473
Cdd:TIGR02168 969 EARRrlkrlenkikelgpvnlaaieeyeelkerydfltaqKEDLTEAKETLEEAIEEI 1026
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
219-533 |
6.24e-06 |
|
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: 49.33 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 294
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 295 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 374
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 375 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQ 454
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE-----------------KEMN 545
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708515 455 EKQDLEQVTTDLQLTISELRQQLEELKERERllvAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQ 533
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENAR---SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-459 |
6.40e-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: 49.67 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDLTR-LNKHVGALTQL---VGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRH 293
Cdd:TIGR02168 251 AEEELEELTAeLQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 294 QLLtetcDLKTKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELD 373
Cdd:TIGR02168 331 KLD----ELAEELAELEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 374 KEKARVDSMVRHQESLQAKQRTLLQ------------QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQ 441
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKkleeaelkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250 260
....*....|....*....|.
gi 148708515 442 LQAQQELL---QSLQQEKQDL 459
Cdd:TIGR02168 484 LAQLQARLdslERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-549 |
1.23e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 329 QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQERE 408
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 409 ELRGSLDEAEAQRSELEEQLQSLQSdrEQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLv 488
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL- 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708515 489 afPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREvaQQGGLK 549
Cdd:TIGR02169 832 --EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES--RLGDLK 888
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
462-623 |
1.25e-05 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 48.28 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 462 VTTDLQLTISELRQQLEELKERerllvafpdlhqpeeaqiqsssnvTQDMERQVQANAIRIQVLQEENKRLQSMLTKIRE 541
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRE------------------------LDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 542 VAQQGGLKMVPQGQLWSP-----PYKGIQGATPPAQAQSAFSGLTGRrqSPGSrtsstGRTHPGGLRTSPSRQPGGLPSK 616
Cdd:PRK13729 126 NPVTATGEPVPQMPASPPgpegePQPGNTPVSFPPQGSVAVPPPTAF--YPGN-----GVTPPPQVTYQSVPVPNRIQRK 198
|
....*...
gi 148708515 617 -FSLGDGS 623
Cdd:PRK13729 199 tFTYNEGK 206
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
386-545 |
2.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 386 QESLQAKQRTLLQQLDCLDQEREELRGSLDEAEA-----------------------QRSELEEQLQSLQSDREQEQCQL 442
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvdlseeaklllqQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 443 QAQQELLQSLQQEKQDLEQ--VTTDLQLTISELRQQLEELkeRERLLVAFPDLhQPEEAQIQS--------SSNVTQDME 512
Cdd:COG3206 243 AALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAEL--SARYTPNHPDV-IALRAQIAAlraqlqqeAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|...
gi 148708515 513 RQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 545
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
313-525 |
2.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 313 LKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARvdsmvRHQESLQAK 392
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 393 QRTLLQQLdcldQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlqaqqellqSLQQEKQDLEQVTTDLQltisE 472
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQ----------------LSLATEEELQDLAEELE----E 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148708515 473 LRQQLEELKERERLLVAFPDLHQPEEAQIQSSSnVTQDMERQVQANAIRIQVL 525
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
243-434 |
2.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 243 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 322
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 323 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 397
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 148708515 398 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 434
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-534 |
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 148708515 312 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 391
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 392 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQLTI 470
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRrARLEALLAALGLPL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708515 471 SELRQQLEELKERERLLVAfpdlhQPEEAQIQSSSNVTQDMERQVQANAiRIQVLQEENKRLQS 534
Cdd:COG4913 376 PASAEEFAALRAEAAALLE-----ALEEELEALEEALAEAEAALRDLRR-ELRELEAEIASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
236-528 |
3.94e-05 |
|
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: 46.89 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 236 TQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQL------LTETCDLKTKVAVL 309
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 310 EGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGAS--QQIRWASTELDKEKARVDSMVRHQE 387
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRihTELQSKMRSRAKLLMKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 388 SLQAKQR---TLLQQLDCLDQEREELRGSLDEAEAQRSE-------------LEEQLQSLQSDREQEQCQLQAQQELLQS 451
Cdd:TIGR00618 339 SIEEQRRllqTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihtlqqqkttLTQKLQSLCKELDILQREQATIDTRTSA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 452 LQQEKQDLEQVTTDLQLTISELRQ-------QLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQV 524
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELcaaaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
....
gi 148708515 525 LQEE 528
Cdd:TIGR00618 499 LQEE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-430 |
6.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 294
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 295 lLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAA-AERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 372
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLREKREALAElNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYL 662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708515 373 DKEKARVDSMVRHQESLQAK---QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEqLQS 430
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEALYDEAEE-LES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-483 |
8.18e-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: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 244 AQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 323
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 324 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQAK 392
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 393 QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcqlqaqqellqslqqekqDLEQVTTDLQLTISE 472
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------------------------ELEAEIASLERRKSN 437
|
250
....*....|.
gi 148708515 473 LRQQLEELKER 483
Cdd:COG4913 438 IPARLLALRDA 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
219-534 |
1.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 289
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 290 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 369
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 370 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELL 449
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 450 QSLQQEKQDLEQVTtdlqltisELRQQLEELKERERLLVAFPDLHQPEEAQiqsssnvtQDMER--QVQANAI-RIQVLQ 526
Cdd:PRK02224 610 RLREKREALAELND--------ERRERLAEKRERKRELEAEFDEARIEEAR--------EDKERaeEYLEQVEeKLDELR 673
|
....*...
gi 148708515 527 EENKRLQS 534
Cdd:PRK02224 674 EERDDLQA 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-545 |
1.31e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 360 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQ 439
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 440 CQLQAQQEL-------------------------LQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAfpdLH 494
Cdd:COG4942 97 AELEAQKEElaellralyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA---ER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148708515 495 QPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 545
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
211-417 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 211 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 290
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 291 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 368
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148708515 369 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 417
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
246-553 |
1.69e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 246 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCEHDRH---QLLTETCDLKTKVAVLEGDLKQQQKSI 320
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 321 QAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQl 400
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 401 dclDQEREELRGSLDEAEAQRSELEEQLQSLQS--DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLE 478
Cdd:COG5185 419 ---DRQIEELQRQIEQATSSNEEVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVS 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708515 479 ELKERERLLVAfpdlhqPEEAQIQSSSN-VTQDMERQVQANAIRiqvlQEENKRLQSMLTKIREVAQQGGLKMVPQ 553
Cdd:COG5185 496 TLKATLEKLRA------KLERQLEGVRSkLDQVAESLKDFMRAR----GYAHILALENLIPASELIQASNAKTDGQ 561
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
301-550 |
1.74e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 301 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 380
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 381 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 460
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 461 QVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIR 540
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250
....*....|
gi 148708515 541 EVAQQGGLKM 550
Cdd:COG4372 272 DTEEEELEIA 281
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
243-547 |
1.77e-04 |
|
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: 44.94 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 243 RAQLEDAEGQKDGLRKQVSKLEQALQQEQ------GQRQRQTEEAERTLAKCE-------------HDRHQLLTETC-DL 302
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLADYQQALDVQQtraiqyQQAVQALEKARALCGLPDltpenaedylaafRAKEQQATEEVlEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 303 KTKVAVLEGDLKQQQKSIQAMEAKAqqleEEGERRAAAE--RQVQQLEEQVQLLAGRLdgasQQIRWASTELDKEKARVD 380
Cdd:COG3096 461 EQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQtaRELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQ 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 381 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqellqslqqekQDLE 460
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR------------------------QQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 461 QvttdlqltiseLRQQLEELKERE-RLLVAFPDLHQPEE---AQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSML 536
Cdd:COG3096 589 Q-----------LRARIKELAARApAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALE 657
|
330
....*....|.
gi 148708515 537 TKIREVAQQGG 547
Cdd:COG3096 658 SQIERLSQPGG 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
219-426 |
2.20e-04 |
|
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: 44.67 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQ-LVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH------- 290
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereiee 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 291 ---DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGASQ 363
Cdd:TIGR02169 348 erkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708515 364 QI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 426
Cdd:TIGR02169 428 AIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
227-536 |
2.54e-04 |
|
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: 44.40 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 227 RLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQA---LQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 303
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 304 TKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDG-------ASQQIRWASTELDKEK 376
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 377 ARV----DSMVRHQEsLQAKQRTLLQQLD-CLDQER------------------EELRGSLDEAEAQRSELEEQLQSLQS 433
Cdd:pfam01576 306 TELedtlDTTAAQQE-LRSKREQEVTELKkALEEETrsheaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 434 DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPD-----LHQPE----------- 497
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvsslLNEAEgkniklskdvs 464
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 148708515 498 --EAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSML 536
Cdd:pfam01576 465 slESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL 505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
317-485 |
2.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 317 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 395
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 396 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQEKQDLEQVTtdlQLTISELRQ 475
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-----------------LIEEQLQELERIS---GLTAEEAKE 157
|
170
....*....|.
gi 148708515 476 Q-LEELKERER 485
Cdd:PRK12704 158 IlLEKVEEEAR 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
316-556 |
4.95e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 316 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 395
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 396 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQ-----LTI 470
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 471 SELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKM 550
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
....*.
gi 148708515 551 VPQGQL 556
Cdd:COG4372 259 EIEELE 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
259-545 |
6.26e-04 |
|
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: 43.24 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 259 QVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGdlkQQQKSIQAMEAKAQQLEEEGERRA 338
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ---AKQDSEHKRKKLEGQLQELQARLS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 339 AAERQVQQLEEQVQLLAGRLDGASQQIRWA---STELDKEKARVDSMVRH-QESLQAKQRTLLQ---QLDCLDQEREELR 411
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAegkNIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERNSLQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 412 GSLDEAEAQRSELEEQLQSLQSdreqeqcQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEEL--------KER 483
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA-------QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKaaaydkleKTK 575
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148708515 484 ERLLVAFPDLhqpeeaqiqsssNVTQDMERQVQANairiqvLQEENKRLQSMLTKIREVAQQ 545
Cdd:pfam01576 576 NRLQQELDDL------------LVDLDHQRQLVSN------LEKKQKKFDQMLAEEKAISAR 619
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
356-534 |
8.30e-04 |
|
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: 42.75 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 356 GRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAkqrtllqQLDCLDQEREELRGSLDE-------AEAQRSELEEQL 428
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDElsqelsdASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 429 QSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQ-PE--------EA 499
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEiqaelsklEE 805
|
170 180 190
....*....|....*....|....*....|....*
gi 148708515 500 QIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQS 534
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
381-487 |
9.99e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 381 SMVR-HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQR-SELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 458
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*....
gi 148708515 459 LEQVTTDLQLTISELRQQLEELKERERLL 487
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
219-545 |
1.16e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 219 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 298
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 299 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGErraaaerqvQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAr 378
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 379 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQlqslqsdreqeqcqlqaqqellqslqqeKQD 458
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------------------------KKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 459 LEQVTTDLQLTISELRQQLEEL------KERErllvafpdLHQPEEAQIQSSSNVTQD-MERQVQANAIRIQVLQEENKR 531
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLesekkeKESK--------ISDLEDELNKDDFELKKEnLEKEIDEKNKEIEELKQTQKS 579
|
330
....*....|....
gi 148708515 532 LQSMLTKIREVAQQ 545
Cdd:TIGR04523 580 LKKKQEEKQELIDQ 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-545 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 398 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEqcqlqaqqellqslqqekQDLEQVTTDlQLTISELRQQL 477
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL------------------QRLAEYSWD-EIDVASAEREI 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708515 478 EELK-ERERLLVAFPDLHQPEEaQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 545
Cdd:COG4913 671 AELEaELERLDASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
374-541 |
1.53e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 374 KEKAR--VDSMVRHQESLQAKQRTLLQQLDCLDQERE------ELRGSLDEAEA-----QRSELEEQLQSLQSDReqeqc 440
Cdd:TIGR02169 172 KEKALeeLEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGyellkEKEALERQKEAIERQL----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 441 qlqaqqellqslqqekQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPDLHQPEEAQIQS-----SSNVTQdMERQ 514
Cdd:TIGR02169 247 ----------------ASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIKDLGEEEQLRVKEkigelEAEIAS-LERS 309
|
170 180
....*....|....*....|....*..
gi 148708515 515 VQANAIRIQVLQEENKRLQSMLTKIRE 541
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLA 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-545 |
1.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 397 LQQLDCLDQEREELRGSLDE---AEAQRSELEEQLQSLQSDREQEQCQLQA--QQELLQSLQQEKQDLEQVTTDLQLTIS 471
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148708515 472 ELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSN-VTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 545
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
358-627 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 358 LDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQL--------- 428
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 429 --------------------------------------QSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTI 470
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 471 SELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKM 550
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708515 551 VPQGQLWSPPYKGIQGATPPAQAQSAFSGLTGRRQSPGSRTSSTGRTHPGGLRTSPSRQPGGLPSKFSLGDGSHSAS 627
Cdd:COG3883 258 AAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGS 334
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
331-538 |
1.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 331 EEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL 410
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 411 RGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLvaf 490
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL--- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148708515 491 pdlhqpeEAQIQSSSNVTQDMERQVQANAIRiQVLQEENKRLQSMLTK 538
Cdd:COG4372 163 -------QEELAALEQELQALSEAEAEQALD-ELLKEANRNAEKEEEL 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-545 |
2.43e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 402 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR--------------EQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQ 467
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708515 468 LTISELRQQLEELkeRERLLVAFPDLHQPEEaQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 545
Cdd:TIGR02168 754 KELTELEAEIEEL--EERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-432 |
2.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 225 LTRLNKHVGALTQLVGPLRAQLEDAE------------GQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDR 292
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEarlshsripeiqAELSKLEEEVSRIEARL-----------REIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 293 HQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTEL 372
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKI 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 373 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELR 411
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVL 985
|
250 260
....*....|....*....|.
gi 148708515 412 GSLDEAEAQRSELEEQLQSLQ 432
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-489 |
3.26e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 290
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 291 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 366
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 367 WASTELDKEKARVDSMVRHQESLQAKQRTLlqqldclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQ 446
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148708515 447 ELLQSLQQEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA 489
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVE---EAEALLEA 451
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
235-433 |
3.41e-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: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 235 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 312
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 313 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 387
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148708515 388 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 433
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
218-432 |
4.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqteeaertlakcehDRHQLLT 297
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----------------------QLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 298 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWAsteldkEKA 377
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE--------------ELEELLEQLSLA------TEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148708515 378 RVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 432
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
242-509 |
5.49e-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: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 242 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 319
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 320 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 397
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 398 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqslqqEKQDLEQVTTDLQLTISELRQQL 477
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQA---------------------QLAQLEARLAELPELEAELRRLE 357
|
250 260 270
....*....|....*....|....*....|..
gi 148708515 478 EELKERERLLVAFpdLHQPEEAQIQSSSNVTQ 509
Cdd:COG3206 358 REVEVARELYESL--LQRLEEARLAEALTVGN 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
218-534 |
5.55e-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: 40.16 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 218 AAEQSKDLTRLNKHvgaltqlvgpLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKCEHDRHQ 294
Cdd:pfam01576 648 ALEAKEELERTNKQ----------LRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 295 LLTETCDLKTKvavLEGDL-----------KQQQKSIQAMEAkaqQLEEEGERRAAAerqvqqleeqvqlLAGRldgasq 363
Cdd:pfam01576 718 LEVNMQALKAQ---FERDLqardeqgeekrRQLVKQVRELEA---ELEDERKQRAQA-------------VAAK------ 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 364 qiRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlq 443
Cdd:pfam01576 773 --KKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA---------- 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 444 aqqellqslqqekqDLEQVTTDLQlTISELRQQLEElkERERLlvafpdlhQPEEAQIQSSSNVTQDMERQVQAnaiRIQ 523
Cdd:pfam01576 841 --------------ELLQLQEDLA-ASERARRQAQQ--ERDEL--------ADEIASGASGKSALQDEKRRLEA---RIA 892
|
330
....*....|.
gi 148708515 524 VLQEENKRLQS 534
Cdd:pfam01576 893 QLEEELEEEQS 903
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-435 |
6.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 244 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 323
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 324 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQ-ESLQAKQRTLLQQLDC 402
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 148708515 403 LDQEREELRgslDEAEAQRSELEEQLQSLQSDR 435
Cdd:COG4717 211 LEEELEEAQ---EELEELEEELEQLENELEAAA 240
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
302-541 |
7.08e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 302 LKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTEldKEKARVDS 381
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK--ALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 382 MVRHQESLQAKQRTLLQQL-DCLDQEREELRGSLDEAEAQRSELEEQL--QSLQSDREQEQCQLQAQQELLQSLQQEKQD 458
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHqAWLEEQKEQKREARTEKQAYWQVVEGALdaQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 459 L------EQVTTDLQLTISELRQQLEELKERERLLVAFPD-------LHQP----EEAQIQSS-SNVTQDMERQVQANAI 520
Cdd:pfam12128 760 LaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwlQRRPrlatQLSNIERAiSELQQQLARLIADTKL 839
|
250 260
....*....|....*....|.
gi 148708515 521 RIQVLQEENKRLQSMLTKIRE 541
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSE 860
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
355-432 |
8.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708515 355 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQ 432
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQ 561
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-333 |
8.16e-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: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708515 220 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 299
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 148708515 300 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 333
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| |
