|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-582 |
2.06e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH---DRHQLLTETCDLKTKVAVLEGDLKQQQK 387
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 388 SIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmVRHQESLQAKQRTLLQ 467
Cdd:COG1196 338 ELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 468 QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLqslqqekQDLEQVTTDLQLTISELRQQLE 547
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-------AELLEEAALLEAALAELLEELA 487
|
250 260 270
....*....|....*....|....*....|....*
gi 755536291 548 ELKERERLLVAFPDLHQPEEAQIQSPTGGEQAAPV 582
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-552 |
4.58e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEHDRHQ 363
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 364 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE-----GERRAAAERQVQQLEeqvqllagRLDGASQQIRWAS 438
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllnEEAANLRERLESLER--------RIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 439 TELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqell 518
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR-------------- 910
|
250 260 270
....*....|....*....|....*....|....*..
gi 755536291 519 qslQQEKQDLEQVTT---DLQLTISELRQQLEELKER 552
Cdd:TIGR02168 911 ---SELRRELEELREklaQLELRLEGLEVRIDNLQER 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-572 |
2.48e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 319 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQ 398
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 399 LEEEGERRAAAERQVQQLEEQVqllAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREE 478
Cdd:COG1196 279 LELELEEAQAEEYELLAELARL---EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 479 LRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVA 558
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250
....*....|....
gi 755536291 559 FPDLHQPEEAQIQS 572
Cdd:COG1196 436 EEEEEEEALEEAAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-606 |
6.58e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 390
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAEL-----------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 391 AMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLD 470
Cdd:COG1196 313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 471 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELK 550
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755536291 551 ERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALV 606
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-572 |
6.20e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAE-----GQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQ 385
Cdd:TIGR02168 218 LKAELRELElallvLRLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 386 QKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTL 465
Cdd:TIGR02168 294 ANEISRLE---QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 466 LQQLDCLDQEREELRGSLDEAE-------AQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQ-----DLEQVTT 533
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLElqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELE 450
|
250 260 270
....*....|....*....|....*....|....*....
gi 755536291 534 DLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQS 572
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-560 |
6.07e-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: 62.78 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 390
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 391 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 457
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 458 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQE 524
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270
....*....|....*....|....*....|....*.
gi 755536291 525 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFP 560
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-556 |
6.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 313 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLltetcdlKTKVAVLEGDLKQQQKSIQAM 392
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAEL-----------EELEAELAELEAELEEL-------RLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 393 EAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQ 468
Cdd:COG1196 294 LAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 469 LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEE 548
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
....*...
gi 755536291 549 LKERERLL 556
Cdd:COG1196 454 LEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-554 |
7.52e-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: 62.78 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 387
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 388 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 452
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 453 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVT 532
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 755536291 533 TDLQLTISELRQQLEELKERER 554
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-552 |
1.50e-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: 61.61 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 370 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 449
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 450 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 529
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180
....*....|....*....|...
gi 755536291 530 QVTTDLQLTISELRQQLEELKER 552
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQ 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-504 |
1.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 367
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 368 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 447
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755536291 448 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-552 |
1.84e-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: 61.23 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 289 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLL 365
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 366 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEegerraaaerqvqqleeqvqllagRLDGASQQIRWASTELDKEK 445
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEA------------------------QIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 446 ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQ----CQLQAQQELLQSL 521
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleALLNERASLEEAL 889
|
250 260 270
....*....|....*....|....*....|....
gi 755536291 522 QQEKQDLEQVTTDLQ---LTISELRQQLEELKER 552
Cdd:TIGR02168 890 ALLRSELEELSEELReleSKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-504 |
2.06e-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: 61.23 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDLTR-LNKHVGALTQL---VGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEH 359
Cdd:TIGR02168 251 AEEELEELTAeLQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 360 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAAAERQvqqleeqvqllAGRLDGASQQIRWAS 438
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQLETL-----------RSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536291 439 TELDKEKARVDSMVRHQESLQAKQRTLLQ------------QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKkleeaelkelqaELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-554 |
5.22e-09 |
|
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: 59.01 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 313 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAM 392
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-----------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 393 EAKAQQLEEEGERRAAAerqvqqleeqvqlLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCL 472
Cdd:COG4942 89 EKEIAELRAELEAQKEE-------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 473 DQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 552
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 755536291 553 ER 554
Cdd:COG4942 236 AA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
374-554 |
5.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 374 KVAVLEGDLKQQQKSIQAMEAKAQQLEEEgeRRAAAERQVQqleeqvqllAGRLDGAS-QQIRWAST-----ELDKEKAR 447
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAE--LDALQERREA---------LQRLAEYSwDEIDVASAereiaELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 448 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 527
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*..
gi 755536291 528 LEQVTTDLQLTISELRQQLEELKERER 554
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-504 |
1.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAegqkdglRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQ 390
Cdd:COG4913 240 AHEALEDA-------REQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 391 AMEAKAQQLEEegERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQ 459
Cdd:COG4913 306 RLEAELERLEA--RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755536291 460 AKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-555 |
2.14e-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: 54.68 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 313 AQLEDA----EGQKDGLRKQVSKLEQALQQeqgqrqrqtEEAERtlakcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 388
Cdd:TIGR02168 189 DRLEDIlnelERQLKSLERQAEKAERYKEL---------KAELR-----ELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 389 IQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIRWASTELDKEKARVDSMVRHQeslQAKQRTLLQQ 468
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEV--------------SELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 469 LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEE 548
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
....*...
gi 755536291 549 L-KERERL 555
Cdd:TIGR02168 398 LnNEIERL 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-567 |
9.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 382 LKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARvdsmvRHQESLQAK 461
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 462 QRTLLQQLdcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQslqqekQDLEQVTTDLQLTISE 541
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*.
gi 755536291 542 LRQQLEELKERERLLVAFPDLHQPEE 567
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEE 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
315-558 |
3.78e-06 |
|
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: 50.34 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 315 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCE----HDRHQLLTETcDLKTKVAVLEGDLKQQQKS 388
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEaeqeLEESKRETET-GIQNLTAEIEQGQESLTEN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 389 IQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQ 468
Cdd:COG5185 356 LEAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 469 ldclDQEREELRGSLDEAEAQRSELEEQLQSLQS--DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQL 546
Cdd:COG5185 419 ----DRQIEELQRQIEQATSSNEEVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV 494
|
250
....*....|..
gi 755536291 547 EELKERERLLVA 558
Cdd:COG5185 495 STLKATLEKLRA 506
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-590 |
5.07e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 370 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 449
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 450 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQ---SDREQEQCQLQAQQELLQSLQQEKQ 526
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQeelAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536291 527 DLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRG 590
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-503 |
1.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 312 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 391
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 392 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 466
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 755536291 467 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-502 |
2.03e-05 |
|
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: 48.13 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQ-------LEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTL---AKC 357
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASL 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 358 EHDRHQLLTETCDLKTKVAVLEgdlKQQQKSIQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIR-W 436
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLE--------------VRIDNLQERLSeE 948
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536291 437 ASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-------QEREELRGSLDEAEAQRSELEEQLQSLQS 502
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-499 |
2.17e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 363
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 364 lLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAA-AERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 441
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLREKREALAElNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYL 662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536291 442 DKEKARVDSMVRHQESLQAK---QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEqLQS 499
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEALYDEAEE-LES 722
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
385-553 |
2.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 385 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 464
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 465 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQ 544
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI-------AELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
....*....
gi 755536291 545 QLEELKERE 553
Cdd:COG4372 172 ELQALSEAE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
288-495 |
2.90e-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: 47.76 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALT---QLvgPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH----- 359
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGeeeQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerei 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 360 -----DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGA 430
Cdd:TIGR02169 346 eeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536291 431 SQQI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 495
Cdd:TIGR02169 426 NAAIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
304-502 |
3.20e-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: 47.48 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 304 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 381
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 382 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 456
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755536291 457 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 502
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
293-564 |
3.68e-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: 47.27 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 293 DLTRLNKHvgalTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQL------LT 366
Cdd:TIGR00618 171 NLFPLDQY----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 367 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqlEEQVQLLAGRLDGASQQIRWASTELDKEKA 446
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 447 RVDSMVRHQESLQAKQRTLLQQ---LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellqslqQ 523
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH------------------T 383
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755536291 524 EKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQ 564
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
328-502 |
4.23e-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: 47.09 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 328 QVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQKSIQAmeakaqQLEEEGE 404
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqDSEHKRKKLEG------QLQELQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 405 RRAAAERQVQQLEEQVQLLAGRLDGASQQIRWA---STELDKEKARVDSMVRH-QESLQAKQRTLLQ---QLDCLDQERE 477
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVSSLLNEAegkNIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERN 499
|
170 180
....*....|....*....|....*
gi 755536291 478 ELRGSLDEAEAQRSELEEQLQSLQS 502
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQA 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-552 |
4.47e-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: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 313 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQrqrqtEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 392
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERY-----AAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 393 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQAK 461
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 462 QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcqlqaqqellqslqqekqDLEQVTTDLQLTISE 541
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------------------------ELEAEIASLERRKSN 437
|
250
....*....|.
gi 755536291 542 LRQQLEELKER 552
Cdd:COG4913 438 IPARLLALRDA 448
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-670 |
4.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 318 AEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQ 397
Cdd:COG3883 14 ADPQIQAKQKELSELQAEL-----------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 398 QLEEE-GER-RAAAERQVQQLEEQVQLLAGRLDGASQQIrwasteldkekARVDSMVRHQESLQAKQRTLLQQLDcldQE 475
Cdd:COG3883 83 ERREElGERaRALYRSGGSVSYLDVLLGSESFSDFLDRL-----------SALSKIADADADLLEELKADKAELE---AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 476 REELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERL 555
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 556 LVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALVPSLQGHPGSNPSSPGPECILRVDRQTAVS 635
Cdd:COG3883 229 AAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSG 308
|
330 340 350
....*....|....*....|....*....|....*
gi 755536291 636 WQQDKQHRQDPSWRAPYIPVSAARRLAQQVLFGGW 670
Cdd:COG3883 309 GAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-486 |
5.07e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 280 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 359
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 360 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 437
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755536291 438 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 486
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
312-555 |
5.83e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 312 RAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAErTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 391
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERL-----------ERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 392 MEAKAQQLEEEGE--RRAAAErqvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVrhqESLqAKQRTLLQQL 469
Cdd:PRK02224 542 LRERAAELEAEAEekREAAAE----------------AEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAI 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 470 DCLDQEREEL---RGSLDEAEAQRSE-LEE------QLQS-LQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQL 537
Cdd:PRK02224 602 ADAEDEIERLrekREALAELNDERRErLAEkrerkrELEAeFDEARIEEAREDKERAEEYLEQVEEKlDELREERDDLQA 681
|
250
....*....|....*....
gi 755536291 538 TISELRQQLEELKE-RERL 555
Cdd:PRK02224 682 EIGAVENELEELEElRERR 700
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
213-555 |
6.33e-05 |
|
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: 46.64 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 213 TSEKTKSVYSQTVETALVPCDACTSVQGSLWEVGKVVIslcQSQNlpSSLGQFQKLVKDSlglkplpaATVGHWAAEQSK 292
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV---QAEN--ARLEMHFKLKEDH--------EKIQHLEEEYKK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 293 DLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrQTEEAERTLAKCEHDRHQLLTETCDLK 372
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE-----------KTKLQDENLKELIEKKDHLTKELEDIK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 373 TKV-------AVLEGDLKQQQKSI-QAMEAKAQQLEEEGERRAAA-------ERQVQQLEEQVQLLAGRLDGASQQIRWA 437
Cdd:pfam05483 303 MSLqrsmstqKALEEDLQIATKTIcQLTEEKEAQMEELNKAKAAHsfvvtefEATTCSLEELLRTEQQRLEKNEDQLKII 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 438 STELDKEKARVDSMVRhqesLQAKQRTLLQQLDCLDQEREELrgsLDEAEaQRSELEEQLQSLQSDreqeqcqlqaQQEL 517
Cdd:pfam05483 383 TMELQKKSSELEEMTK----FKNNKEVELEELKKILAEDEKL---LDEKK-QFEKIAEELKGKEQE----------LIFL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755536291 518 LQSLQQEKQDLEQVTTDLQLTISELRQQLEELK---ERERL 555
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtelEKEKL 485
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
400-552 |
7.82e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 400 EEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL 479
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536291 480 RGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 552
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
288-569 |
8.85e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 358
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 359 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 438
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 439 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELL 518
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755536291 519 QSLQQEKQDLEQVTtdlqltisELRQQLEELKERERLLVAFPDLHQPEEAQ 569
Cdd:PRK02224 610 RLREKREALAELND--------ERRERLAEKRERKRELEAEFDEARIEEAR 652
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
296-552 |
9.50e-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: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 296 RLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQA---LQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 372
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 373 TKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDG-------ASQQIRWASTELDKEK 445
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 446 ARV----DSMVRHQEsLQAKQRTLLQQLD-CLDQER------------------EELRGSLDEAEAQRSELEEQLQSLQS 502
Cdd:pfam01576 306 TELedtlDTTAAQQE-LRSKREQEVTELKkALEEETrsheaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536291 503 DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 552
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
266-501 |
1.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 266 QKLVKDSlGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqr 345
Cdd:COG4717 56 DELFKPQ-GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 346 qteeaertlakcehDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllag 425
Cdd:COG4717 126 --------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE-------------- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536291 426 RLDGASQQIRWAsteldkEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 501
Cdd:COG4717 178 ELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
386-554 |
1.72e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 386 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 464
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 465 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQEKQDLEQVTtdlQLTISELRQ 544
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-----------------LIEEQLQELERIS---GLTAEEAKE 157
|
170
....*....|.
gi 755536291 545 Q-LEELKERER 554
Cdd:PRK12704 158 IlLEKVEEEAR 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
294-501 |
2.19e-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: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 294 LTRLNKHVGALTQLVGPLRAQLEDAE------------GQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDR 361
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEarlshsripeiqAELSKLEEEVSRIEARL-----------REIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 362 HQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTEL 441
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKI 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 442 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELR 480
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVL 985
|
250 260
....*....|....*....|.
gi 755536291 481 GSLDEAEAQRSELEEQLQSLQ 501
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAIL 1006
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-503 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDLTRLNKHvgaltqlvgpLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTL--------- 354
Cdd:pfam01576 648 ALEAKEELERTNKQ----------LRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELqatedaklr 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 355 -------AKCEHDRhqlltetcDLKTKVAVLEGDLKQQQKSIQAMEAkaqQLEEEGERRAAAerqvqqleeqvqlLAGRl 427
Cdd:pfam01576 718 levnmqaLKAQFER--------DLQARDEQGEEKRRQLVKQVRELEA---ELEDERKQRAQA-------------VAAK- 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536291 428 dgasqqiRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:pfam01576 773 -------KKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAE 841
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
354-559 |
3.47e-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: 42.99 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 354 LAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQ 433
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-----------------RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 434 IRWASTEldKEkarVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLqsdreqeqcqlqa 513
Cdd:COG1579 82 LGNVRNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755536291 514 qqellqslqqeKQDLEQVTTDLQLTISELRQQLEELKER--ERLLVAF 559
Cdd:COG1579 144 -----------KAELDEELAELEAELEELEAEREELAAKipPELLALY 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
288-556 |
4.21e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 363
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 364 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 443
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 444 EKAR---------------------VDSMV----RHQESL---QAKQRTLLQQLDCLDQEREELRgslDEAEAQRSELEE 495
Cdd:pfam05483 483 EKLKnieltahcdklllenkeltqeASDMTlelkKHQEDIincKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQ 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536291 496 QLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLL 556
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-569 |
5.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 381 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 460
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 461 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellqslqqeKQDLEQVTTDLQLTIS 540
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--------------------LEQLEREIERLERELE 355
|
170 180
....*....|....*....|....*....
gi 755536291 541 ELRQQLEELKERERLLvafpDLHQPEEAQ 569
Cdd:COG4913 356 ERERRRARLEALLAAL----GLPLPASAE 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
313-504 |
5.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 313 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 392
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 393 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQ-ESLQAKQRTLLQQLDC 471
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 755536291 472 LDQEREELRgslDEAEAQRSELEEQLQSLQSDR 504
Cdd:COG4717 211 LEEELEEAQ---EELEELEEELEQLENELEAAA 240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
311-584 |
6.62e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 311 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 388
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 389 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 466
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 467 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqellqslqqekQDLEQVTTDLQlTISELRQQL 546
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQ------------------------AQLAQLEARLA-ELPELEAEL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755536291 547 EELkERE-----RLLVAFpdLHQPEEAQIQSPTGGEQAAPVDA 584
Cdd:COG3206 354 RRL-EREvevarELYESL--LQRLEEARLAEALTVGNVRVIDP 393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
249-503 |
6.64e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 249 VISLCQSQNLPSSLGQFQK-LVKDSLGLKPLPAAT-VGHWAAEQSKDLT--------RLNKHVGALTQLVGPLRAQLEDA 318
Cdd:TIGR00606 628 LFDVCGSQDEESDLERLKEeIEKSSKQRAMLAGATaVYSQFITQLTDENqsccpvcqRVFQTEAELQEFISDLQSKLRLA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 319 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTetcdLKTKVAVLEGDLKQQQKSIQAMEAKAQQ 398
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK----VNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 399 LE----------------EEGERRAAaerqvqqlEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQ 462
Cdd:TIGR00606 784 AKvcltdvtimerfqmelKDVERKIA--------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755536291 463 RTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
287-501 |
6.69e-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: 42.83 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLT 366
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----------AALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 367 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEG--------------------------ERRAAAE---RQVQQLE 417
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylkylapARREQAEelrADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 418 EQVQllagRLDGASQQIRWASTELDKEKARVdsmvrhqESLQAKQRTLLQQldcLDQEREELRGSLDEAEAQRSELEEQL 497
Cdd:COG4942 164 ALRA----ELEAERAELEALLAELEEERAAL-------EALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
....
gi 755536291 498 QSLQ 501
Cdd:COG4942 230 ARLE 233
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
361-500 |
7.17e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 361 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAA--AErqvqqleeqvqllagrldgASQQIRWAS 438
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVlhAE-------------------DIKALQALR 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536291 439 TELDKEKARVDSMV----RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSL 500
Cdd:pfam07926 64 EELNELKAEIAELKaeaeSAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
287-567 |
8.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 287 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 359
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 360 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 435
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 436 WASTELDKEKARVDSMVRHQESLQAKQRTLlqqldclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQ 515
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755536291 516 ELLQSLQQEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA--FPDLHQPEE 567
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVE---EAEALLEAgkCPECGQPVE 462
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
306-567 |
8.65e-04 |
|
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: 43.03 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 306 QLVGPLRAQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERtLAKCEHDR---HQLLTETCDLKTKVAVLEGDL 382
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRA-----RKAAPLAAHIKA-VTQIEQQAqriHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 383 KQQQKSIQAMEAKAQQLEEEGER-RAAAERQvqqleeqvqllAGRLDGASQQIrwasteldkekarvdSMVRHQESLQAK 461
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHiRDAHEVA-----------TSIREISCQQH---------------TLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 462 QRTLLQQLDCLDQEREELRgsldeaeAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISE 541
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260
....*....|....*....|....*.
gi 755536291 542 LRQQLEELKERERLLVAFPDLHQPEE 567
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQET 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
429-504 |
1.04e-03 |
|
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: 42.06 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536291 429 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
292-544 |
1.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 292 KDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLLTET 368
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 369 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARV 448
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 449 DSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDL 528
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250
....*....|....*.
gi 755536291 529 EQVTTDLQLTISELRQ 544
Cdd:COG4372 285 LEALEEAALELKLLAL 300
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
450-556 |
1.47e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 450 SMVR-HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQR-SELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 527
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*....
gi 755536291 528 LEQVTTDLQLTISELRQQLEELKERERLL 556
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
426-561 |
1.90e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 426 RLDGASQQIRWASTELD---KEKARVDSMVRHQESLQAKQRTLLQQ------LDCLDQEREELRGSLDEAEAQRSELEEQ 496
Cdd:COG1579 39 ELAALEARLEAAKTELEdleKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536291 497 LQSLQSDReqeqcqlqaqQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPD 561
Cdd:COG1579 119 IEELEEEL----------AELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
292-552 |
2.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 292 KDLTRLNKHVGALTqlVGPLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKC--------EHD 360
Cdd:PRK03918 372 EELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 361 RHQLLTE-TCDLKTkvavLEGDLKQQQKSIQAMEAKAQQLEEE--GERR-----AAAERQVQQLEEQVQLLAGRLDGASQ 432
Cdd:PRK03918 450 RKELLEEyTAELKR----IEKELKEIEEKERKLRKELRELEKVlkKESEliklkELAEQLKELEEKLKKYNLEELEKKAE 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 433 QIRWASTELDKEKARVDSMVRHQESLQA---KQRTLLQQLDCLDQEREELRGSLDE-AEAQRSELEEQLQSLQS---DRE 505
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPfynEYL 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536291 506 QEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLT---ISELRQQLEELKER 552
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETekrLEELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
288-562 |
2.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqTEEAERTLAKCEHDRHQLLTE 367
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 368 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQL--LAGRLDGASQQIRWASTELDKEK 445
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 446 --ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRS-------ELEEQlqslqsDReqeqcqlqaqqe 516
Cdd:PRK03918 389 leKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEE------HR------------ 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755536291 517 lLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDL 562
Cdd:PRK03918 451 -KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
288-556 |
2.66e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 367
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 368 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGErraaaerqvQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAr 447
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 448 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQlqslqsdreqeqcqlqaqqellqslqqeKQD 527
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------------------------KKE 507
|
250 260
....*....|....*....|....*....
gi 755536291 528 LEQvttdlqlTISELRQQLEELKERERLL 556
Cdd:TIGR04523 508 LEE-------KVKDLTKKISSLKEKIEKL 529
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
432-551 |
2.72e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 432 QQIRWASTELDKEKARVDS-MVRHQESL-QAKQR-TLLQQL---------DCLDQEREELRGSLDEA-EAQR-------- 490
Cdd:COG3096 839 AALRQRRSELERELAQHRAqEQQLRQQLdQLKEQlQLLNKLlpqanlladETLADRLEELREELDAAqEAQAfiqqhgka 918
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755536291 491 -SELEEQLQSLQSDreqeqcqlqaqqelLQSLQQEKQDLEQVTTDLQltisELRQQLEELKE 551
Cdd:COG3096 919 lAQLEPLVAVLQSD--------------PEQFEQLQADYLQAKEQQR----RLKQQIFALSE 962
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
288-499 |
2.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 288 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 367
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER-----------QDLEQQRKQLEAQIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 368 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 447
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755536291 448 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQS 499
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
424-501 |
3.62e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536291 424 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQ 501
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQ 561
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
456-504 |
3.97e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.48 E-value: 3.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755536291 456 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQER 55
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
456-571 |
4.49e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 456 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlqaqqellqslqqeKQDLEQVT--- 532
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKD---------------------KQSLKNLKarl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755536291 533 TDLQLTISELRQQLEELKER-ERLLVAFPDLHQPEEAQIQ 571
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRfEKVERERDELYDKFEAAIQ 134
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
425-554 |
4.80e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 425 GRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAkqrtllqQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 504
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536291 505 EQEQCQLQAQQELLQSLQ--------------QEKQDLEQVTTDLQLTISELRQQLEELKERER 554
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEedlssleqeienvkSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
531-634 |
5.27e-03 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 40.19 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 531 VTTDLQLTISELRQQLEELKERERLLVAFPdlhQPEEAQIQ------SPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPA 604
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRELDVLNKQR---GDDQRRIEklgqdnAALAEQVKALGANPVTATGEPVPQMPASPPGPE 146
|
90 100 110
....*....|....*....|....*....|
gi 755536291 605 LVPSlqghPGSNPSSPGPECILRVDRQTAV 634
Cdd:PRK13729 147 GEPQ----PGNTPVSFPPQGSVAVPPPTAF 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
443-569 |
5.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 443 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQsLQSDREQEQCQLQAQQELLQSLQ 522
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755536291 523 QEKQDLEQVTtDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQ 569
Cdd:COG4717 150 ELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
361-500 |
5.50e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 38.40 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 361 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllagRLDGASQQIR----- 435
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAI---------------RAEIEKQAIEdmarl 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755536291 436 --WASTELDKEKARVDSMVRHQESLQAkqrtllqqldcLDQEREELRGSLDEAeAQRSELEEQLQSL 500
Cdd:PRK07352 117 kqTAAADLSAEQERVIAQLRREAAELA-----------IAKAESQLPGRLDED-AQQRLIDRSIANL 171
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
272-503 |
5.59e-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: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 272 SLGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLvgplRAQLEDAEGQKDGLRK---QVSKLE----QALQQEQGQRQ 344
Cdd:COG3096 827 AVAFAPDPEAELAALRQRRSELERELAQHRAQEQQL----RQQLDQLKEQLQLLNKllpQANLLAdetlADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 345 RQTEEAERTLAKCEhdrhQLLTEtcdLKTKVAVLEGD-LKQQQKSIQAMEAKAQQ---------LEEEGERRAA-----A 409
Cdd:COG3096 903 DAAQEAQAFIQQHG----KALAQ---LEPLVAVLQSDpEQFEQLQADYLQAKEQQrrlkqqifaLSEVVQRRPHfsyedA 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 410 ERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESL----QAKQRTL------LQQL---------D 470
Cdd:COG3096 976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLqeleqeLEELgvqadaeaeE 1055
|
250 260 270
....*....|....*....|....*....|...
gi 755536291 471 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:COG3096 1056 RARIRRDELHEELSQNRSRRSQLEKQLTRCEAE 1088
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
295-572 |
6.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 295 TRLNKHVGALTQLVGP---LRAQLEDAEGQKDGLRK---QVSKLE----QALQQEQGQRQRQTEEAERTLakcehDRHQ- 363
Cdd:PRK04863 844 RRRVELERALADHESQeqqQRSQLEQAKEGLSALNRllpRLNLLAdetlADRVEEIREQLDEAEEAKRFV-----QQHGn 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 364 LLTEtcdLKTKVAVLEGD------LKQQQKSIQAMEAKAQQ----LEEEGERRAA-----AERQVQQLEEQVQLLAGRLD 428
Cdd:PRK04863 919 ALAQ---LEPIVSVLQSDpeqfeqLKQDYQQAQQTQRDAKQqafaLTEVVQRRAHfsyedAAEMLAKNSDLNEKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 429 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL-----RGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadSGAEERARARRDELHARLSANRSR 1075
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536291 504 ReqeqcqlqaqqellqslqqekqdlEQVTTDLQLTISELRQQLEELKERERllvafpDLHQPEEAQIQS 572
Cdd:PRK04863 1076 R------------------------NQLEKQLTFCEAEMDNLTKKLRKLER------DYHEMREQVVNA 1114
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
319-503 |
6.19e-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: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 319 EGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLLTEtcdlktkvavLEGDLKQQQKSIQAMEAKAQQ 398
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAEE-EEKAKSLSKLKNKHEAMISD----------LEERLKKEEKGRQELEKAKRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 399 LEeeGERRAAAERQVQQLEeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREE 478
Cdd:pfam01576 213 LE--GESTDLQEQIAELQA--------QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
170 180
....*....|....*....|....*
gi 755536291 479 LRGSLDEAEAQRSELEEQLQSLQSD 503
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEELEALKTE 307
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
303-559 |
6.38e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 303 ALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDL 382
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 383 KQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQ 462
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 463 RTLLQQLDCLDQE-----------REELRGSLDEAEAQRSEL-------EEQLQSLQsDReqeqcqlqaqqellqslqqe 524
Cdd:COG1196 738 LEELLEEEELLEEealeelpeppdLEELERELERLEREIEALgpvnllaIEEYEELE-ER-------------------- 796
|
250 260 270
....*....|....*....|....*....|....*..
gi 755536291 525 KQDLEQVTTDLQLTISELRQQLEELKE--RERLLVAF 559
Cdd:COG1196 797 YDFLSEQREDLEEARETLEEAIEEIDRetRERFLETF 833
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-402 |
7.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536291 289 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 368
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 755536291 369 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 402
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| |
