|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
300-571 |
2.08e-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: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH---DRHQLLTETCDLKTKVAVLEGDLKQQQK 376
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 377 SIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmVRHQESLQAKQRTLLQ 456
Cdd:COG1196 338 ELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 457 QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLqslqqekQDLEQVTTDLQLTISELRQQLE 536
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-------AELLEEAALLEAALAELLEELA 487
|
250 260 270
....*....|....*....|....*....|....*
gi 755536295 537 ELKERERLLVAFPDLHQPEEAQIQSPTGGEQAAPV 571
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-542 |
5.82e-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: 72.78 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqteEAERtlakCEHDRHQLLT 355
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--------------EVEQ----LEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 356 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE---GERRAAAERQvqqleeqvqllagRLDGASQQIRWASTELDK 432
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALRE-------------ALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 433 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQ 512
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270
....*....|....*....|....*....|
gi 755536295 513 EKQDLEQVTTDLQLTISELRQQLEELKERE 542
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-561 |
2.26e-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: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 308 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQ 387
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 388 LEEEGERRAAAERQVQQLEEQVqllAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREE 467
Cdd:COG1196 279 LELELEEAQAEEYELLAELARL---EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 468 LRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVA 547
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250
....*....|....
gi 755536295 548 FPDLHQPEEAQIQS 561
Cdd:COG1196 436 EEEEEEEALEEAAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
300-595 |
7.69e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 379
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAEL-----------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 380 AMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLD 459
Cdd:COG1196 313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 460 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELK 539
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755536295 540 ERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALV 595
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-493 |
8.29e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 356
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 357 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLE---EEGERRA-AAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDK 432
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLErriAATERRLeDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536295 433 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
300-561 |
7.62e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAE-----GQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQ 374
Cdd:TIGR02168 218 LKAELRELElallvLRLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 375 QKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTL 454
Cdd:TIGR02168 294 ANEISRLE---QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 455 LQQLDCLDQEREELRGSLDEAE-------AQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQ-----DLEQVTT 522
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLElqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELE 450
|
250 260 270
....*....|....*....|....*....|....*....
gi 755536295 523 DLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQS 561
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
302-545 |
6.95e-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: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 302 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLltetcdlKTKVAVLEGDLKQQQKSIQAM 381
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAEL-----------EELEAELAELEAELEEL-------RLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 382 EAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQ 457
Cdd:COG1196 294 LAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 458 LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEE 537
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
....*...
gi 755536295 538 LKERERLL 545
Cdd:COG1196 454 LEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
300-549 |
7.73e-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: 62.39 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 379
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 380 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 446
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 447 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQE 513
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270
....*....|....*....|....*....|....*.
gi 755536295 514 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFP 549
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
300-543 |
8.64e-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: 62.39 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 376
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 377 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 441
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 442 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVT 521
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 755536295 522 TDLQLTISELRQQLEELKERER 543
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-493 |
1.63e-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: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 356
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 357 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 436
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755536295 437 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-541 |
1.74e-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: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 359 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 438
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 439 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 518
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180
....*....|....*....|...
gi 755536295 519 QVTTDLQLTISELRQQLEELKER 541
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-541 |
2.07e-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: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 278 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLL 354
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 355 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEegerraaaerqvqqleeqvqllagRLDGASQQIRWASTELDKEK 434
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEA------------------------QIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 435 ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQ----CQLQAQQELLQSL 510
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELEseleALLNERASLEEAL 889
|
250 260 270
....*....|....*....|....*....|....
gi 755536295 511 QQEKQDLEQVTTDLQ---LTISELRQQLEELKER 541
Cdd:TIGR02168 890 ALLRSELEELSEELReleSKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-493 |
2.74e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDLTR-LNKHVGALTQL---VGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEH 348
Cdd:TIGR02168 251 AEEELEELTAeLQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 349 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAAAERQvqqleeqvqllAGRLDGASQQIRWAS 427
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQLETL-----------RSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536295 428 TELDKEKARVDSMVRHQESLQAKQRTLLQ------------QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKkleeaelkelqaELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-543 |
5.30e-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: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 302 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAM 381
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-----------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 382 EAKAQQLEEEGERRAAAerqvqqleeqvqlLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCL 461
Cdd:COG4942 89 EKEIAELRAELEAQKEE-------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 462 DQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 541
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 755536295 542 ER 543
Cdd:COG4942 236 AA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
363-543 |
5.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 363 KVAVLEGDLKQQQKSIQAMEAKAQQLEEEgeRRAAAERQVQqleeqvqllAGRLDGAS-QQIRWAST-----ELDKEKAR 436
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAE--LDALQERREA---------LQRLAEYSwDEIDVASAereiaELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 437 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 516
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*..
gi 755536295 517 LEQVTTDLQLTISELRQQLEELKERER 543
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-493 |
1.46e-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: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAegqkdglRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQ 379
Cdd:COG4913 240 AHEALEDA-------REQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 380 AMEAKAQQLEEegERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQ 448
Cdd:COG4913 306 RLEAELERLEA--RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755536295 449 AKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
302-544 |
2.64e-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: 54.29 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 302 AQLEDA----EGQKDGLRKQVSKLEQALQQeqgqrqrqtEEAERtlakcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 377
Cdd:TIGR02168 189 DRLEDIlnelERQLKSLERQAEKAERYKEL---------KAELR-----ELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 378 IQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIRWASTELDKEKARVDSMVRHQeslQAKQRTLLQQ 457
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEV--------------SELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 458 LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEE 537
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
....*...
gi 755536295 538 L-KERERL 544
Cdd:TIGR02168 398 LnNEIERL 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
371-556 |
1.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 371 LKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARvdsmvRHQESLQAK 450
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 451 QRTLLQQLdcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQslqqekQDLEQVTTDLQLTISE 530
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*.
gi 755536295 531 LRQQLEELKERERLLVAFPDLHQPEE 556
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEE 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
304-547 |
5.27e-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: 49.96 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 304 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCE----HDRHQLLTETcDLKTKVAVLEGDLKQQQKS 377
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEaeqeLEESKRETET-GIQNLTAEIEQGQESLTEN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 378 IQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQ 457
Cdd:COG5185 356 LEAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 458 ldclDQEREELRGSLDEAEAQRSELEEQLQSLQS--DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQL 535
Cdd:COG5185 419 ----DRQIEELQRQIEQATSSNEEVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV 494
|
250
....*....|..
gi 755536295 536 EELKERERLLVA 547
Cdd:COG5185 495 STLKATLEKLRA 506
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
359-579 |
8.26e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 359 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 438
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 439 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQ---SDREQEQCQLQAQQELLQSLQQEKQ 515
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQeelAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536295 516 DLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRG 579
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-492 |
2.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 301 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 380
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 381 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 455
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 755536295 456 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
276-488 |
2.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 352
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 353 lLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAA-AERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 430
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLREKREALAElNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYL 662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536295 431 DKEKARVDSMVRHQESLQAK---QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEqLQS 488
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEALYDEAEE-LES 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-491 |
2.73e-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: 47.74 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQ-------LEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTL---AKC 346
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASL 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 347 EHDRHQLLTETCDLKTKVAVLEgdlKQQQKSIQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIR-W 425
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLE--------------VRIDNLQERLSeE 948
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536295 426 ASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-------QEREELRGSLDEAEAQRSELEEQLQSLQS 491
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
374-542 |
3.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 374 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 453
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 454 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQ 533
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI-------AELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
....*....
gi 755536295 534 QLEELKERE 542
Cdd:COG4372 172 ELQALSEAE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
277-484 |
3.70e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALT---QLvgPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH----- 348
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGeeeQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerei 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 349 -----DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGA 419
Cdd:TIGR02169 346 eeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536295 420 SQQI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 484
Cdd:TIGR02169 426 NAAIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
307-659 |
4.79e-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: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 307 AEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQ 386
Cdd:COG3883 14 ADPQIQAKQKELSELQAEL-----------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 387 QLEEE-GER-RAAAERQVQQLEEQVQLLAGRLDGASQQIrwasteldkekARVDSMVRHQESLQAKQRTLLQQLDcldQE 464
Cdd:COG3883 83 ERREElGERaRALYRSGGSVSYLDVLLGSESFSDFLDRL-----------SALSKIADADADLLEELKADKAELE---AK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 465 REELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERL 544
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 545 LVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALVPSLQGHPGSNPSSPGPECILRVDRQTAVS 624
Cdd:COG3883 229 AAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSG 308
|
330 340 350
....*....|....*....|....*....|....*
gi 755536295 625 WQQDKQHRQDPSWRAPYIPVSAARRLAQQVLFGGW 659
Cdd:COG3883 309 GAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-541 |
4.93e-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: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 302 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQrqrqtEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 381
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERY-----AAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 382 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQAK 450
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 451 QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcqlqaqqellqslqqekqDLEQVTTDLQLTISE 530
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------------------------ELEAEIASLERRKSN 437
|
250
....*....|.
gi 755536295 531 LRQQLEELKER 541
Cdd:COG4913 438 IPARLLALRDA 448
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
293-491 |
5.50e-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: 46.71 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 293 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 370
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 371 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 445
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755536295 446 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 491
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
282-553 |
6.01e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 282 DLTRLNKHvgalTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQL------LT 355
Cdd:TIGR00618 171 NLFPLDQY----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 356 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqlEEQVQLLAGRLDGASQQIRWASTELDKEKA 435
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 436 RVDSMVRHQESLQAKQRTLLQQ---LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellqslqQ 512
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH------------------T 383
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755536295 513 EKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQ 553
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 ... |
317-491 |
6.30e-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: 46.71 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 317 QVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQKSIQAmeakaqQLEEEGE 393
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqDSEHKRKKLEG------QLQELQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 394 RRAAAERQVQQLEEQVQLLAGRLDGASQQIRWA---STELDKEKARVDSMVRH-QESLQAKQRTLLQ---QLDCLDQERE 466
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVSSLLNEAegkNIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERN 499
|
170 180
....*....|....*....|....*
gi 755536295 467 ELRGSLDEAEAQRSELEEQLQSLQS 491
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQA 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
269-475 |
6.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 269 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 348
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 349 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 426
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755536295 427 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 475
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
202-544 |
8.03e-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: 46.25 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 202 TSEKTKSVYSQTVETALVPCDACTSVQGSLWEVGKVVIslcQSQNlpSSLGQFQKLVKDSlglkplpaATVGHWAAEQSK 281
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV---QAEN--ARLEMHFKLKEDH--------EKIQHLEEEYKK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 282 DLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrQTEEAERTLAKCEHDRHQLLTETCDLK 361
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE-----------KTKLQDENLKELIEKKDHLTKELEDIK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 362 TKV-------AVLEGDLKQQQKSI-QAMEAKAQQLEEEGERRAAA-------ERQVQQLEEQVQLLAGRLDGASQQIRWA 426
Cdd:pfam05483 303 MSLqrsmstqKALEEDLQIATKTIcQLTEEKEAQMEELNKAKAAHsfvvtefEATTCSLEELLRTEQQRLEKNEDQLKII 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 427 STELDKEKARVDSMVRhqesLQAKQRTLLQQLDCLDQEREELrgsLDEAEaQRSELEEQLQSLQSDreqeqcqlqaQQEL 506
Cdd:pfam05483 383 TMELQKKSSELEEMTK----FKNNKEVELEELKKILAEDEKL---LDEKK-QFEKIAEELKGKEQE----------LIFL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755536295 507 LQSLQQEKQDLEQVTTDLQLTISELRQQLEELK---ERERL 544
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtelEKEKL 485
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
301-544 |
8.46e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 301 RAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAErTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 380
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERL-----------ERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 381 MEAKAQQLEEEGE--RRAAAErqvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVrhqESLqAKQRTLLQQL 458
Cdd:PRK02224 542 LRERAAELEAEAEekREAAAE----------------AEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAI 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 459 DCLDQEREEL---RGSLDEAEAQRSE-LEE------QLQS-LQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQL 526
Cdd:PRK02224 602 ADAEDEIERLrekREALAELNDERRErLAEkrerkrELEAeFDEARIEEAREDKERAEEYLEQVEEKlDELREERDDLQA 681
|
250
....*....|....*....
gi 755536295 527 TISELRQQLEELKE-RERL 544
Cdd:PRK02224 682 EIGAVENELEELEElRERR 700
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
389-541 |
1.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 389 EEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL 468
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536295 469 RGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 541
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-558 |
1.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 347
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 348 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 427
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 428 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELL 507
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755536295 508 QSLQQEKQDLEQVTtdlqltisELRQQLEELKERERLLVAFPDLHQPEEAQ 558
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 ... |
285-541 |
1.40e-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: 45.55 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 285 RLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQA---LQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 361
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 362 TKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDG-------ASQQIRWASTELDKEK 434
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 435 ARV----DSMVRHQEsLQAKQRTLLQQLD-CLDQER------------------EELRGSLDEAEAQRSELEEQLQSLQS 491
Cdd:pfam01576 306 TELedtlDTTAAQQE-LRSKREQEVTELKkALEEETrsheaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536295 492 DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 541
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
375-543 |
1.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 375 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 453
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 454 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQEKQDLEQVTtdlQLTISELRQ 533
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-----------------LIEEQLQELERIS---GLTAEEAKE 157
|
170
....*....|.
gi 755536295 534 Q-LEELKERER 543
Cdd:PRK12704 158 IlLEKVEEEAR 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
255-490 |
2.42e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 255 QKLVKDSlGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqr 334
Cdd:COG4717 56 DELFKPQ-GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 335 qteeaertlakcehDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllag 414
Cdd:COG4717 126 --------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE-------------- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536295 415 RLDGASQQIRWAsteldkEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 490
Cdd:COG4717 178 ELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-490 |
2.85e-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: 44.29 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 283 LTRLNKHVGALTQLVGPLRAQLEDAE------------GQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDR 350
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEarlshsripeiqAELSKLEEEVSRIEARL-----------REIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 351 HQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTEL 430
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKI 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 431 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELR 469
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVL 985
|
250 260
....*....|....*....|.
gi 755536295 470 GSLDEAEAQRSELEEQLQSLQ 490
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 ... |
276-492 |
4.86e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDLTRLNKHvgaltqlvgpLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTL--------- 343
Cdd:pfam01576 648 ALEAKEELERTNKQ----------LRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELqatedaklr 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 344 -------AKCEHDRhqlltetcDLKTKVAVLEGDLKQQQKSIQAMEAkaqQLEEEGERRAAAerqvqqleeqvqlLAGRl 416
Cdd:pfam01576 718 levnmqaLKAQFER--------DLQARDEQGEEKRRQLVKQVRELEA---ELEDERKQRAQA-------------VAAK- 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536295 417 dgasqqiRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:pfam01576 773 -------KKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAE 841
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
277-545 |
5.12e-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: 43.56 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 352
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 353 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 432
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 433 EKAR---------------------VDSMV----RHQESL---QAKQRTLLQQLDCLDQEREELRgslDEAEAQRSELEE 484
Cdd:pfam05483 483 EKLKnieltahcdklllenkeltqeASDMTlelkKHQEDIincKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQ 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536295 485 QLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLL 545
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
343-548 |
5.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 343 LAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQ 422
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-----------------RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 423 IRWASTEldKEkarVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLqsdreqeqcqlqa 502
Cdd:COG1579 82 LGNVRNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755536295 503 qqellqslqqeKQDLEQVTTDLQLTISELRQQLEELKER--ERLLVAF 548
Cdd:COG1579 144 -----------KAELDEELAELEAELEELEAEREELAAKipPELLALY 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-547 |
6.56e-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: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 370 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 449
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 450 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQLTI 528
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRrARLEALLAALGLPL 375
|
170
....*....|....*....
gi 755536295 529 SELRQQLEELKERERLLVA 547
Cdd:COG4913 376 PASAEEFAALRAEAAALLE 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-490 |
7.75e-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: 42.44 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLT 355
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----------AALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 356 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEG--------------------------ERRAAAE---RQVQQLE 406
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylkylapARREQAEelrADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 407 EQVQllagRLDGASQQIRWASTELDKEKARVdsmvrhqESLQAKQRTLLQQldcLDQEREELRGSLDEAEAQRSELEEQL 486
Cdd:COG4942 164 ALRA----ELEAERAELEALLAELEEERAAL-------EALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
....
gi 755536295 487 QSLQ 490
Cdd:COG4942 230 ARLE 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
300-573 |
8.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 300 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 377
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 378 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 455
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 456 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqellqslqqekQDLEQVTTDLQlTISELRQQL 535
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQ------------------------AQLAQLEARLA-ELPELEAEL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755536295 536 EELkERE-----RLLVAFpdLHQPEEAQIQSPTGGEQAAPVDA 573
Cdd:COG3206 354 RRL-EREvevarELYESL--LQRLEEARLAEALTVGNVRVIDP 393
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
302-493 |
8.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 302 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 381
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 382 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQ-ESLQAKQRTLLQQLDC 460
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 755536295 461 LDQEREELRgslDEAEAQRSELEEQLQSLQSDR 493
Cdd:COG4717 211 LEEELEEAQ---EELEELEEELEQLENELEAAA 240
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
238-492 |
9.55e-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: 42.73 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 238 VISLCQSQNLPSSLGQFQK-LVKDSLGLKPLPAAT-VGHWAAEQSKDLT--------RLNKHVGALTQLVGPLRAQLEDA 307
Cdd:TIGR00606 628 LFDVCGSQDEESDLERLKEeIEKSSKQRAMLAGATaVYSQFITQLTDENqsccpvcqRVFQTEAELQEFISDLQSKLRLA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 308 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTetcdLKTKVAVLEGDLKQQQKSIQAMEAK--- 384
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK----VNRDIQRLKNDIEEQETLLGTIMPEees 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 385 ----------AQQLEEEGErraaaERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTL 454
Cdd:TIGR00606 784 akvcltdvtiMERFQMELK-----DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
250 260 270
....*....|....*....|....*....|....*...
gi 755536295 455 LQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
276-556 |
9.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 276 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 348
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 349 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 424
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 425 WASTELDKEKARVDSMVRHQESLQAKQRTLlqqldclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQ 504
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755536295 505 ELLQSLQQEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA--FPDLHQPEE 556
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVE---EAEALLEAgkCPECGQPVE 462
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
350-489 |
1.13e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 350 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAA--AErqvqqleeqvqllagrldgASQQIRWAS 427
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVlhAE-------------------DIKALQALR 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536295 428 TELDKEKARVDSMV----RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSL 489
Cdd:pfam07926 64 EELNELKAEIAELKaeaeSAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
418-493 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536295 418 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
295-556 |
1.27e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 295 QLVGPLRAQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERtLAKCEHDR---HQLLTETCDLKTKVAVLEGDL 371
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRA-----RKAAPLAAHIKA-VTQIEQQAqriHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 372 KQQQKSIQAMEAKAQQLEEEGER-RAAAERQvqqleeqvqllAGRLDGASQQIrwasteldkekarvdSMVRHQESLQAK 450
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHiRDAHEVA-----------TSIREISCQQH---------------TLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 451 QRTLLQQLDCLDQEREELRgsldeaeAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISE 530
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260
....*....|....*....|....*.
gi 755536295 531 LRQQLEELKERERLLVAFPDLHQPEE 556
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQET 486
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
439-545 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 439 SMVR-HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQR-SELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 516
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*....
gi 755536295 517 LEQVTTDLQLTISELRQQLEELKERERLL 545
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
281-533 |
1.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 281 KDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLLTET 357
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 358 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARV 437
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 438 DSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDL 517
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250
....*....|....*.
gi 755536295 518 EQVTTDLQLTISELRQ 533
Cdd:COG4372 285 LEALEEAALELKLLAL 300
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
415-550 |
2.41e-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: 40.29 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 415 RLDGASQQIRWASTELD---KEKARVDSMVRHQESLQAKQRTLLQQ------LDCLDQEREELRGSLDEAEAQRSELEEQ 485
Cdd:COG1579 39 ELAALEARLEAAKTELEdleKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536295 486 LQSLQSDReqeqcqlqaqQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPD 550
Cdd:COG1579 119 IEELEEEL----------AELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-545 |
2.46e-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: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 356
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 357 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGErraaaerqvQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAr 436
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 437 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQlqslqsdreqeqcqlqaqqellqslqqeKQD 516
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------------------------KKE 507
|
250 260
....*....|....*....|....*....
gi 755536295 517 LEQvttdlqlTISELRQQLEELKERERLL 545
Cdd:TIGR04523 508 LEE-------KVKDLTKKISSLKEKIEKL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
281-541 |
3.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 281 KDLTRLNKHVGALTqlVGPLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKC--------EHD 349
Cdd:PRK03918 372 EELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 350 RHQLLTE-TCDLKTkvavLEGDLKQQQKSIQAMEAKAQQLEEE--GERR-----AAAERQVQQLEEQVQLLAGRLDGASQ 421
Cdd:PRK03918 450 RKELLEEyTAELKR----IEKELKEIEEKERKLRKELRELEKVlkKESEliklkELAEQLKELEEKLKKYNLEELEKKAE 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 422 QIRWASTELDKEKARVDSMVRHQESLQA---KQRTLLQQLDCLDQEREELRGSLDE-AEAQRSELEEQLQSLQS---DRE 494
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPfynEYL 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536295 495 QEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLT---ISELRQQLEELKER 541
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETekrLEELRKELEELEKK 655
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
421-540 |
3.35e-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: 41.09 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 421 QQIRWASTELDKEKARVDS-MVRHQESL-QAKQR-TLLQQL---------DCLDQEREELRGSLDEA-EAQR-------- 479
Cdd:COG3096 839 AALRQRRSELERELAQHRAqEQQLRQQLdQLKEQlQLLNKLlpqanlladETLADRLEELREELDAAqEAQAfiqqhgka 918
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755536295 480 -SELEEQLQSLQSDreqeqcqlqaqqelLQSLQQEKQDLEQVTTDLQltisELRQQLEELKE 540
Cdd:COG3096 919 lAQLEPLVAVLQSD--------------PEQFEQLQADYLQAKEQQR----RLKQQIFALSE 962
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-551 |
3.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqTEEAERTLAKCEHDRHQLLTE 356
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 357 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQL--LAGRLDGASQQIRWASTELDKEK 434
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 435 --ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRS-------ELEEQlqslqsdreqeqcqlqaqqE 505
Cdd:PRK03918 389 leKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEE-------------------H 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755536295 506 LLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDL 551
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
413-490 |
3.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 3.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536295 413 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQ 490
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQ 561
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
520-623 |
4.36e-03 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 40.19 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 520 VTTDLQLTISELRQQLEELKERERLLVAFPdlhQPEEAQIQ------SPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPA 593
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRELDVLNKQR---GDDQRRIEklgqdnAALAEQVKALGANPVTATGEPVPQMPASPPGPE 146
|
90 100 110
....*....|....*....|....*....|
gi 755536295 594 LVPSlqghPGSNPSSPGPECILRVDRQTAV 623
Cdd:PRK13729 147 GEPQ----PGNTPVSFPPQGSVAVPPPTAF 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
277-488 |
4.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 277 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 356
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER-----------QDLEQQRKQLEAQIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 357 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 436
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755536295 437 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQS 488
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
445-493 |
4.95e-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: 36.09 E-value: 4.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755536295 445 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQER 55
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
414-543 |
5.08e-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: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 414 GRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAkqrtllqQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 493
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536295 494 EQEQCQLQAQQELLQSLQ--------------QEKQDLEQVTTDLQLTISELRQQLEELKERER 543
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEedlssleqeienvkSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
445-560 |
6.09e-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: 38.73 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 445 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlqaqqellqslqqeKQDLEQVT--- 521
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKD---------------------KQSLKNLKarl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755536295 522 TDLQLTISELRQQLEELKER-ERLLVAFPDLHQPEEAQIQ 560
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRfEKVERERDELYDKFEAAIQ 134
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
432-558 |
6.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 432 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQsLQSDREQEQCQLQAQQELLQSLQ 511
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755536295 512 QEKQDLEQVTtDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQ 558
Cdd:COG4717 150 ELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
350-489 |
6.22e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 38.40 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 350 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASqqirwastE 429
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAA--------D 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 430 LDKEKARVDSMVRHQESLQAkqrtllqqldcLDQEREELRGSLDEAeAQRSELEEQLQSL 489
Cdd:PRK07352 124 LSAEQERVIAQLRREAAELA-----------IAKAESQLPGRLDED-AQQRLIDRSIANL 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
292-548 |
7.42e-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: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 292 ALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDL 371
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 372 KQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQ 451
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 452 RTLLQQLDCLDQE-----------REELRGSLDEAEAQRSEL-------EEQLQSLQsDReqeqcqlqaqqellqslqqe 513
Cdd:COG1196 738 LEELLEEEELLEEealeelpeppdLEELERELERLEREIEALgpvnllaIEEYEELE-ER-------------------- 796
|
250 260 270
....*....|....*....|....*....|....*..
gi 755536295 514 KQDLEQVTTDLQLTISELRQQLEELKE--RERLLVAF 548
Cdd:COG1196 797 YDFLSEQREDLEEARETLEEAIEEIDRetRERFLETF 833
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
261-492 |
7.44e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 261 SLGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLvgplRAQLEDAEGQKDGLRK---QVSKLE----QALQQEQGQRQ 333
Cdd:COG3096 827 AVAFAPDPEAELAALRQRRSELERELAQHRAQEQQL----RQQLDQLKEQLQLLNKllpQANLLAdetlADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 334 RQTEEAERTLAKCEhdrhQLLTEtcdLKTKVAVLEGD-LKQQQKSIQAMEAKAQQ---------LEEEGERRAA-----A 398
Cdd:COG3096 903 DAAQEAQAFIQQHG----KALAQ---LEPLVAVLQSDpEQFEQLQADYLQAKEQQrrlkqqifaLSEVVQRRPHfsyedA 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 399 ERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESL----QAKQRTL------LQQL---------D 459
Cdd:COG3096 976 VGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLqeleqeLEELgvqadaeaeE 1055
|
250 260 270
....*....|....*....|....*....|...
gi 755536295 460 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:COG3096 1056 RARIRRDELHEELSQNRSRRSQLEKQLTRCEAE 1088
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
308-492 |
7.71e-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: 39.77 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 308 EGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLLTEtcdlktkvavLEGDLKQQQKSIQAMEAKAQQ 387
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAEE-EEKAKSLSKLKNKHEAMISD----------LEERLKKEEKGRQELEKAKRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 388 LEeeGERRAAAERQVQQLEeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREE 467
Cdd:pfam01576 213 LE--GESTDLQEQIAELQA--------QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
170 180
....*....|....*....|....*
gi 755536295 468 LRGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEELEALKTE 307
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
278-391 |
7.73e-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: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 278 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 357
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 755536295 358 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 391
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
284-493 |
7.95e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 284 TRLNKHVGALTQLVGP---LRAQLEDAEGQKDGLRK---QVSKLE----QALQQEQGQRQRQTEEAERTLakcehDRHQ- 352
Cdd:PRK04863 844 RRRVELERALADHESQeqqQRSQLEQAKEGLSALNRllpRLNLLAdetlADRVEEIREQLDEAEEAKRFV-----QQHGn 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 353 LLTEtcdLKTKVAVLEGD------LKQQQKSIQAMEAKAQQ----LEEEGERRAA-----AERQVQQLEEQVQLLAGRLD 417
Cdd:PRK04863 919 ALAQ---LEPIVSVLQSDpeqfeqLKQDYQQAQQTQRDAKQqafaLTEVVQRRAHfsyedAAEMLAKNSDLNEKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536295 418 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL-----RGSLDEAEAQRSELEEQLQSLQSD 492
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadSGAEERARARRDELHARLSANRSR 1075
|
.
gi 755536295 493 R 493
Cdd:PRK04863 1076 R 1076
|
|
| |
