|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-448 |
4.90e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH---DRHQLLTETCDLKTKVAVLEGDLKQQQK 274
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 275 SIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmVRHQESLQAKQRTLLQ 354
Cdd:COG1196 338 ELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 355 QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLE 434
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250
....*....|....
gi 1907080929 435 ELKERERLLVAFPD 448
Cdd:COG1196 495 LLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-498 |
1.84e-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: 70.47 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEHDRHQ 250
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 251 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQLEEQVqllagRLDGASQQIRWASTEL 328
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLER-----RIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 329 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellQSL 408
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR--------------SEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 409 QQEKQDLEQVTTDLQLTISELRQQLEELKER-----ERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQA----NAIRIQ 479
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIE 993
|
330
....*....|....*....
gi 1907080929 480 VLQEENKRLQSMLTKIREV 498
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDL 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-509 |
2.91e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 180 DLTRLNKHVGALTQLVGPLRAQLEDAE------GQKDGLRKQVSKLE-QALQQEQGQRQRQTEEAERTLAKCEHDRHQLL 252
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAEKAEryrelkEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 253 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 328
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 329 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSL 408
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 409 QQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAfpdLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRL 488
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE---LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|.
gi 1907080929 489 QSMLTKIREVAQQGGLKMVPQ 509
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAG 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-494 |
1.57e-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: 64.32 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 278 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 344
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 345 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQE 411
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 412 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSM 491
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
...
gi 1907080929 492 LTK 494
Cdd:TIGR02169 992 KEK 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-501 |
1.07e-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: 61.61 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 257 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 336
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 337 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 416
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 417 QVTTDLQLTISELRQQLEELKER-ERLLVAFPDLhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEE----NKRLQSM 491
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQiEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEAlallRSELEEL 899
|
250
....*....|
gi 1907080929 492 LTKIREVAQQ 501
Cdd:TIGR02168 900 SEELRELESK 909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-391 |
2.25e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 254
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 334
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080929 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-441 |
3.37e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 274
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 275 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 339
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 340 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVT 419
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 1907080929 420 TDLQLTISELRQQLEELKERER 441
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-472 |
4.40e-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: 59.69 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKL-----------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 278 AMEAKAQQLEEEGE----RRAAAERQVQQLeeqvqllagrldgaSQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLL 353
Cdd:TIGR02168 313 NLERQLEELEAQLEelesKLDELAEELAEL--------------EEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 354 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQ-----DLEQVTTDLQLTISE 428
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907080929 429 LRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQ 472
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-509 |
1.04e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 268 DLKQQQKSIQAmEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIrwasTELDKEKARVDsmvRHQESLQA 347
Cdd:TIGR02168 217 ELKAELRELEL-ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELE---EEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 348 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELlqslqqeKQDLEQVTTDLQLTIS 427
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK-------LEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 428 ELRQQLEELKERERLLvafpdlhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKMV 507
Cdd:TIGR02168 362 ELEAELEELESRLEEL----------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
..
gi 1907080929 508 PQ 509
Cdd:TIGR02168 432 EA 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
200-441 |
6.55e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 200 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-----------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 280 EAKAQQLEEEGERRAAAerqvqqleeqvqlLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCL 359
Cdd:COG4942 89 EKEIAELRAELEAQKEE-------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 360 DQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 439
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 1907080929 440 ER 441
Cdd:COG4942 236 AA 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-441 |
6.92e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLL 252
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 253 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE---GERRAAAERQvqqleeqvqllagRLDGASQQIRWASTELD 329
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALRE-------------ALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 330 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQeqcqlqaqqellqslq 409
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS---------------- 884
|
250 260 270
....*....|....*....|....*....|..
gi 1907080929 410 qekqdleqvttdLQLTISELRQQLEELKERER 441
Cdd:TIGR02168 885 ------------LEEALALLRSELEELSEELR 904
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-441 |
1.78e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 261 KVAVLEGDLKQQQKSIQAMEAKAQQLEEEgeRRAAAERQVQqleeqvqllAGRLDGAS-QQIRWAST-----ELDKEKAR 334
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAE--LDALQERREA---------LQRLAEYSwDEIDVASAereiaELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 414
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*..
gi 1907080929 415 LEQVTTDLQLTISELRQQLEELKERER 441
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-391 |
2.95e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAegqkdglRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQ 277
Cdd:COG4913 240 AHEALEDA-------REQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 278 AMEAKAQQLEEegERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQ 346
Cdd:COG4913 306 RLEAELERLEA--RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907080929 347 AKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-429 |
3.50e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLL-- 252
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDel 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 253 -TETCDLKTKVAVLEGDLKQQQKSI----QAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTE 327
Cdd:TIGR02168 809 rAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 328 LDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQS 407
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080929 408 LQQE------------------------------------KQDLEQVTTDLQLTISEL 429
Cdd:TIGR02168 969 EARRrlkrlenkikelgpvnlaaieeyeelkerydfltaqKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-415 |
8.73e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 174 AAEQSKDLTR-LNKHVGALTQL---VGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRH 249
Cdd:TIGR02168 251 AEEELEELTAeLQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 250 QLLtetcDLKTKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELD 329
Cdd:TIGR02168 331 KLD----ELAEELAELEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 330 KEKARVDSMVRHQESLQAKQRTLLQ------------QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQ 397
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKkleeaelkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250 260
....*....|....*....|.
gi 1907080929 398 LQAQQELL---QSLQQEKQDL 415
Cdd:TIGR02168 484 LAQLQARLdslERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-505 |
1.34e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 285 QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQERE 364
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 365 ELRGSLDEAEAQRSELEEQLQSLQSdrEQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLv 444
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL- 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907080929 445 afPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREvaQQGGLK 505
Cdd:TIGR02169 832 --EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES--RLGDLK 888
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-489 |
1.85e-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: 47.79 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 250
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 251 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 330
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 331 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQ 410
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE-----------------KEMN 545
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080929 411 EKQDLEQVTTDLQLTISELRQQLEELKERERllvAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQ 489
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENAR---SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
418-579 |
1.86e-05 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 47.51 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 418 VTTDLQLTISELRQQLEELKERerllvafpdlhqpeeaqiqsssnvTQDMERQVQANAIRIQVLQEENKRLQSMLTKIRE 497
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRE------------------------LDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 498 VAQQGGLKMVPQGQLWSP-----PYKGIQGATPPAQAQSAFSGLTGRrqSPGSrtsstGRTHPGGLRTSPSRQPGGLPSK 572
Cdd:PRK13729 126 NPVTATGEPVPQMPASPPgpegePQPGNTPVSFPPQGSVAVPPPTAF--YPGN-----GVTPPPQVTYQSVPVPNRIQRK 198
|
....*...
gi 1907080929 573 -FSLGDGS 579
Cdd:PRK13729 199 tFTYNEGK 206
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-501 |
2.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 342 QESLQAKQRTLLQQLDCLDQEREELRGSLDEAEA-----------------------QRSELEEQLQSLQSDREQEQCQL 398
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvdlseeaklllqQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 399 QAQQELLQSLQQEKQDLEQ--VTTDLQLTISELRQQLEELkeRERLLVAFPDLhQPEEAQIQS--------SSNVTQDME 468
Cdd:COG3206 243 AALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAEL--SARYTPNHPDV-IALRAQIAAlraqlqqeAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|...
gi 1907080929 469 RQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 501
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-390 |
3.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 279 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 353
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907080929 354 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 390
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-481 |
3.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 269 LKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARvdsmvRHQESLQAK 348
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 349 QRTLLQQLdcldQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlqaqqellqSLQQEKQDLEQVTTDLQltisE 428
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQ----------------LSLATEEELQDLAEELE----E 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907080929 429 LRQQLEELKERERLLVAFPDLHQPEEAQIQSSSnVTQDMERQVQANAIRIQVL 481
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-490 |
3.78e-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: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 268 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 347
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 348 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQLTI 426
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRrARLEALLAALGLPL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907080929 427 SELRQQLEELKERERLLVAfpdlhQPEEAQIQSSSNVTQDMERQVQANAiRIQVLQEENKRLQS 490
Cdd:COG4913 376 PASAEEFAALRAEAAALLE-----ALEEELEALEEALAEAEAALRDLRR-ELRELEAEIASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
192-484 |
7.91e-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: 45.73 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 192 TQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQL------LTETCDLKTKVAVL 265
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 266 EGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGAS--QQIRWASTELDKEKARVDSMVRHQE 343
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRihTELQSKMRSRAKLLMKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 344 SLQAKQR---TLLQQLDCLDQEREELRGSLDEAEAQRSE-------------LEEQLQSLQSDREQEQCQLQAQQELLQS 407
Cdd:TIGR00618 339 SIEEQRRllqTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihtlqqqkttLTQKLQSLCKELDILQREQATIDTRTSA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 408 LQQEKQDLEQVTTDLQLTISELRQ-------QLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQV 480
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELcaaaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
....
gi 1907080929 481 LQEE 484
Cdd:TIGR00618 499 LQEE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-386 |
7.92e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 251 lLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAA-AERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 328
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLREKREALAElNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYL 662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907080929 329 DKEKARVDSMVRHQESLQAK---QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEqLQS 386
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEALYDEAEE-LES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-439 |
9.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 200 AQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 280 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQAK 348
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 349 QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcqlqaqqellqslqqekqDLEQVTTDLQLTISE 428
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------------------------ELEAEIASLERRKSN 437
|
250
....*....|.
gi 1907080929 429 LRQQLEELKER 439
Cdd:COG4913 438 IPARLLALRDA 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-490 |
1.65e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 245
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 246 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 325
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 326 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELL 405
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 406 QSLQQEKQDLEQVTtdlqltisELRQQLEELKERERLLVAFPDLHQPEEAQiqsssnvtQDMER--QVQANAI-RIQVLQ 482
Cdd:PRK02224 610 RLREKREALAELND--------ERRERLAEKRERKRELEAEFDEARIEEAR--------EDKERaeEYLEQVEeKLDELR 673
|
....*...
gi 1907080929 483 EENKRLQS 490
Cdd:PRK02224 674 EERDDLQA 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-501 |
1.81e-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: 43.98 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 316 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQ 395
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 396 CQLQAQQEL-------------------------LQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAfpdLH 450
Cdd:COG4942 97 AELEAQKEElaellralyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA---ER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907080929 451 QPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 501
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-373 |
2.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 167 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 246
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 247 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 324
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907080929 325 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 373
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
199-503 |
2.73e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEQ------GQRQRQTEEAERTLAKCE-------------HDRHQLLTETC-DL 258
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLADYQQALDVQQtraiqyQQAVQALEKARALCGLPDltpenaedylaafRAKEQQATEEVlEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 259 KTKVAVLEGDLKQQQKSIQAMEAKAqqleEEGERRAAAE--RQVQQLEEQVQLLAGRLdgasQQIRWASTELDKEKARVD 336
Cdd:COG3096 461 EQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQtaRELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQ 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 337 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqellqslqqekQDLE 416
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR------------------------QQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 417 QvttdlqltiseLRQQLEELKERE-RLLVAFPDLHQPEE---AQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSML 492
Cdd:COG3096 589 Q-----------LRARIKELAARApAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALE 657
|
330
....*....|.
gi 1907080929 493 TKIREVAQQGG 503
Cdd:COG3096 658 SQIERLSQPGG 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
175-382 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQ-LVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH------- 246
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereiee 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 247 ---DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGASQ 319
Cdd:TIGR02169 348 erkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080929 320 QI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 382
Cdd:TIGR02169 428 AIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-441 |
2.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 273 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 351
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQEKQDLEQVTtdlQLTISELRQ 431
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-----------------LIEEQLQELERIS---GLTAEEAKE 157
|
170
....*....|.
gi 1907080929 432 Q-LEELKERER 441
Cdd:PRK12704 158 IlLEKVEEEAR 168
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
202-509 |
3.80e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 202 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCEHDRH---QLLTETCDLKTKVAVLEGDLKQQQKSI 276
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 277 QAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQl 356
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 357 dclDQEREELRGSLDEAEAQRSELEEQLQSLQS--DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLE 434
Cdd:COG5185 419 ---DRQIEELQRQIEQATSSNEEVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVS 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080929 435 ELKERERLLVAfpdlhqPEEAQIQSSSN-VTQDMERQVQANAIRiqvlQEENKRLQSMLTKIREVAQQGGLKMVPQ 509
Cdd:COG5185 496 TLKATLEKLRA------KLERQLEGVRSkLDQVAESLKDFMRAR----GYAHILALENLIPASELIQASNAKTDGQ 561
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-506 |
4.73e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 257 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 336
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 337 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 416
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 417 QVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIR 496
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250
....*....|
gi 1907080929 497 EVAQQGGLKM 506
Cdd:COG4372 272 DTEEEELEIA 281
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-492 |
6.60e-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: 42.85 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 183 RLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQA---LQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 259
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 260 TKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDG-------ASQQIRWASTELDKEK 332
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 333 ARV----DSMVRHQEsLQAKQRTLLQQLD-CLDQER------------------EELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 306 TELedtlDTTAAQQE-LRSKREQEVTELKkALEEETrsheaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 390 DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPD-----LHQPE----------- 453
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvsslLNEAEgkniklskdvs 464
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907080929 454 --EAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSML 492
Cdd:pfam01576 465 slESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQL 505
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
337-443 |
8.44e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 337 SMVR-HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQR-SELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 414
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*....
gi 1907080929 415 LEQVTTDLQLTISELRQQLEELKERERLL 443
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-490 |
1.04e-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: 42.36 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 312 GRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAkqrtllqQLDCLDQEREELRGSLDE-------AEAQRSELEEQL 384
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDElsqelsdASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 385 QSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPE---------EA 455
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEE 805
|
170 180 190
....*....|....*....|....*....|....*
gi 1907080929 456 QIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQS 490
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-512 |
1.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 272 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 351
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQ-----LTI 426
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 427 SELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKM 506
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
....*.
gi 1907080929 507 VPQGQL 512
Cdd:COG4372 259 EIEELE 264
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
215-389 |
1.39e-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: 41.70 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 215 QVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGdlkQQQKSIQAMEAKAQQLEEEGERRA 294
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ---AKQDSEHKRKKLEGQLQELQARLS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 295 AAERQVQQLEEQVQLLAGRLDGASQQIRWA---STELDKEKARVDSMVRH-QESLQAKQRTLLQ---QLDCLDQEREELR 367
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAegkNIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERNSLQ 502
|
170 180
....*....|....*....|..
gi 1907080929 368 GSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
354-501 |
1.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 354 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEqcqlqaqqellqslqqekQDLEQVTTDlQLTISELRQQL 433
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL------------------QRLAEYSWD-EIDVASAEREI 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080929 434 EELK-ERERLLVAFPDLHQPEEaQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 501
Cdd:COG4913 671 AELEaELERLDASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-501 |
2.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 353 LQQLDCLDQEREELRGSLDE---AEAQRSELEEQLQSLQSDREQEQCQLQA--QQELLQSLQQEKQDLEQVTTDLQLTIS 427
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907080929 428 ELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSN-VTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 501
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-497 |
2.63e-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: 40.82 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 330 KEKAR--VDSMVRHQESLQAKQRTLLQQLDCLDQERE------ELRGSLDEAEA-----QRSELEEQLQSLQSDReqeqc 396
Cdd:TIGR02169 172 KEKALeeLEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGyellkEKEALERQKEAIERQL----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 397 qlqaqqellqslqqekQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPDLHQPEEAQIQS-----SSNVTQdMERQ 470
Cdd:TIGR02169 247 ----------------ASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIKDLGEEEQLRVKEkigelEAEIAS-LERS 309
|
170 180
....*....|....*....|....*..
gi 1907080929 471 VQANAIRIQVLQEENKRLQSMLTKIRE 497
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLA 336
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-501 |
2.96e-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: 40.77 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 254
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGErraaaerqvQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAr 334
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQlqslqsdreqeqcqlqaqqellqslqqeKQD 414
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------------------------KKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 415 LEQVTTDLQLTISELRQQLEEL------KERErllvafpdLHQPEEAQIQSSSNVTQD-MERQVQANAIRIQVLQEENKR 487
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLesekkeKESK--------ISDLEDELNKDDFELKKEnLEKEIDEKNKEIEELKQTQKS 579
|
330
....*....|....
gi 1907080929 488 LQSMLTKIREVAQQ 501
Cdd:TIGR04523 580 LKKKQEEKQELIDQ 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-501 |
3.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 358 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR--------------EQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQ 423
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080929 424 LTISELRQQLEELkeRERLLVAFPDLHQPEEaQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 501
Cdd:TIGR02168 754 KELTELEAEIEEL--EERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-388 |
3.48e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 181 LTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLR-KQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 259
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 260 TKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTELDKEKARVDSMV 339
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 340 RHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELRGSLDEAEAQRS 378
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVLKRLDELKEKRA 996
|
250
....*....|
gi 1907080929 379 ELEEQLQSLQ 388
Cdd:TIGR02169 997 KLEEERKAIL 1006
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
314-583 |
4.43e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 314 LDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQL--------- 384
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 385 --------------------------------------QSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTI 426
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 427 SELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKM 506
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080929 507 VPQGQLWSPPYKGIQGATPPAQAQSAFSGLTGRRQSPGSRTSSTGRTHPGGLRTSPSRQPGGLPSKFSLGDGSHSAS 583
Cdd:COG3883 258 AAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGS 334
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-445 |
4.53e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 174 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 246
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 247 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 322
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 323 WASTELDKEKARVDSMVRHQESLQAKQRTLlqqldclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQ 402
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907080929 403 ELLQSLQQEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA 445
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVE---EAEALLEA 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-502 |
4.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 287 EEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL 366
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 367 RGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER-ERLLVA 445
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080929 446 FPDLHQ-PEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQG 502
Cdd:COG4372 166 LAALEQeLQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-465 |
5.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 198 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 275
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 276 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 353
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 354 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqslqqEKQDLEQVTTDLQLTISELRQQL 433
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQA---------------------QLAQLEARLAELPELEAELRRLE 357
|
250 260 270
....*....|....*....|....*....|..
gi 1907080929 434 EELKERERLLVAFpdLHQPEEAQIQSSSNVTQ 465
Cdd:COG3206 358 REVEVARELYESL--LQRLEEARLAEALTVGN 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-388 |
8.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqteeaertlakcehDRHQLLT 253
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----------------------QLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 254 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWAsteldkEKA 333
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE--------------ELEELLEQLSLA------TEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080929 334 RVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 388
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-289 |
8.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 255
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 1907080929 256 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 289
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
311-388 |
8.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 8.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080929 311 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQ 388
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQ 561
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
258-497 |
8.58e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 258 LKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTEldKEKARVDS 337
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK--ALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 338 MVRHQESLQAKQRTLLQQL-DCLDQEREELRGSLDEAEAQRSELEEQL--QSLQSDREQEQCQLQAQQELLQSLQQEKQD 414
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHqAWLEEQKEQKREARTEKQAYWQVVEGALdaQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 415 L------EQVTTDLQLTISELRQQLEELKERERLLVAFPD-------LHQP----EEAQIQSS-SNVTQDMERQVQANAI 476
Cdd:pfam12128 760 LaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwlQRRPrlatQLSNIERAiSELQQQLARLIADTKL 839
|
250 260
....*....|....*....|.
gi 1907080929 477 RIQVLQEENKRLQSMLTKIRE 497
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSE 860
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-389 |
9.13e-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: 39.39 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 191 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 268
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 269 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 343
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907080929 344 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-391 |
9.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 200 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080929 280 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQ-ESLQAKQRTLLQQLDC 358
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 1907080929 359 LDQEREELRgslDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4717 211 LEEELEEAQ---EELEELEEELEQLENELEAAA 240
|
|
| |
