|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-490 |
1.58e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEHDRHQ 250
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 251 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQLEEQVqllagRLDGASQQIRWASTEL 328
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLER-----RIAATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 329 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKqdLE 408
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK--LA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 409 QVTTDLQLTISELRQQLEELKERERLLvafPDLHQPEEAQIQSSSNVTQD----MERQVQA----NAIRIQVLQEENKRL 480
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLT---LEEAEALENKIEDDEEEARRrlkrLENKIKElgpvNLAAIEEYEELKERY 1002
|
330
....*....|
gi 148708516 481 QSMLTKIREV 490
Cdd:TIGR02168 1003 DFLTAQKEDL 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-457 |
2.03e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH---DRHQLLTETCDLKTKVAVLEGDLKQQQK 274
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 275 SIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmVRHQESLQAKQRTLLQ 354
Cdd:COG1196 338 ELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 355 QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEK-QDLEQVTTDLQLTISELRQQLEELKERER 433
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELlAELLEEAALLEAALAELLEELAEAAARLL 494
|
250 260
....*....|....*....|....
gi 148708516 434 LLVAFPDLHQPEEAQIQSSSNVTQ 457
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-501 |
9.72e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 180 DLTRLNKHVGALTQLVGPLRAQLEDAE------GQKDGLRKQVSKLE-QALQQEQGQRQRQTEEAERTLAKCEHDRHQLL 252
Cdd:COG1196 187 NLERLEDILGELERQLEPLERQAEKAEryrelkEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 253 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 328
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 329 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQS-----DREQEQCQLQAQQE 403
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeealLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 404 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSM 483
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330
....*....|....*...
gi 148708516 484 LTKIREVAQQGGLKMVPQ 501
Cdd:COG1196 507 LEGVKAALLLAGLRGLAG 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-481 |
1.87e-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: 67.39 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 180 DLTRLNKHVGALTQLVGPLRAQLEDAEGQKDgLRKQVSKLE--------QALQQEQGQRQRQTEEAERTLAKCEHDRHQL 251
Cdd:TIGR02168 187 NLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 252 LTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTE 327
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 328 LDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAE-------AQRSELEEQLQSLQSDREQEQCQLQA 400
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiaslnNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 401 QQEKQDLEQVtTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRL 480
Cdd:TIGR02168 426 LLKKLEEAEL-KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
.
gi 148708516 481 Q 481
Cdd:TIGR02168 505 S 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-431 |
3.29e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 191 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT----------EEAERTLAKCEHDRHQLLTETCDLKT 260
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisalrkdlARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 261 KVAVLEGDLKQQQKSIQAMEAKAQQLEEE---GERRAAAERQvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDS 337
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALRE-------------ALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 338 MVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqEQCQLQAQQEKQDLEQVTTDLQ-- 415
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER--ASLEEALALLRSELEELSEELRel 906
|
250
....*....|....*..
gi 148708516 416 -LTISELRQQLEELKER 431
Cdd:TIGR02168 907 eSKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-501 |
7.96e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 268 DLKQQQKSIQAmEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIrwasTELDKEKARVDsmvRHQESLQA 347
Cdd:TIGR02168 217 ELKAELRELEL-ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELE---EEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 348 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEK-QDLEQVTTDLQLTISELRQQLE 426
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKlEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148708516 427 ELKERERLLvafpdlhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKMVPQ 501
Cdd:TIGR02168 369 ELESRLEEL----------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-486 |
9.75e-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: 61.62 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 278 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 344
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 345 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEK------- 404
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKieeleaq 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 405 -QDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSM 483
Cdd:TIGR02169 912 iEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
...
gi 148708516 484 LTK 486
Cdd:TIGR02169 992 KEK 994
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-489 |
1.48e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 257 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 336
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 337 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD---------------REQEQCQLQAQ 401
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalrealdelraelTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 402 QEKQDLEQVTTDLQLTISELRQQLEELKER-ERLLVAFPDLHQPE---EAQIQSSSNVTQDMERQVQANAIRIQVLQEEN 477
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDiESLAAEIEELEELIeelESELEALLNERASLEEALALLRSELEELSEEL 903
|
250
....*....|..
gi 148708516 478 KRLQSMLTKIRE 489
Cdd:TIGR02168 904 RELESKRSELRR 915
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-391 |
2.20e-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: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 254
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 334
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148708516 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-433 |
1.02e-08 |
|
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: 58.54 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 274
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 275 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 339
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 340 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQ-----SDREQEQCQLQAQQEKQDLEQVTTDL 414
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikkQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 148708516 415 QLT---ISELRQQLEELKERER 433
Cdd:TIGR02169 479 DRVekeLSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-498 |
1.62e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 199 RAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKAL-----------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 279 MEAKAQQLEEEgerRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDC 358
Cdd:TIGR02168 745 LEERIAQLSKE---LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 359 LDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqekQDLEQVTTDLQLTISELRQQLEEL-KERERLLVA 437
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDI-------------ESLAAEIEELEELIEELESELEALlNERASLEEA 888
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708516 438 fpdLHQPEEAQIQSSSNVtQDMERQVQAnairiqvLQEENKRLQSMLTKIREvaQQGGLKM 498
Cdd:TIGR02168 889 ---LALLRSELEELSEEL-RELESKRSE-------LRRELEELREKLAQLEL--RLEGLEV 936
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-493 |
1.97e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEhdrhQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD----DLEERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 279 MEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGASQQIrwasTELDKEKARVDSMVRHQESLQA------- 347
Cdd:PRK02224 382 RREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELRERE----AELEATLRTARERVEEAEALLEagkcpec 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 348 ----KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQDLEQVTTDLQLTISELRQ 423
Cdd:PRK02224 458 gqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708516 424 QLEELKERERLLVAFPDLH----QPEEAQIQSSSNVTQDMERQVQANAIRIQVLQeenkRLQSMLTKIREVAQQ 493
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKreaaAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAIADAEDE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-391 |
3.14e-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: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDLTRLNKHVGALTQLvgplRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqteeAERTLAKCEHDRHQLlt 253
Cdd:COG4913 247 AREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLWFAQRRLEL-------------LEAELEELRAELARL-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 254 etcdlKTKVAVLEGDLKQQQKSIQamEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEka 333
Cdd:COG4913 308 -----EAELERLEARLDALREELD--ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS-- 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148708516 334 rvdsmvrhQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4913 379 --------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-448 |
3.17e-07 |
|
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: 52.84 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 217 SKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEgerraaA 296
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE------I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 297 ERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQ 376
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148708516 377 RSELEEQLQSLQSDReqeqcqLQAQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQ 448
Cdd:COG4942 173 RAELEALLAELEEER------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-497 |
5.74e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 285 QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQERE 364
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 365 ELRGSLDEAEAQRSELEEQLQSLQS------DREQEQCQLQAQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLvaf 438
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEalndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--- 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148708516 439 PDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREvaQQGGLK 497
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES--RLGDLK 888
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-481 |
2.02e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 250
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 251 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 330
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 331 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlQAQQEKQDLEQV 410
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE---------KEMNLRDELESV 553
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708516 411 TTDLQLTISELRQQLEELKERERllvAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQ 481
Cdd:pfam05483 554 REEFIQKGDEVKCKLDKSEENAR---SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-482 |
2.83e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 245
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 246 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 325
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 326 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQ 405
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 406 DLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQiqsssnvtQDMER--QVQANAI-RIQVLQEENKRLQS 482
Cdd:PRK02224 610 RLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAR--------EDKERaeEYLEQVEeKLDELREERDDLQA 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-431 |
3.26e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 179 KDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKcehdrhqlltetcdL 258
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-----------AALEAELAE--------------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 259 KTKVAVLEGDLKQQQKSIQAMEAKAQQLeeeGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRwasteldkekARVDSM 338
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----------EQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 339 VRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLqaqqekQDLEQVTTDLQLTI 418
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL------AELQQEAEELEALI 229
|
250
....*....|...
gi 148708516 419 SELRQQLEELKER 431
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-489 |
3.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 273 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDkekarVDSMVRHQESLQAKqrtl 352
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAE---- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 353 LQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqekqdleqvtTDLQLTISELRQQLEELKERE 432
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI--------------------GRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148708516 433 RLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQAN-AIRIQVLQEENKRLQSMLTKIRE 489
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERAMR 794
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-489 |
8.98e-06 |
|
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: 48.86 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 254
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 255 TCDLKTKVAVLEGDLKQQQKS-------IQAMEAKAQQLEEEGER------------------RAAAERQVQQLEEQVQL 309
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLnqqkdeqIKKLQQEKELLEKEIERlketiiknnseikdltnqDSVKELIIKNLDNTRES 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 310 LAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 390 DreqeQCQLQAQQEKQDLEQVTTDLQLTISELRQ----------QLEEL---KERERLlvafpDLHQPEEAQIQSSSNVT 456
Cdd:TIGR04523 546 E----LNKDDFELKKENLEKEIDEKNKEIEELKQtqkslkkkqeEKQELidqKEKEKK-----DLIKEIEEKEKKISSLE 616
|
330 340 350
....*....|....*....|....*....|...
gi 148708516 457 QDMERqvqanairiqvLQEENKRLQSMLTKIRE 489
Cdd:TIGR04523 617 KELEK-----------AKKENEKLSSIIKNIKS 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-435 |
9.38e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 251 LLTETCDLKTKVAVLEgdlkqqqksiqAMEAKAQQLEEEGERRAA-AERQVQQLEeqvqllagRLDGASQQIRWASTELD 329
Cdd:PRK02224 584 LKERIESLERIRTLLA-----------AIADAEDEIERLREKREAlAELNDERRE--------RLAEKRERKRELEAEFD 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 330 keKARVdsmvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQDLEQ 409
Cdd:PRK02224 645 --EARI-------EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYD 715
|
250 260 270
....*....|....*....|....*....|.
gi 148708516 410 VTTDLQLTI----SELRQQ-LEELkerERLL 435
Cdd:PRK02224 716 EAEELESMYgdlrAELRQRnVETL---ERML 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-431 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 200 AQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 280 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKekarvdsmvrhQESLQAKQRTLLQQLD-C 358
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-----------RERRRARLEALLAALGlP 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708516 359 LDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEqcqlqaqqeKQDLEQVTTDLQltisELRQQLEELKER 431
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEA---------EAALRDLRRELR----ELEAEIASLERR 434
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
192-493 |
1.52e-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: 48.04 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 192 TQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQ 271
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 272 QQ--KSIQAMEAKAQQLEEEGERrAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQ 349
Cdd:TIGR00618 259 QQllKQLRARIEELRAQEAVLEE-TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 350 RTLLQQ---LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqQEKQDLEQVTTDLQLTISELRQQLE 426
Cdd:TIGR00618 338 SSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH----------TLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 427 ELKERERLLVAFPDLHQP---EEAQIQSSSnvtQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQlahAKKQQELQQ---RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
410-571 |
1.83e-05 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 47.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 410 VTTDLQLTISELRQQLEELKERerllvafpdlhqpeeaqiqsssnvTQDMERQVQANAIRIQVLQEENKRLQSMLTKIRE 489
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRE------------------------LDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 490 VAQQGGLKMVPQGQLWSP-----PYKGIQGATPPAQAQSAFSGLTGRrqSPGSrtsstGRTHPGGLRTSPSRQPGGLPSK 564
Cdd:PRK13729 126 NPVTATGEPVPQMPASPPgpegePQPGNTPVSFPPQGSVAVPPPTAF--YPGN-----GVTPPPQVTYQSVPVPNRIQRK 198
|
....*...
gi 148708516 565 -FSLGDGS 571
Cdd:PRK13729 199 tFTYNEGK 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-493 |
2.76e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 316 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeq 395
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 396 cqlqaqqekqdleqvttdlqltISELRQQLEELKER--ERLLVAFPDLHQPEEAQIQSSSNVTQD------MERQVQANA 467
Cdd:COG4942 92 ----------------------IAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDFLDAvrrlqyLKYLAPARR 149
|
170 180
....*....|....*....|....*.
gi 148708516 468 IRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAE 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-390 |
2.95e-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: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 279 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 353
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 148708516 354 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 390
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
199-495 |
3.02e-05 |
|
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: 47.25 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEQ------GQRQRQTEEAERTLAKCE-------------HDRHQLLTETC-DL 258
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLADYQQALDVQQtraiqyQQAVQALEKARALCGLPDltpenaedylaafRAKEQQATEEVlEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 259 KTKVAVLEGDLKQQQKSIQAMEAKAqqleEEGERRAAAE--RQVQQLEEQVQLLAGRLdgasQQIRWASTELDKEKARVD 336
Cdd:COG3096 461 EQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQtaRELLRRYRSQQALAQRL----QQLRAQLAELEQRLRQQQ 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 337 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqekQDLEQvttdlql 416
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR----------------QQLEQ------- 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 417 tiseLRQQLEELKERE-RLLVAFPDLHQPEE---AQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQ 492
Cdd:COG3096 590 ----LRARIKELAARApAWLAAQDALERLREqsgEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
...
gi 148708516 493 QGG 495
Cdd:COG3096 666 PGG 668
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-433 |
3.16e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 273 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 351
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlQAQQEKQDLEQVTtdlQLTISELRQQ-LEELKE 430
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE---------LIEEQLQELERIS---GLTAEEAKEIlLEKVEE 165
|
...
gi 148708516 431 RER 433
Cdd:PRK12704 166 EAR 168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
265-493 |
4.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 265 LEGDLKQQQKSIQAMEAKAQQLEEEgerRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQES 344
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 345 LQAKQRTLLQQLDCLDQER--EELRGSLDEAEAQRS---------ELEEQLQSLQSDReqeqcqlqaqqekQDLEQVTTD 413
Cdd:COG4942 102 QKEELAELLRALYRLGRQPplALLLSPEDFLDAVRRlqylkylapARREQAEELRADL-------------AELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 414 LQLTISELRQQLEELKERERLLvafpdlhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:COG4942 169 LEAERAELEALLAELEEERAAL----------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-494 |
4.92e-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: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 268 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 347
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 348 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqeKQDLEQVTTDLQLTISELRQQLEE 427
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------------LEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708516 428 LKERERLLvafpDLHQPEEA--------QIQSSSNVTQDMERQVQANAIRIQV-LQEENKRLQSMLTKIREVAQQG 494
Cdd:COG4913 364 LEALLAAL----GLPLPASAeefaalraEAAALLEALEEELEALEEALAEAEAaLRDLRRELRELEAEIASLERRK 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-493 |
5.84e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 342 QESLQAKQRTLLQQLDCLDQEREELRGSLDEAEA-----------------------QRSELEEQLQSLQSDREQEQCQL 398
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglvdlseeaklllqQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 399 QAQQEKQDLEQVTTDLQL---TISELRQQLEELK-ERERLLVAFPDLHqPE----EAQIQS--------SSNVTQDMERQ 462
Cdd:COG3206 243 AALRAQLGSGPDALPELLqspVIQQLRAQLAELEaELAELSARYTPNH-PDvialRAQIAAlraqlqqeAQRILASLEAE 321
|
170 180 190
....*....|....*....|....*....|.
gi 148708516 463 VQANAIRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
205-571 |
1.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 205 AEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEhdrhqlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQ 284
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-----------ELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 285 QLEEEGERRAAA--ERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQE 362
Cdd:COG3883 83 ERREELGERARAlyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 363 REELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqLQAQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFpdlh 442
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEE------AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 443 QPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGGLKMVPQGQLWSPPYKGIQGATPPAQAQ 522
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 148708516 523 SAFSGLTGRRQSPGSRTSSTGRTHPGGLRTSPSRQPGGLPSKFSLGDGS 571
Cdd:COG3883 313 VGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSG 361
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-493 |
1.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 330 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcQLQAQQEKQDLEQ 409
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----------LLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 410 VTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSN-VTQDMERQVQANAIRIQVLQEENKRLQSMLTKIR 488
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
....*
gi 148708516 489 EVAQQ 493
Cdd:COG4717 220 EELEE 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
257-575 |
2.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 257 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEgerRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 336
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQA--------------EIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 337 SMVRHQ----------------ESLQakqrTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqCQLQA 400
Cdd:COG3883 90 ERARALyrsggsvsyldvllgsESFS----DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA------KLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 401 QQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRL 480
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 481 QSMLTKIREVAQQGGLKMVPQGQLWSPPYKGIQGATPPAQAQSAFSGLTGRRQSPGSRTSSTGRTHPGGLRTSPSRQPGG 560
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGA 319
|
330
....*....|....*
gi 148708516 561 LPSKFSLGDGSHSAS 575
Cdd:COG3883 320 GAVVGGASAGGGGGS 334
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
354-493 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 354 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEqcqlqaqqekQDLEQVTTDlQLTISELRQQLEELK-ERE 432
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD-EIDVASAEREIAELEaELE 678
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708516 433 RLLVAFPDLHQPEEaQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:COG4913 679 RLDASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-373 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 167 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 246
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 247 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 324
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148708516 325 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 373
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-429 |
2.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 200 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 280 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQEslqakqRTLLQQLDCL 359
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEEL------QDLAEELEEL 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 360 DQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqekqdleqvttdlQLTISELRQQLEELK 429
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLEN-------------------------ELEAAALEERLKEAR 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
175-382 |
2.69e-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: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQ-LVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH------- 246
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereiee 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 247 ---DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGASQ 319
Cdd:TIGR02169 348 erkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708516 320 QI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 382
Cdd:TIGR02169 428 AIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-489 |
2.91e-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: 43.90 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 330 KEKAR--VDSMVRHQESLQAKQRTLLQQLDCLDQERE------ELRGSLDEAEA-----QRSELEEQLQSLQSDReqeqc 396
Cdd:TIGR02169 172 KEKALeeLEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGyellkEKEALERQKEAIERQL----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 397 qlqaqqekQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPDLHQPEEAQIQS-----SSNVTQdMERQVQANAIRI 470
Cdd:TIGR02169 247 --------ASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIKDLGEEEQLRVKEkigelEAEIAS-LERSIAEKEREL 317
|
170
....*....|....*....
gi 148708516 471 QVLQEENKRLQSMLTKIRE 489
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLA 336
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-389 |
3.17e-04 |
|
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: 43.89 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 254
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----------ESLAAEIEELEELIEELESE 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 255 TCDLKTKVAVLEGDLKQQQKsiqAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRW--------AST 326
Cdd:TIGR02168 875 LEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlseeYSL 951
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 327 ELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-------QEREELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
258-500 |
3.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 258 LKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDS 337
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ---------------LSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 338 MVRHQESLQAKQ---------RTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqQEKQDLE 408
Cdd:COG3206 245 LRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA------------QLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 409 QVTTDLQLTISELRQQLEELKERERLLvafpdlhqpeEAQIQSSSNVTQ---DMERQVQANairiqvlqeeNKRLQSMLT 485
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQL----------EARLAELPELEAelrRLEREVEVA----------RELYESLLQ 372
|
250
....*....|....*
gi 148708516 486 KIREVAQQGGLKMVP 500
Cdd:COG3206 373 RLEEARLAEALTVGN 387
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-432 |
4.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 272 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 351
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEK-QDLEQVTTDLQLTISELRQQLEELKE 430
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEElKELEEQLESLQEELAALEQELQALSE 178
|
..
gi 148708516 431 RE 432
Cdd:COG4372 179 AE 180
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-504 |
5.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 257 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 336
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 337 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqekQDLEQVTTDLQ- 415
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ----------------EELAALEQELQa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 416 LTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQGG 495
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
....*....
gi 148708516 496 LKMVPQGQL 504
Cdd:COG4372 256 ILKEIEELE 264
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-457 |
6.03e-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: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 198 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 275
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 276 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 353
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 354 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqEKQDLEQVTTDLQLTISELRQQLEELKERER 433
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQA-------------QLAQLEARLAELPELEAELRRLEREVEVARE 365
|
250 260
....*....|....*....|....
gi 148708516 434 LLVAFpdLHQPEEAQIQSSSNVTQ 457
Cdd:COG3206 366 LYESL--LQRLEEARLAEALTVGN 387
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
202-501 |
9.62e-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: 42.25 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 202 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCEHDRH---QLLTETCDLKTKVAVLEGDLKQQQKSI 276
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 277 QAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQl 356
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 357 dclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKqdleQVTTDLQLTISELRQQLEELKER----E 432
Cdd:COG5185 419 ---DRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS----RLEEAYDEINRSVRSKKEDLNEEltqiE 491
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 433 RLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQE-ENKRLQSMLTKIREVAQQGGLKMVPQ 501
Cdd:COG5185 492 SRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGyAHILALENLIPASELIQASNAKTDGQ 561
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
241-438 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 241 LAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQ 320
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-----------------RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 321 IRWASTEldKEkarVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLqsdreqeqcqlqa 400
Cdd:COG1579 82 LGNVRNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148708516 401 qqeKQDLEQVTTDLQLTISELRQQLEELKER--ERLLVAF 438
Cdd:COG1579 144 ---KAELDEELAELEAELEELEAEREELAAKipPELLALY 180
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
193-494 |
2.17e-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: 41.36 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 193 QLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCehdRHQLLTETCDLKTKVAVLEGDL--- 269
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELNGELsaa 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 270 ----KQQQKSIQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllagrldgASQQIRWaSTELDKEKARVDSMVRHQESL 345
Cdd:pfam12128 314 daavAKDRSELEALEDQHGAFLDADIETAAAD-------------------QEQLPSW-QSELENLEERLKALTGKHQDV 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 346 QAKQRTLLQQLDC--------LDQEREELRgslDEAEAQRSELEEQLQSLQSdreqeqcqlqaqQEKQDLEQVTTDLQLT 417
Cdd:pfam12128 374 TAKYNRRRSKIKEqnnrdiagIKDKLAKIR---EARDRQLAVAEDDLQALES------------ELREQLEAGKLEFNEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 418 ISELRQQLEELKERERLLVAFPDL-----------HQPEEAQIQSSSNVTQDMERQVQANAIRIQV---LQEENKRLQSM 483
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQATATPELllqlenfderiERAREEQEAANAEVERLQSELRQARKRRDQAseaLRQASRRLEER 518
|
330
....*....|.
gi 148708516 484 LTKIREVAQQG 494
Cdd:pfam12128 519 QSALDELELQL 529
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
258-489 |
2.25e-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: 41.36 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 258 LKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTE-LDKEKARVD 336
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 337 SMVR------------HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQ--------RSELEEQLQSLQSDREQEQC 396
Cdd:pfam12128 682 ERLNsleaqlkqldkkHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALlkaaiaarRSGAKAELKALETWYKRDLA 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 397 QLQAQQEK-QDLEQVTTDLQLTISELRQQLEELKE-----RERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRI 470
Cdd:pfam12128 762 SLGVDPDViAKLKREIRTLERKIERIAVRRQEVLRyfdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR 841
|
250
....*....|....*....
gi 148708516 471 QVLQEENKRLQSMLTKIRE 489
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSE 860
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
311-480 |
2.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 311 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 390 DReqeqcqlqaQQEKQDLEQvttdlqltisELRQQLEELKErerllvafpdlhqpEEAQIQSSSNVTQDMerqvQANAIR 469
Cdd:PRK00409 563 EE---------DKLLEEAEK----------EAQQAIKEAKK--------------EADEIIKELRQLQKG----GYASVK 605
|
170
....*....|.
gi 148708516 470 IQVLQEENKRL 480
Cdd:PRK00409 606 AHELIEARKRL 616
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-493 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 358 CLDQEREELRGSLDEAEAQRSELEEQLQSL-QSDREQEQCQLQAQQEKQDLEQVTTDLQLTISELRQQLEELKER----E 432
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlS 753
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708516 433 RLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREVAQQ 493
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
176-484 |
2.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 176 EQSKDLTRL-NKHVGALTQLVGPL------RAQLEDAEGQKDG----LRKQVSKLEQALQQEQGQRQRQTEEAERTLAKC 244
Cdd:pfam01576 173 EKAKSLSKLkNKHEAMISDLEERLkkeekgRQELEKAKRKLEGestdLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 245 EH---DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE------------------GERRAAAERQVQQL 303
Cdd:pfam01576 253 EEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElealkteledtldttaaqQELRSKREQEVTEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 304 EEQVQLLAGRLDGASQQIRWAST--------ELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQER------------ 363
Cdd:pfam01576 333 KKALEEETRSHEAQLQEMRQKHTqaleelteQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKqdsehkrkkleg 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 364 --EELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEK------------------QDLEQVTTDLQLTISE--- 420
Cdd:pfam01576 413 qlQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKniklskdvsslesqlqdtQELLQEETRQKLNLSTrlr 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148708516 421 --------LRQQLEELKERERLLvafpdlhqpeEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSML 484
Cdd:pfam01576 493 qledernsLQEQLEEEEEAKRNV----------ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
174-482 |
2.77e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDLTRLNKHvgaltqlvgpLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKCEHDRHQ 250
Cdd:pfam01576 648 ALEAKEELERTNKQ----------LRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 251 LLTETCDLKTKvavLEGDL-----------KQQQKSIQAMEAkaqQLEEEGERRAAAerqvqqleeqvqlLAGRldgasq 319
Cdd:pfam01576 718 LEVNMQALKAQ---FERDLqardeqgeekrRQLVKQVRELEA---ELEDERKQRAQA-------------VAAK------ 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 320 qiRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlq 399
Cdd:pfam01576 773 --KKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA---------- 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 400 aqqekqDLEQVTTDLQlTISELRQQLEElkERERLlvafpdlhQPEEAQIQSSSNVTQDMERQVQAnaiRIQVLQEENKR 479
Cdd:pfam01576 841 ------ELLQLQEDLA-ASERARRQAQQ--ERDEL--------ADEIASGASGKSALQDEKRRLEA---RIAQLEEELEE 900
|
...
gi 148708516 480 LQS 482
Cdd:pfam01576 901 EQS 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
265-431 |
2.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 265 LEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQES 344
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 345 LQAKQR---TLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQDLEQVTTDLQLTISEL 421
Cdd:PRK03918 240 IEELEKeleSLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170
....*....|
gi 148708516 422 RQQLEELKER 431
Cdd:PRK03918 320 EEEINGIEER 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-388 |
3.42e-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: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 181 LTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLR-KQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 259
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 260 TKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTELDKEKARVDSMV 339
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 340 RHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELRGSLDEAEAQRS 378
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVLKRLDELKEKRA 996
|
250
....*....|
gi 148708516 379 ELEEQLQSLQ 388
Cdd:TIGR02169 997 KLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-441 |
3.75e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqTEEAERTLAKCEHDRHQLLTE 254
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQL--LAGRLDGASQQIRWASTELDKEK 332
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 333 --ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRS-------ELEEQlqslqsdreqeQCQLQAQQE 403
Cdd:PRK03918 389 leKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrELTEE-----------HRKELLEEY 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 148708516 404 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDL 441
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-431 |
3.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 195 VGPLRAQLEDAEGQKDGLRK---QVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAvlegDLKQ 271
Cdd:COG4913 663 VASAEREIAELEAELERLDAssdDLAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELE----QAEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 272 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLeeqvqllagrLDGASQQIR-WASTELDKEKARVDsmvRHQESLQAKQR 350
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAAL----------GDAVERELReNLEERIDALRARLN---RAEEELERAMR 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 351 TLLQQLDCldqEREELRGSLDEAEaqrsELEEQLQSLQSDREQEQCQLQAQQEKQDLEQVTTDLQltiSELRQQLEELKE 430
Cdd:COG4913 795 AFNREWPA---ETADLDADLESLP----EYLALLDRLEEDGLPEYEERFKELLNENSIEFVADLL---SKLRRAIREIKE 864
|
.
gi 148708516 431 R 431
Cdd:COG4913 865 R 865
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
342-489 |
4.16e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 342 QESLQAKQRTLLQQL----DCLD------QEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlQAQQEKQDLEQVT 411
Cdd:PRK11281 51 QKLLEAEDKLVQQDLeqtlALLDkidrqkEETEQLKQQLAQAPAKLRQAQAELEALKDD--------NDEETRETLSTLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 412 -TDLQLTISELRQQLEELkeRERLLVAFPDL----HQPEEAQIQSSSNVTQDME----------RQVQANAIRIQVLQEE 476
Cdd:PRK11281 123 lRQLESRLAQTLDQLQNA--QNDLAEYNSQLvslqTQPERAQAALYANSQRLQQirnllkggkvGGKALRPSQRVLLQAE 200
|
170 180 190
....*....|....*....|....*....|
gi 148708516 477 -----------------NKRLQSMLTKIRE 489
Cdd:PRK11281 201 qallnaqndlqrkslegNTQLQDLLQKQRD 230
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
340-474 |
4.47e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 340 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEqcqlqaqqekqdlEQVTTDLQLTIS 419
Cdd:PRK09039 74 QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE-------------KQVSARALAQVE 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 148708516 420 ELRQQLEELKERerlLVAFPDLHQPEEAQIQSSSNVTQDMERQVQ-ANAIRIQVLQ 474
Cdd:PRK09039 141 LLNQQIAALRRQ---LAALEAALDASEKRDRESQAKIADLGRRLNvALAQRVQELN 193
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
343-435 |
5.03e-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: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 343 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQqekQDLEQVTTDLQLTISELR 422
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARL---KVLEKELKDLKWEHEVLE 112
|
90
....*....|....
gi 148708516 423 QQLEEL-KERERLL 435
Cdd:pfam13851 113 QRFEKVeRERDELY 126
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
197-485 |
6.87e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.40 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 197 PLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTE--EAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQ- 273
Cdd:PRK10246 423 PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAalNEMRQRYKEKTQQLADVKTICEQEARIKDLEAQRAQLQa 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 274 ---------------KSIQAMEAKAQQLeeegeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTEldkekarVDSM 338
Cdd:PRK10246 503 gqpcplcgstshpavEAYQALEPGVNQS-----RLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESE-------AQSL 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 339 VRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEaqrsELEEQLQSLqsdreqeqcqlqaqQEKQDLEQVTTDLQLTI 418
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQE----EHERQLRLL--------------SQRHELQGQIAAHNQQI 632
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708516 419 SELRQQLEELKERERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLT 485
Cdd:PRK10246 633 IQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLE 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-437 |
7.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 246
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 247 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 322
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 323 WASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR-EQEQCQLQAQ 401
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLgNAEDFLEELR 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 148708516 402 QEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA 437
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVE---EAEALLEA 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-388 |
7.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqteeaertlakcehDRHQLLT 253
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----------------------QLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 254 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWAsteldkEKA 333
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE--------------ELEELLEQLSLA------TEE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148708516 334 RVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 388
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-289 |
7.92e-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: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 255
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 148708516 256 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 289
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-446 |
8.30e-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: 39.18 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 193 QLVGPLRAQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERtLAKCEHDR---HQLLTETCDLKTKVAVLEGDL 269
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRA-----RKAAPLAAHIKA-VTQIEQQAqriHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 270 KQQQKSIQAMEAKAQQLEEEGERRAAAerqvqqleeqVQLLAGRLDGASQQIrwasteldkekarvdSMVRHQESLQAKQ 349
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHIRDA----------HEVATSIREISCQQH---------------TLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 350 RTLLQQLDCLDQEREELRGSLDEAEAQRSELE-EQLQSLQSDREQEQCQLQAQQEKQDLEQVTTDLQLTISELRQQLEEL 428
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
250
....*....|....*...
gi 148708516 429 KERERLLVAFPDLHQPEE 446
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQET 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
176-484 |
8.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 255
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 256 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAER------------------------------------- 298
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlfl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 299 ----------QVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELrg 368
Cdd:COG4717 282 vlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 369 sldEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQDLEQVttDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQ 448
Cdd:COG4717 360 ---EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ--ELKEELEELEEQLEELLGELEELLEALDEEELEEEL 434
|
330 340 350
....*....|....*....|....*....|....*.
gi 148708516 449 iqsssnvtQDMERQVQANAIRIQVLQEENKRLQSML 484
Cdd:COG4717 435 --------EELEEELEELEEELEELREELAELEAEL 462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-489 |
8.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 198 LRAQLEDAEGQKDGLRKQV-------SKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLK 270
Cdd:COG4717 137 LEAELAELPERLEELEERLeelreleEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 271 QQQKSIQAMEAKAQQLEEEGERRAAAER-------------------QVQQLEEQVQLLAGRLDGASQQIRWASTELDKE 331
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 332 KARVDSMVRHQESLQA----KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQEKQDL 407
Cdd:COG4717 297 KASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 408 EQVTTDlqlTISELRQQLEELKERERLLVAFPDLhqpeEAQIQSSSNVTQDMERQVQANAI--RIQVLQEENKRLQSMLT 485
Cdd:COG4717 377 AEAGVE---DEEELRAALEQAEEYQELKEELEEL----EEQLEELLGELEELLEALDEEELeeELEELEEELEELEEELE 449
|
....
gi 148708516 486 KIRE 489
Cdd:COG4717 450 ELRE 453
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-389 |
8.98e-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: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 191 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 268
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 269 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 343
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148708516 344 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
202-431 |
9.05e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 202 LEDAEGQKDGLRKQVSKLEQAlqqeqgqrqrqteeaertlakcehDRHQLLTEtcdLKTKVAVLEGDLK----QQQKSIQ 277
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEK------------------------DLHERLNG---LESELAELDEEIEryeeQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 278 AMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAG---RLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQ 354
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708516 355 QLDCLDQEREELRGSLDEA---------EAQR-----SELEEQLQSLQSDREQEQCQLqaqqekQDLEQVTTDLQLTISE 420
Cdd:PRK02224 315 RREELEDRDEELRDRLEECrvaaqahneEAESlredaDDLEERAEELREEAAELESEL------EEAREAVEDRREEIEE 388
|
250
....*....|.
gi 148708516 421 LRQQLEELKER 431
Cdd:PRK02224 389 LEEEIEELRER 399
|
|
| |
