|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-512 |
2.06e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 199 RKEIEKQL-----QAE-------MSQKLQHfKEVEVAKIKME----EKAQTQKEISELRYELER--THQAKAEALVSREK 260
Cdd:COG1196 195 LGELERQLeplerQAEkaeryreLKEELKE-LEAELLLLKLReleaELEELEAELEELEAELEEleAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 261 NAIERLQKQQEIEAKEVYAQRQS---LLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY 337
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 338 DQKLKtELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 417
Cdd:COG1196 354 EEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 418 QNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES 497
Cdd:COG1196 433 LEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
330
....*....|....*
gi 2024343399 498 HKQFLEKQLQSEVER 512
Cdd:COG1196 510 VKAALLLAGLRGLAG 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-491 |
1.84e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 191 LEGKLHEYRkEIEKQLQAEMSQKLQHFKEVEVAKikmEEKAQTQKEISELRYELER-----THQAKAEALVSREKNAIER 265
Cdd:COG1196 227 AELLLLKLR-ELEAELEELEAELEELEAELEELE---AELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 266 LQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTel 345
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 346 lkyQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 425
Cdd:COG1196 381 ---LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343399 426 LKEVSDyPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV 491
Cdd:COG1196 458 EEALLE-LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| LisH_2 |
pfam16045 |
LisH; |
70-95 |
2.07e-10 |
|
LisH;
Pssm-ID: 464992 Cd Length: 28 Bit Score: 56.31 E-value: 2.07e-10
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-550 |
2.95e-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: 64.69 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 230 KAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQE--IEAKEVYAQRQSLLKDIEVMRTReaELKQRIEAFEI 307
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaERYKELKAELRELELALLVLRLE--ELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 308 TQKLQEEKNKTIDDALRRREVAVkNIEETYDQKLKTELLKYQLELKEEYIartnkvtedekknkekamllreeavAVNSK 387
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALAN-------------------------EISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 388 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 467
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 468 SQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEkQLQSEVERSAQLKTQLLD--SEATVRKLNVQVEDLKLQLKQTQ 545
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQ 453
|
....*
gi 2024343399 546 AALEN 550
Cdd:TIGR02168 454 EELER 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-455 |
2.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 163 YRESLAEKLQLIDEQFADsypqhhkyepLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRY 242
Cdd:COG1196 233 KLRELEAELEELEAELEE----------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 243 ELERTHQAKAEALVSREKNAIERLQKQQEIEAKEvyAQRQSLLKDIEvmrTREAELKQRIEAFEITQKLQEEKNKTIDDA 322
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELE--EELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 323 LRRREVAVKNIEEtydqkLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE 402
Cdd:COG1196 378 EEELEELAEELLE-----ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024343399 403 LDLESVKAQVLLVNKQNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDE 455
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEAD 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
168-584 |
5.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 168 AEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE---KAQTQKEISELRYEL 244
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKA 1479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 245 ErtHQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEvmRTREAELKQRIEAFEITQKLQEEKNKTIDDALR 324
Cdd:PTZ00121 1480 E--EAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 325 RREvAVKNIEEtydqKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVnsKKEELKQAvsrtKELELD 404
Cdd:PTZ00121 1553 KAE-ELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKA----EEAKIK 1621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 405 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLR--DKLSQPSAEHLACQA-EL 481
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAeEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 482 RKVEHSRRLVMDEFESHKQfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDL-KLQLKQTQAALENEVYRNPKPSL 560
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAV 1780
|
410 420
....*....|....*....|....
gi 2024343399 561 VDRSVIDLIDDRIVPHDVYTDSIF 584
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-549 |
9.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 187 KYEPLEGKLHEYRKEIEKqLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELertHQAKAEALVsREKNAIERL 266
Cdd:TIGR02169 171 KKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYE---LLKEKEALE-RQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 267 QKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRI------EAFEITQKLQEEKNK--TIDDALRRREVAVKNIEETyD 338
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEER-L 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 339 QKLKTELLKYQLELK------EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSK----KEELKQAVSRTKELELDLESV 408
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEelereiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 409 KAQVLLVNKQNQLLTEKLKEV-SDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHS 487
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343399 488 RRLVMDEFEShkqfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 549
Cdd:TIGR02169 485 LSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-511 |
1.56e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 194 KLHEYRKEIEKQLQA-------------EMSQKLQHFK-EVEVAKIKMEEKAQ-TQKEISELRYELERTHQAKAEALVSR 258
Cdd:TIGR02168 169 KYKERRKETERKLERtrenldrledilnELERQLKSLErQAEKAERYKELKAElRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 259 EKNAIERLQKQQEIEAKEvyaqrqsllKDIEVMRTREAELKQRIE----AFEITQKLQEEKNKTIDDALRRREVAVKNIE 334
Cdd:TIGR02168 249 KEAEEELEELTAELQELE---------EKLEELRLEVSELEEEIEelqkELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 335 ETYDQKL----KTELLKYQLELKEEYIARTNKVTED-EKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVK 409
Cdd:TIGR02168 320 ELEAQLEelesKLDELAEELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 410 AQV-LLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVqnKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSR 488
Cdd:TIGR02168 400 NEIeRLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340
....*....|....*....|....*
gi 2024343399 489 RLVMDEFESHKQFLE--KQLQSEVE 511
Cdd:TIGR02168 478 DAAERELAQLQARLDslERLQENLE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-566 |
4.41e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 187 KYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKA---EALVSREKNAI 263
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 264 ERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY-----D 338
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyeeE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 339 QKLKTELLKYQLELKEEyiARTNKVTEDEKKNKEKAMLLREEAVavnSKKEELKQAvsrtkelELDLESVKAQVLLVNKQ 418
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKA-------EEENKIKAAEEAKKAEE 1672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 419 NQLLTEKLKevsdypllKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESH 498
Cdd:PTZ00121 1673 DKKKAEEAK--------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343399 499 KQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVedLKLQLKQTQAALENEVYRNPKPSLVDRSVI 566
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-543 |
6.66e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 232 QTQKEISELRYELERThQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKL 311
Cdd:TIGR02168 674 ERRREIEELEEKIEEL-EEKIAEL---EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 312 QEEkNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELK-EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE 390
Cdd:TIGR02168 750 AQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 391 LKQAVSRTK----ELELDLESVKAQVLLVNKQ-NQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRD 465
Cdd:TIGR02168 829 LERRIAATErrleDLEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343399 466 KLSQPSAEHLACQAELRKVEhsrrLVMDEFESHKQFLEKQLQSEVERSAQ-LKTQLLDSEATVRKLNVQVEDLKLQLKQ 543
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
167-430 |
8.00e-08 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 56.40 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 167 LAEKLQLIDEQFADSYPQHHKYEP-LEGKLHEYRKEIEKQLQ-----AEMSQKLQHFKEVEVAKIKMEEKAQTQK----- 235
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQLMHPvLMEKIEKLKDEFNKRLSrapnyLSLKYKLDMLNEFSRAKALSEKKSKAEKlkaei 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 236 -----------EISE----LRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVYaqrQSLLKDIEVMRTREAELKQ 300
Cdd:PLN03229 564 nkkfkevmdrpEIKEkmeaLKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVL---KSMGLEVIGVTKKNKDTAE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 301 RIEAFEITQK---LQEEKNKTIDDALRrrevavknieeTYDQKLKTELLKyqLELKEEyiARTNKVTEDEKKNKEKAMLL 377
Cdd:PLN03229 641 QTPPPNLQEKiesLNEEINKKIERVIR-----------SSDLKSKIELLK--LEVAKA--SKTPDVTEKEKIEALEQQIK 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024343399 378 REEAVAVNSKkeELKQavsrtKELELDLESVKAQVLLVNKQNQLLTEKLKEVS 430
Cdd:PLN03229 706 QKIAEALNSS--ELKE-----KFEELEAELAAARETAAESNGSLKNDDDKEED 751
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
194-524 |
1.24e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 194 KLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELerthqakAEALVSREKNAIERLQKQQEIE 273
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-------YLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 274 AKEVYAQRQSLLKDIEVMRTREAELKQRIEAfeitQKLQEEKNKTIDDAL------RRREVAVKNIEETYDQKLKTELLK 347
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKE----KKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 348 YQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESvKAQVLLVNKQNQLLTEKLK 427
Cdd:pfam02463 326 AEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-ERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 428 EVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQ 507
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSEDLLKETQLVK 481
|
330
....*....|....*..
gi 2024343399 508 SEVERSAQLKTQLLDSE 524
Cdd:pfam02463 482 LQEQLELLLSRQKLEER 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-520 |
1.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 165 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLqAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYEL 244
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 245 ERTHQaKAEALVSREKNAIERLQKQ-QEIEAKEvyAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNK------ 317
Cdd:PRK03918 306 LDELR-EIEKRLSRLEEEINGIEERiKELEEKE--ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrlt 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 318 --TIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKeeyIARTNKVTEDEKKNK-------------EKAMLLREEAV 382
Cdd:PRK03918 383 glTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE---IKELKKAIEELKKAKgkcpvcgrelteeHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 383 AVNSKKEELKQAVSRTKELELDLESVKAqvlLVNKQNQLLteKLKEVSDYPLLKEEKLElqvqnKLLRQQLDETRTENQH 462
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELI--KLKELAEQLKELEEKLK-----KYNLEELEKKAEEYEK 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343399 463 LRDKLSQPSAEHLACQAELRKVEhsrrlvmdEFESHKQFLEKQLQSEVERSAQLKTQL 520
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLE--------ELKKKLAELEKKLDELEEELAELLKEL 579
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-430 |
2.13e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 184 QHHKYEPLEGKLHEY---RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVS 257
Cdd:TIGR02168 237 LREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 258 REKNAIERLQ--KQQEIEAKEVYAQRQsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEE 335
Cdd:TIGR02168 317 QLEELEAQLEelESKLDELAEELAELE---EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 336 T-YDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLL 414
Cdd:TIGR02168 394 QiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*.
gi 2024343399 415 VNKQNQLLTEKLKEVS 430
Cdd:TIGR02168 473 AEQALDAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-522 |
2.19e-06 |
|
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: 51.99 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 227 MEEKAQTQKEISELRYELERTHQ-------------AKAEALVSREKNAIERLQK-QQEIEAKEvyAQRQSLLKDIEVMR 292
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRkigeiekeieqleQEEEKLKERLEELEEDLSSlEQEIENVK--SELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 293 TREAELKQRIEAFE------ITQKLQEEKNKtIDDALRRREVAVKNIE---------ETYDQKLKTELLKYQLELKEEYI 357
Cdd:TIGR02169 772 EDLHKLEEALNDLEarlshsRIPEIQAELSK-LEEEVSRIEARLREIEqklnrltleKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 358 ARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvNKQNQLLTEKLKEVSDYPLLKE 437
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE------RKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 438 EKLELQVQNKLLRQQLDETRTENQHLRDkLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLeKQLQSEVERSAQLK 517
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEER 1002
|
....*
gi 2024343399 518 TQLLD 522
Cdd:TIGR02169 1003 KAILE 1007
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
202-513 |
3.46e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 202 IEKQLQAEMSQKLQHFKEVEVAKIKmEEKAQTQKEIsELRYELERTHQAKAEAL-------VSREKNAIERLQKQQEIEA 274
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLR-QEKEEKAREV-ERRRKLEEAEKARQAEMdrqaaiyAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 275 KEvyaqrqsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA--VKNIEETYDQKLKTELLKYQLEL 352
Cdd:pfam17380 356 EE---------RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArkVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 353 KEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDY 432
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 433 PLLKEEKLELQVQNKLLRQQL----DETRTENQHLRDKlSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQS 508
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKaiyeEERRREAEEERRK-QQEMEERRRIQEQMRKATEERSR-LEAMEREREMMRQIVES 584
|
....*
gi 2024343399 509 EVERS 513
Cdd:pfam17380 585 EKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-551 |
6.32e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 296 AELKQRIEAFEItQKLQEEKNKTIDDALRRREV--AVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEK 373
Cdd:COG1196 196 GELERQLEPLER-QAEKAERYRELKEELKELEAelLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 374 AMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvnKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQL 453
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEE------LEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 454 DETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQSEVE---RSAQLKTQLLDSEATVRKL 530
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElaaQLEELEEAEEALLERLERL 419
|
250 260
....*....|....*....|.
gi 2024343399 531 NVQVEDLKLQLKQTQAALENE 551
Cdd:COG1196 420 EEELEELEEALAELEEEEEEE 440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-402 |
7.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 192 EGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE--KAQTQKEISELRY--ELERTHQAKAEALV-SREKNAIERL 266
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKfeEARMAHFARRQAAIkAEEARKADEL 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 267 QKQQEIEAKEvYAQRQSLLKDIEVMRTREAELKQRIEA---FEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKT 343
Cdd:PTZ00121 1284 KKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343399 344 ELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE 402
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-551 |
7.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 187 KYEPLEGKLHEYRKEIEKQLQaEMSQKLQHFKEVE-VAKIKMEEKAQTQKEISELRYELERTHQAKAEalVSREKNAIER 265
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEeLIKEKEKELEEVLREINEISSELPELREELEK--LEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 266 LQkqQEIEAKEVyaQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTEL 345
Cdd:PRK03918 236 LK--EEIEELEK--ELESLEGSKRKLEEKIRELEERIE--ELKKEIEELEEK------------VKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 346 LKyqlELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 425
Cdd:PRK03918 298 LS---EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 426 LKevsdyplLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSAEhlacQAELRKVEHSRRLVMDEFESHKQF--LE 503
Cdd:PRK03918 375 ER-------LKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITAR----IGELKKEIKELKKAIEELKKAKGKcpVC 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024343399 504 KQLQSEVERS---AQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 551
Cdd:PRK03918 442 GRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
191-549 |
1.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 191 LEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVakiKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQ 270
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEE---ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 271 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQ- 349
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEe 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 350 LELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQA-------------VSRTKELELDLESVKAQVLLV- 415
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 416 ----------NKQNQLLTEKLKEVSDYPLLKE-EKLELQVQNKLLRQQLDETRTENQHLRDKLSQ-----PSAEHLACQA 479
Cdd:COG4717 284 gllallflllAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEElqellREAEELEEEL 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343399 480 ELRKVEHSRRLVMDEF--ESHKQFLEK-----QLQSEVERSAQLKTQLLDSEATVRKLNVQV--EDLKLQLKQTQAALE 549
Cdd:COG4717 364 QLEELEQEIAALLAEAgvEDEEELRAAleqaeEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
134-543 |
2.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 134 LMWILMGLTEHHLSKECNDRETQTISIPpyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIE--KQLQAEMS 211
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 212 QKLQHFKEVEVAKIKMEEKAQTQKEISEL--RYE-LERTHQAKAEALVSREKNAIERLQKQQEIEAK------EVYAQRQ 282
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELpeRLEeLEERLEELRELEEELEELEAELAELQEELEELleqlslATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 283 SLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIARTNK 362
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 363 ------------VTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRT--KELELDLESVKAQVLLVNKQNQLLTEKLKE 428
Cdd:COG4717 276 agvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 429 VSDYpllkEEKLELQVQNKLLRQQLDETRTENqhlRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQS 508
Cdd:COG4717 356 AEEL----EEELQLEELEQEIAALLAEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430
....*....|....*....|....*....|....*.
gi 2024343399 509 EV-ERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQ 543
Cdd:COG4717 429 ELeEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-555 |
3.80e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 228 EEKAQTQKEISELRYELERTHQakaealvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEI 307
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQS---------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 308 TQKLQEEKNKTIDDALRRREvavKNIEEtydqkLKTELLKYQLELkeeyiartnkvtedekkNKEKAMLLREEAVAVNSK 387
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELE---ARIEE-----LEEDLHKLEEAL-----------------NDLEARLSHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 388 KEELKQAVSRtkeLELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 467
Cdd:TIGR02169 800 LSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQE------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 468 sqpsAEHlacQAELRKVEHSRrlvmdefeshkqfleKQLQSEVERsaqLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAA 547
Cdd:TIGR02169 871 ----EEL---EAALRDLESRL---------------GDLKKERDE---LEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
....*...
gi 2024343399 548 LENEVYRN 555
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
199-340 |
4.92e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 199 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAK--- 275
Cdd:TIGR02794 83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA--EAERKAKEEAAKQAEEEAKaka 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343399 276 --EVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQK 340
Cdd:TIGR02794 161 aaEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
309-463 |
8.32e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 309 QKLQEEKNKTIDDALRRREVAVKNIEetydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKK 388
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL----LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343399 389 EELKQAVSRTKELELDLESVKAQV-LLVNKQNQllteKLKEVSDypLLKEEklelqVQNKLLRQQLDETRTENQHL 463
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELeELIEEQLQ----ELERISG--LTAEE-----AKEILLEKVEEEARHEAAVL 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
192-356 |
1.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 192 EGKLHEYRKEIEKQLQAEmsqklqhfkEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQ---- 267
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEA---------KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 268 KQQEIEAKE--VYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTIDDAlrrREVAVKNIEEtydqKLKTEL 345
Cdd:PRK12704 101 KLELLEKREeeLEKKEKELEQKQQELEKKEEELEELIE--EQLQELERISGLTAEEA---KEILLEKVEE----EARHEA 171
|
170
....*....|.
gi 2024343399 346 LKYQLELKEEY 356
Cdd:PRK12704 172 AVLIKEIEEEA 182
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-538 |
2.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 187 KYEPLEGKLHEYRK---EIEKQLqAEMSQKLQHFKE-VEVAKIKMEEKAQTQKEISELRYELERTHQ-AKAEALVSREKN 261
Cdd:PRK03918 294 EYIKLSEFYEEYLDelrEIEKRL-SRLEEEINGIEErIKELEEKEERLEELKKKLKELEKRLEELEErHELYEEAKAKKE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 262 AIERLQKQQEIEAKEvyaqrqSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNktiddalrRREVAVKNIEETYDQKL 341
Cdd:PRK03918 373 ELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEEIS--KITARIGELKK--------EIKELKKAIEELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 342 KTELLKYQL------ELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE------LKQAVSRTKELE-----LD 404
Cdd:PRK03918 437 KCPVCGRELteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEeklkkYN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 405 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLA-CQAELRK 483
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKE 596
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343399 484 VE--HSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLK 538
Cdd:PRK03918 597 LEpfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
212-445 |
2.14e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 212 QKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT----------HQAKAEALVSREKNAIERLQKQQEIEAKEVYAQR 281
Cdd:PRK05771 23 EALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklrsylpkLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 282 QSLLKDIEVMRTREAELKQRIEAFEITQKLqeeknkTIDDA-LRRRE---VAVKNIEETYDqklktELLKYQLELKEEYI 357
Cdd:PRK05771 103 KELEEEISELENEIKELEQEIERLEPWGNF------DLDLSlLLGFKyvsVFVGTVPEDKL-----EELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 358 ARTNK-------VTEDEKKNKEKAMLLREEAVAVN-----SKKEELKQAVSRTKELELDLESVKAQvllvnkqnqlLTEK 425
Cdd:PRK05771 172 ISTDKgyvyvvvVVLKELSDEVEEELKKLGFERLEleeegTPSELIREIKEELEEIEKERESLLEE----------LKEL 241
|
250 260
....*....|....*....|
gi 2024343399 426 LKEVSDYPLLKEEKLELQVQ 445
Cdd:PRK05771 242 AKKYLEELLALYEYLEIELE 261
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
143-551 |
3.28e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 143 EHHLSKECNDRETQTISIppyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQL---------------- 206
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQryaelcaaaitctaqc 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 207 -------QAEMSQKL----QHFKEVEVAKIKMEEK-------AQTQKEI------SELRYELERTHQAKAEALVSREKNA 262
Cdd:TIGR00618 454 eklekihLQESAQSLkereQQLQTKEQIHLQETRKkavvlarLLELQEEpcplcgSCIHPNPARQDIDNPGPLTRRMQRG 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 263 IERLQKQQEIEAKeVYAQRQSLLKDIEVMRTREAELKQRIEAFEIT-QKLQEEKNKTIDDALRRREVAVKNIEEtydQKL 341
Cdd:TIGR00618 534 EQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCdNRSKEDIPNLQNITVRLQDLTEKLSEA---EDM 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 342 KTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLRE-EAVAVNSKKEELKQAVSRTKELELDLesvkaqvllvNKQNQ 420
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLTLTQERVREHALSIRVLPKEL----------LASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 421 LLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES--- 497
Cdd:TIGR00618 680 LALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlk 757
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024343399 498 HKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 551
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-517 |
3.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 188 YEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRyeleRTHQAKAEALVSREKNAIERLQ 267
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR----KAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 268 KQQEIEAKEVYAQRqsllKDIEVMRT---REAELKQRIEA---FEITQKLQE----EKNKTIdDALRRREVAVKNIEETY 337
Cdd:PTZ00121 1169 ARKAEDAKKAEAAR----KAEEVRKAeelRKAEDARKAEAarkAEEERKAEEarkaEDAKKA-EAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 338 ---DQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTK----------ELELD 404
Cdd:PTZ00121 1244 kaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkaeeakkadEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 405 LESVKAQVLLVNKQnqllTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKV 484
Cdd:PTZ00121 1324 AEEAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350
....*....|....*....|....*....|...
gi 2024343399 485 EHSRRLVMDEFEshKQFLEKQLQSEVERSAQLK 517
Cdd:PTZ00121 1400 AEEDKKKADELK--KAAAAKKKADEAKKKAEEK 1430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-550 |
3.94e-04 |
|
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: 44.24 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 191 LEGKLHEYRKEIE---KQLQAEMSQKLQHF-KEVEVAKIKMEEK-AQTQKEISELRYELERTHQAKAEALVSREKNAIER 265
Cdd:TIGR04523 286 LEKQLNQLKSEISdlnNQKEQDWNKELKSElKNQEKKLEEIQNQiSQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 266 LQKQQEIEakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNI-EETYDQKLKTE 344
Cdd:TIGR04523 366 EEKQNEIE--KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLkETIIKNNSEIK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 345 LLKYQLELKEEYIARTNKVTEDEKKNKEKAML--------LREEAVAVNSKKEELKQAVSRTKELELDLESVKAQV-LLV 415
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsSLK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 416 NKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKllRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVehsrrlvMDEF 495
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL-------IDQK 594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2024343399 496 ESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALEN 550
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
189-550 |
4.54e-04 |
|
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: 44.44 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 189 EPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVeVAKIKMEEKAQTQK-----------EISELRYELERTHQAKAEA--- 254
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEK-RDELNGELSAADAAvakdrselealEDQHGAFLDADIETAAADQeql 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 255 -LVSREKNAIER-----LQKQQEIEAKevYAQRQSLLK-----DIEVMR-----TREAELKQRIEAFEITQKLQEEKNKT 318
Cdd:pfam12128 350 pSWQSELENLEErlkalTGKHQDVTAK--YNRRRSKIKeqnnrDIAGIKdklakIREARDRQLAVAEDDLQALESELREQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 319 IDDALRRREVAVKNIEET-------YDQKLKTELLKYQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVA---VNSKK 388
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKSRlgelklrLNQATATPELLLQLENFDERIERARE--EQEAANAEVERLQSELRQArkrRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 389 EELKQAVSRTKELELDLESVKAQvlLVNKQNQLLTEKLKEVSDYpllKEEKLELQVQNKLLRQQLDETRTEnqhlrdklS 468
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQ--LFPQAGTLLHFLRKEAPDW---EQSIGKVISPELLHRTDLDPEVWD--------G 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 469 QPSAEH--LACQAELRKVEHSRRLVM-DEFESHKQFLEKQLQSEVERSAQLKTQLLdseatvrKLNVQVEDLKLQLKQTQ 545
Cdd:pfam12128 573 SVGGELnlYGVKLDLKRIDVPEWAASeEELRERLDKAEEALQSAREKQAAAEEQLV-------QANGELEKASREETFAR 645
|
....*
gi 2024343399 546 AALEN 550
Cdd:pfam12128 646 TALKN 650
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-549 |
5.38e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 197 EYRKEIE---KQLQAEMSQKL-------QHFKEVEVAKIKMEEKAQTQK-EISELRYELERTHQAKAEALVSREKnaiER 265
Cdd:pfam01576 650 EAKEELErtnKQLRAEMEDLVsskddvgKNVHELERSKRALEQQVEEMKtQLEELEDELQATEDAKLRLEVNMQA---LK 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 266 LQKQQEIEAKEVYAQ--RQSLLKDIEVMRT-REAELKQRIEAFEITQKLQ---EEKNKTIDDALRRREVAVKNIeetydQ 339
Cdd:pfam01576 727 AQFERDLQARDEQGEekRRQLVKQVRELEAeLEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAVKQL-----K 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 340 KLKTELLKYQLELKEEYIAR-----TNKVTEDEKKNKEKAMLLREEAVAVNSKKEelKQAVSRTKEL--ELDLESVKAQV 412
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRdeilaQSKESEKKLKNLEAELLQLQEDLAASERAR--RQAQQERDELadEIASGASGKSA 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 413 LLVNKQN------QLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEH 486
Cdd:pfam01576 880 LQDEKRRleariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343399 487 SRR----LVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 549
Cdd:pfam01576 960 TVKskfkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-537 |
5.49e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 199 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 278
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 279 AQRQSLLKDIEVMRTREAELKQRIEAfEITQKLQEEKNKTIDDALRRREVAVKNIEET----YDQKLKTELLKYQLELKE 354
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARG 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 355 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL 434
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 435 LKEEKLELQVQ-----NKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQSE 509
Cdd:COG1196 676 EAEAELEELAErlaeeELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
330 340
....*....|....*....|....*...
gi 2024343399 510 VERSAQLKTQlldsEATVRKLNVQVEDL 537
Cdd:COG1196 756 LPEPPDLEEL----ERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-431 |
5.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 167 LAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELER 246
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 247 THQAKAEALVSREKNAIERLQKQQEIEAKEVyaqrqsllkdiEVMRTREAELKQRIEAFeitqKLQEEKNKTIDDALRRR 326
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----------EELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKE 1738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 327 EvavkniEEtydQKLKTELLKYQLELKeeyiartNKVTEDEKKNKEKAMLLREEAVAV---NSKKEELKQAVSRTKELEl 403
Cdd:PTZ00121 1739 A------EE---DKKKAEEAKKDEEEK-------KKIAHLKKEEEKKAEEIRKEKEAVieeELDEEDEKRRMEVDKKIK- 1801
|
250 260
....*....|....*....|....*...
gi 2024343399 404 DLESVKAQVLLVNKQNQLLTEKLKEVSD 431
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
191-430 |
5.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 191 LEGKLHEYRKEIEkqlQAEmsQKLQHFKE----VEVAkikmEEKAQTQKEISELRYELERTHQAKAEAlvsreKNAIERL 266
Cdd:COG3206 180 LEEQLPELRKELE---EAE--AALEEFRQknglVDLS----EEAKLLLQQLSELESQLAEARAELAEA-----EARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 267 QKQQEIEAKEVYAQRQSLLkdIEVMRTREAELKQRIEafEITQKLQEEkNKTIDDALRRREVAvknieetyDQKLKTELL 346
Cdd:COG3206 246 RAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELA--ELSARYTPN-HPDVIALRAQIAAL--------RAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 347 KYQLELKEEYIArtnkvtedekknkekamlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKL 426
Cdd:COG3206 313 RILASLEAELEA------------------LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
....
gi 2024343399 427 KEVS 430
Cdd:COG3206 375 EEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-538 |
6.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 187 KYEPLEGKLHEYRKEIEKQLQ------AEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREK 260
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 261 NAIERLQKQQEieakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQ--------KLQEEKNKTIddaLRRREVAVKN 332
Cdd:PRK03918 391 KELEELEKAKE----EIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL---LEEYTAELKR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 333 IEETY------DQKLKTELLKYQLELKEEYIARTNKVTEDE----------------KKNKEKAMLLREEAVAVNSKKEE 390
Cdd:PRK03918 464 IEKELkeieekERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleelEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 391 LKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEV--SDYPLLKEEKLELQ------VQNKLLRQQLDETRTENQH 462
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELEpfyneyLELKDAEKELEREEKELKK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 463 LRDKLSQPSAEHLACQAELRKV-----EHSRRLVMDEFESHKQF---LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQV 534
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELrkeleELEKKYSEEEYEELREEyleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
....
gi 2024343399 535 EDLK 538
Cdd:PRK03918 704 EERE 707
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
228-459 |
8.60e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 228 EEKAQTQKEISELRYELERTHQAKAEALvsREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAfei 307
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 308 tqkLQEEKNKTIDDALRR----REVAVKNIEETYDQKLKTELLKYQLElkeeyiartnkvtedekKNKEKAMLLREEAVA 383
Cdd:COG4942 102 ---QKEELAELLRALYRLgrqpPLALLLSPEDFLDAVRRLQYLKYLAP-----------------ARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343399 384 VNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTE 459
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-549 |
9.42e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 185 HHKYEPLEGKLHEYRKEIEKQlqaeMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREkNAIE 264
Cdd:PRK02224 205 HERLNGLESELAELDEEIERY----EEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERERE-ELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 265 RLQKQQEiEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFeitqklqEEKNKTIDDALRRREVAVKNIEETYDqklkte 344
Cdd:PRK02224 280 EVRDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARREEL-------EDRDEELRDRLEECRVAAQAHNEEAE------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 345 llkyqlelkeeyiartnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAV----SRTKELELDLESVKAQVllvnkqnQ 420
Cdd:PRK02224 346 -----------------SLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF-------G 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 421 LLTEKLKEVSDY-PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSaehlaCQAELRKVEHSRRLVMDEfe 496
Cdd:PRK02224 402 DAPVDLGNAEDFlEELREERDELREREAELEatlRTARERVEEAEALLEAGKCPE-----CGQPVEGSPHVETIEEDR-- 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2024343399 497 shkqflekqlqsevERSAQLKTQLLDSEATVRKLNVQVEDLKlQLKQTQAALE 549
Cdd:PRK02224 475 --------------ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE 512
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
197-484 |
1.00e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.08 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 197 EYRKEIEKQLQAEMSQ----KLQHFKEVEVAKIKMEE---KAQTQKEISELRY--------ELERTHQ-----------A 250
Cdd:NF033838 114 ELTSKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEaekKAKDQKEEDRRNYptntyktlELEIAESdvevkkaelelV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 251 KAEALVSREKNAIErlQKQQEIEAKEVYAQRqslLKDIEVMRTR-EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA 329
Cdd:NF033838 194 KEEAKEPRDEEKIK--QAKAKVESKKAEATR---LEKIKTDREKaEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 330 VKNIEETYDQKlKTELLKYQLELKEEYIARTN-----KVTEDEKKnkekamlLREEAVAVNSKKEELKQAVSRTKELELD 404
Cdd:NF033838 269 VLGEPATPDKK-ENDAKSSDSSVGEETLPSPSlkpekKVAEAEKK-------VEEAKKKAKDQKEEDRRNYPTNTYKTLE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 405 LESVKAQVLLVNKQNQLLTEKLKEVSDypllkEEKLElQVQNKLLRQQLDETRTENqhLRDKLSQPSAEHLACQAELRKV 484
Cdd:NF033838 341 LEIAESDVKVKEAELELVKEEAKEPRN-----EEKIK-QAKAKVESKKAEATRLEK--IKTDRKKAEEEAKRKAAEEDKV 412
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
164-515 |
1.33e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 164 RESLAEKLQLIDEQFAdsypqhhkyeplegkLHEYRKEIEKQ--LQAEMSQKLQ----HFKEVEVAKIKMEEKAQTQKEI 237
Cdd:COG3096 292 RELFGARRQLAEEQYR---------------LVEMARELEELsaRESDLEQDYQaasdHLNLVQTALRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 238 SELRYELERTHQAKAEALVSREKNAIERLQKQQEI-EAKEVYAQRQSLLkdiEVMRTREAELKQRIEAFEITQKLQEEKN 316
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdSLKSQLADYQQAL---DVQQTRAIQYQQAVQALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 317 KTIDDALRRREVAVKNIEETYDQKLKtelLKYQLELKEEYIARTNKVTE---------DEKKNKEKAMLLREEAVAVNSK 387
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLE---LEQKLSVADAARRQFEKAYElvckiagevERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 388 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKE------EKLELQVQNKL-----LRQQLDET 456
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAeleaqlEELEEQAAEAVeqrseLRQQLEQL 590
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343399 457 RTENQHLRDK-------------LSQPSAEHLACQAEL-----RKVEHSRRLVM--DEFESHKQflekQLQSEVERSAQ 515
Cdd:COG3096 591 RARIKELAARapawlaaqdalerLREQSGEALADSQEVtaamqQLLEREREATVerDELAARKQ----ALESQIERLSQ 665
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
195-540 |
3.01e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 195 LHEYRKEIEKQLqaEMSQKLQhfkevevakiKMEEKAQTQKEiselRYELERTHqaKAEALVSREKNAIERLQKQQEIEA 274
Cdd:COG5022 805 LLGSRKEYRSYL--ACIIKLQ----------KTIKREKKLRE----TEEVEFSL--KAEVLIQKFGRSLKAKKRFSLLKK 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 275 KEVYAQRQSLLKDIevmRTREAELKQRIEAFEITQKLQEEKNKTIddalrrrevavknIEETydQKLKTELLKyQLELKE 354
Cdd:COG5022 867 ETIYLQSAQRVELA---ERQLQELKIDVKSISSLKLVNLELESEI-------------IELK--KSLSSDLIE-NLEFKT 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 355 EYIARtnkvtedEKKNKEKAML--LREEAVAVNSKKEELKQAVSRTKELELDLESvkaqvlLVNKQNQLLTEKLKEVSDY 432
Cdd:COG5022 928 ELIAR-------LKKLLNNIDLeeGPSIEYVKLPELNKLHEVESKLKETSEEYED------LLKKSTILVREGNKANSEL 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 433 PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSAEHLACQAELrKVEHSRRLVMDEFESHKQFLeKQLQSE 509
Cdd:COG5022 995 KNFKKELAELSKQYGALQestKQLKELPVEVAELQSASKIISSESTELSILK-PLQKLKGLLLLENNQLQARY-KALKLR 1072
|
330 340 350
....*....|....*....|....*....|..
gi 2024343399 510 VERSAQLKTQLLDSEATVRKLN-VQVEDLKLQ 540
Cdd:COG5022 1073 RENSLLDDKQLYQLESTENLLKtINVKDLEVT 1104
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
169-523 |
3.60e-03 |
|
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: 41.10 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 169 EKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQlQAEMSQKLQH-----FKEVEVAKIKMEEKAQTQKEISELRYE 243
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGE-NAESSKRLNEnannlIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 244 LERTHQAKAEALVSREKNAIErlqkqqeieaKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLqEEKNKTIDDAL 323
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETE----------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL-SKSSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 324 RRREVAVKNIeetyDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELEl 403
Cdd:COG5185 384 DTIESTKESL----DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 404 dlesvkaqvllvNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSaehlacqAELRK 483
Cdd:COG5185 459 ------------EESQSRLEEAYDEINRSVRSKKEDLNEELTQ--IESRVSTLKATLEKLRAKLERQL-------EGVRS 517
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024343399 484 VEHSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDS 523
Cdd:COG5185 518 KLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAK 557
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
436-549 |
4.16e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 436 KEEKL-ELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV---MDEFESHKQFLEKQLQSEVE 511
Cdd:PRK09039 51 KDSALdRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELagaGAAAEGRAGELAQELDSEKQ 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024343399 512 RSAQLKTQlldseatVRKLNVQVEDLKLQLKQTQAALE 549
Cdd:PRK09039 131 VSARALAQ-------VELLNQQIAALRRQLAALEAALD 161
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-397 |
4.83e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 178 FADSYPQHHKYEPLEGKLHEYRKEI---EKQLQAEMSQKLQHFKEVEVAKIKMeekAQTQKEISELRYELERThQAKAEA 254
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAAL-EAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 255 LVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDD-ALRRREVAVKNI 333
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024343399 334 EETYDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSR 397
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
223-399 |
4.93e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 223 AKIKMEEKAQTQKEISELRYE-----LERT-------HQAKAEALVSREKN----AIERLQKQQEIEAKEVYAQRQSLLK 286
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEarqarLEREkaarearHKKAAEARAAKDKDavaaALARVKAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 287 DIEVMRTREAELKQRIEAFEITQKLQEE--KNKTIDDALRR--------REVAVKNIEETYDQKLKTEL------LKYQL 350
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAAdpKKAAVAAAIARakakkaaqQAANAEAEEEVDPKKAAVAAaiarakAKKAA 595
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343399 351 ELKEEYIARTNKVTEDEKKNKEKAMLLR------------EEAVAVNSKKEELKQAVSRTK 399
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARakakkaeqqanaEPEEPVDPRKAAVAAAIARAK 656
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
197-400 |
5.25e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 197 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvsREKNAIERLQKQQEIEAKE 276
Cdd:PRK09510 63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA---EEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 277 VYAQRQSLLKDIEVMrtREAELKQRIEAfeitqklqEEKNKTIDDALRRREV-AVKNIEETYDQKLKTEL-LKYQLELKE 354
Cdd:PRK09510 140 KAAAAAKAKAEAEAK--RAAAAAKKAAA--------EAKKKAEAEAAKKAAAeAKKKAEAEAAAKAAAEAkKKAEAEAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024343399 355 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKE 400
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-554 |
5.63e-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: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 197 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE-KAQTQKEISELRYELERTH---------QAKAEALVSREKNAIERL 266
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtKNRLQQELDDLLVDLDHQRqlvsnlekkQKKFDQMLAEEKAISARY 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 267 QKQQ---EIEAKEVYAQRQSLLKDIEvmrtreaELKQRIEAFEITQKLQEEKnktIDDALRRREVAVKNIE--------- 334
Cdd:pfam01576 621 AEERdraEAEAREKETRALSLARALE-------EALEAKEELERTNKQLRAE---MEDLVSSKDDVGKNVHelerskral 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 335 ETYDQKLKTELLKYQLELKEEYIAR------------------TNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVS 396
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 397 RTKELELDLESVKAQVLLVNKQNQLLTEKLKevsdypllkeeklELQVQNKLLRQQLDETR-------TENQHLRDKLSQ 469
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAANKGREEAVKQLK-------------KLQAQMKDLQRELEEARasrdeilAQSKESEKKLKN 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 470 PSAEHLACQAELRKVEHSRRLVMDEFEshkqflekQLQSEVERSAQLKTQLLDSEatvRKLNVQVEDLKLQLKQTQAALE 549
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERD--------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELEEEQSNTE 906
|
....*..
gi 2024343399 550 --NEVYR 554
Cdd:pfam01576 907 llNDRLR 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-306 |
5.66e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 199 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 278
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
90 100
....*....|....*....|....*...
gi 2024343399 279 AQRQSLLKDIEVMRTREAELKQRIEAFE 306
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEALG 780
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-545 |
5.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 164 RESLAEKLQLIDEQFADSypqhhkyEPLEGKLHEYRKEIEKQLQaEMSQKLQhfKEVEVAKIKMEEKAQTQKEISELRYE 243
Cdd:pfam01576 42 KNALQEQLQAETELCAEA-------EEMRARLAARKQELEEILH-ELESRLE--EEEERSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 244 LERTHQAKAEalVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELK-QRIEAFEITQKLQEEKNK---TI 319
Cdd:pfam01576 112 LDEEEAARQK--LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEKAKSLSKLKNKheaMI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 320 DDALRRREVAVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTE----DEKKNKE-KAMLLR--EEAVAVNSKKEELK 392
Cdd:pfam01576 190 SDLEERLKKEEKGRQEL--EKAKRKLEGESTDLQEQIAELQAQIAElraqLAKKEEElQAALARleEETAQKNNALKKIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 393 QAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEkLELQVQNKLLRQQLDETR-TENQHLRDKLSQPS 471
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAEKQRRDLGEELEA------LKTE-LEDTLDTTAAQQELRSKReQEVTELKKALEEET 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 472 AEHLACQAELRKvEHSRRLV-----MDEFESHKQFLEKQLQSEVERSAQLKTQL-------LDSEATVRKLNVQVEDLKL 539
Cdd:pfam01576 341 RSHEAQLQEMRQ-KHTQALEelteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQA 419
|
....*.
gi 2024343399 540 QLKQTQ 545
Cdd:pfam01576 420 RLSESE 425
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-552 |
5.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 249 QAKAEALVSRE--KNAIERLQKQQEIEAKEVYAQR--QSLLKDIEVMRTREAEL-------KQRIEAFEITQKLQEEknk 317
Cdd:COG3206 84 ETQIEILKSRPvlERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVieisytsPDPELAAAVANALAEA--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 318 TIDDALRRREVAVKNIEETYDQKLKTelLKYQLELKEEYIARTnkvtedekKNKEKAMLLREEAVAVNSKKEELKQAVSr 397
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEEF--------RQKNGLVDLSEEAKLLLQQLSELESQLA- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 398 tkELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL---LKEEKLELQVQnkllRQQLDETRTEN----QHLRDKLSQp 470
Cdd:COG3206 230 --EARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqLRAQLAELEAE----LAELSARYTPNhpdvIALRAQIAA- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 471 saehlacqaelrkvehsrrlvmdefeshkqfLEKQLQSEVERS-AQLKTQLLDSEATVRKLNVQVEDLKLQLK------Q 543
Cdd:COG3206 303 -------------------------------LRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAelpeleA 351
|
....*....
gi 2024343399 544 TQAALENEV 552
Cdd:COG3206 352 ELRRLEREV 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-412 |
6.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 193 GKLHEYRKEIEKQlQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNA--IERLQKQQ 270
Cdd:PRK02224 478 EELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAaeLEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 271 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREvAVKNIEETYDQ---KLKT---- 343
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE-KREALAELNDErreRLAEkrer 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 344 -------------ELLKYQLELKEEYIArtnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE---LDLES 407
Cdd:PRK02224 636 kreleaefdeariEEAREDKERAEEYLE---QVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEnrvEALEA 712
|
....*
gi 2024343399 408 VKAQV 412
Cdd:PRK02224 713 LYDEA 717
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
192-549 |
6.72e-03 |
|
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: 40.48 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 192 EGKLHEYRKEIEKQLQAemSQKLQHfkEVEVAKIKMEEKAQTQKE-ISELRYELERTHQAKAEALVSREKNaierlqKQQ 270
Cdd:pfam05483 105 ENKLQENRKIIEAQRKA--IQELQF--ENEKVSLKLEEEIQENKDlIKENNATRHLCNLLKETCARSAEKT------KKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 271 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIE--AFEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTELLKY 348
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQAEnaRLEMHFKLKEDHEK------------IQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 349 QLELKEeyiartnkVTEDEKKNKEKAMLLREEAVAVNS-------KKEELKQAVSRTKELELDLESVKaqvllVNKQNQL 421
Cdd:pfam05483 243 SLLLIQ--------ITEKENKMKDLTFLLEESRDKANQleektklQDENLKELIEKKDHLTKELEDIK-----MSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 422 LTEKLKEVsdypllkeeklELQVQNKLLRQQLDETRTENQhlrdklsqpsaehlacqaELRKVEHSRRLVMDEFESHKQF 501
Cdd:pfam05483 310 STQKALEE-----------DLQIATKTICQLTEEKEAQME------------------ELNKAKAAHSFVVTEFEATTCS 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2024343399 502 LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 549
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-412 |
7.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 204 KQLQAEMSQKLQHFKEVEvakikmEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAKEVYAQRQS 283
Cdd:COG4942 23 AEAEAELEQLQQEIAELE------KELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 284 LLKDIEvmrTREAELKQRIEAFEITQKLQEEK----NKTIDDALRRREV------AVKNIEETYDQKLKT-ELLKYQLEL 352
Cdd:COG4942 95 LRAELE---AQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYlkylapARREQAEELRADLAElAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343399 353 KEEYIARTNKVTEDEKKNKEKAMLLREEAVA-VNSKKEELKQAVSRTKELELDLESVKAQV 412
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLArLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| LisH |
smart00667 |
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
70-97 |
8.62e-03 |
|
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.
Pssm-ID: 128913 Cd Length: 34 Bit Score: 34.72 E-value: 8.62e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
165-518 |
8.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 165 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQT-QKEISELRYE 243
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAElEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 244 LERTHQAkaealVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFE-------ITQKLQEEKN 316
Cdd:COG4717 222 LEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllALLFLLLARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 317 KTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIArtnkVTEDEKKNKEkamlLREEAVAVNSKKEELKQAVS 396
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE----LLELLDRIEE----LQELLREAEELEEELQLEEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 397 RTKELEL-------DLESVKAQVLLVNKQNQlLTEKLKEVSDY--PLLKEEKLELQVQNK-LLRQQLDETRTENQHLRDK 466
Cdd:COG4717 369 EQEIAALlaeagveDEEELRAALEQAEEYQE-LKEELEELEEQleELLGELEELLEALDEeELEEELEELEEELEELEEE 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2024343399 467 LSQPSAEHLACQAELRKVEHSRRLvmDEFESHKQFLEKQLQSEVERSAQLKT 518
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-336 |
8.91e-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: 40.04 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 164 RESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYE 243
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 244 LERTHQAKAEALVS----------REKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQR-----------I 302
Cdd:TIGR02168 913 LRRELEELREKLAQlelrleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgpvnlaaI 992
|
170 180 190
....*....|....*....|....*....|....
gi 2024343399 303 EAFEITQKLQEEKNKTIDDALRrrevAVKNIEET 336
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTE----AKETLEEA 1022
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
203-549 |
9.66e-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: 39.95 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 203 EKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELE---------------RTHQAKAEALVSREKNAIERLQ 267
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEelraqeavleetqerINRARKAAPLAAHIKAVTQIEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 268 KQQEI--EAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYD----QKL 341
Cdd:TIGR00618 308 QAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihtlQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 342 KTELLKYQLELKEEYIARTNKV----TEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 417
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQatidTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 418 QNQlLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLD-----ETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvm 492
Cdd:TIGR00618 468 LKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPcplcgSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE-- 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343399 493 defeshkQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 549
Cdd:TIGR00618 545 -------EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
192-291 |
9.92e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.47 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 192 EGKLHEYRKEIEKQLQAEMSQKLqhfKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVSREKNAIERLQK 268
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAERE---REIELQEKEAEREEAELEADVRKPAEAEKQaaeAEAEAEAEAIRAKGLAEAEGK 343
|
90 100
....*....|....*....|...
gi 2024343399 269 QQEIEAKEVYAQRQSLLKDIEVM 291
Cdd:COG2268 344 RALAEAWNKLGDAAILLMLIEKL 366
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
247-549 |
9.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 247 THQAKAEALVSRE--KNAIERLQKQQEIEA-----KEVYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTi 319
Cdd:PRK11281 27 ARAASNGDLPTEAdvQAQLDALNKQKLLEAedklvQQDLEQTLALLDKIDRQKEETEQLKQQLA--QAPAKLRQAQAEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 320 dDALRRREVAVKNieetydQKLKTELLKyQLElkeeyiARTNKVTEDEKKnkekamlLREEAVAVNSkkeelkQAVSRTK 399
Cdd:PRK11281 104 -EALKDDNDEETR------ETLSTLSLR-QLE------SRLAQTLDQLQN-------AQNDLAEYNS------QLVSLQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 400 ELEldlesvKAQVLLVNKQNQL--LTEKLKEVSD--YPLLKEEKLELQVQNKLLRQQLDETRTE---NQHLRDKLSQPSA 472
Cdd:PRK11281 157 QPE------RAQAALYANSQRLqqIRNLLKGGKVggKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQDLLQKQRD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343399 473 EHLACQAELRK-------VEHSRRLVMDEfESHKQFLEKQ----------LQSEVERSAQLKTQLLdsEATvRKLNVQVE 535
Cdd:PRK11281 231 YLTARIQRLEHqlqllqeAINSKRLTLSE-KTVQEAQSQDeaariqanplVAQELEINLQLSQRLL--KAT-EKLNTLTQ 306
|
330 340
....*....|....*....|.
gi 2024343399 536 DlKLQLK-------QTQAALE 549
Cdd:PRK11281 307 Q-NLRVKnwldrltQSERNIK 326
|
|
| |
