|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-349 |
2.49e-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: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 84 SLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQ 163
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 164 SLETQIAkwNLQVKMNKQEAVAIKEASRQKAVALKKASKvyRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQF 243
Cdd:TIGR02168 751 QLSKELT--ELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 244 EKIAIEKTELEVQIETMKKQIANLLEDLRKME---THGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASV 320
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260
....*....|....*....|....*....
gi 1907151271 321 ENELVELQEVEKRQKTLVEGYRTQVQKLQ 349
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-460 |
2.58e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 123 EKESALKANRLSQSVKVVHDRLQ-RQIQKREAENEKLKEHVQSLETQIAKWNLQVkmnkQEAVAIKEASRQKAVALKKAS 201
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 202 KVYRQRLRHFTGDIERLASQVRDQEAKLSEtvsassdwksqfekIAIEKTELEVQIETMKKQIANLLEDLrkmethgkns 281
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEEL---------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 282 cEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKN 361
Cdd:COG1196 340 -EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 362 LLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEenhliqlkcENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEK 441
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|....*....
gi 1907151271 442 AAEYTALSRQLEAALEEGR 460
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-488 |
1.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 165 LETQIAKWNLQVKMNKQEAVAikEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFE 244
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 245 KIAIEKTELEVQIETMKKQIANLLEDLrkmethgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENEL 324
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 325 VELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLltKLSLEEENHLIQLKCE 404
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE--RASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 405 NLKEKLEQMDAENKELEKKLADQEEclKHSDLELKEKAAEYTaLSRQLEAALEEGR---QKVSEEVEKMSSRERALQIKI 481
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELRE--KLAQLELRLEGLEVR-IDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRL 974
|
....*..
gi 1907151271 482 LDLEAEL 488
Cdd:TIGR02168 975 KRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-474 |
3.29e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 120 FQNEKESALK----ANRLSQSVKVVHDRLQRQIQKREAENEKlKEHVQSLETQIAKWNLQVKMNKqeavaIKEASRQKAV 195
Cdd:TIGR02169 168 FDRKKEKALEeleeVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKE-----KEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 196 ALKKASKVyRQRLRHFTGDIERLASQVRDQEAKLSEtVSASSDWKSQFEKIAIEKT--ELEVQIETMKKQIANLLEDLRK 273
Cdd:TIGR02169 242 IERQLASL-EEELEKLTEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKigELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 274 METHGKNSCEEI---LRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELvelQEVEKRQKTLvegyRTQVQKLQE 350
Cdd:TIGR02169 320 AEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAET----RDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 351 AAEMVKSRCKNLLHENNLIITNKNKKLEKV-DGNQSLLTKLS----LEEENHLIQLKCENLKEKLEQMDAENKELEKKLA 425
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELaDLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907151271 426 DQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRE 474
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-535 |
8.69e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 310 LDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEmvksRCKNLLHENNLIITNKNKKLEKVDGNQSLLTK 389
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 390 LSLEEENHLIQLK--CENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEV 467
Cdd:COG1196 310 RRRELEERLEELEeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151271 468 EKMSSRERALQiKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQ 535
Cdd:COG1196 390 EALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-490 |
3.28e-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: 50.07 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 205 RQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKME--------- 275
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkse 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 276 -THGKNSCEEILRKLHSLEDENEALNIENV-----KLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQ 349
Cdd:TIGR02169 760 lKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 350 EAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLtkLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLadqeE 429
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL--RDLESRLGDLKKERDELEAQLRELERKIEELEAQI----E 913
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907151271 430 CLKHSDLELKEKAAeytALSRQLEAALEEGRQKVSEEVEKMSsrERALQIKILDLEAELRK 490
Cdd:TIGR02169 914 KKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-455 |
5.93e-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: 49.28 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 214 DIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLE 293
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 294 DENEALNienvklkgtldALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLI---I 370
Cdd:TIGR02168 334 ELAEELA-----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 371 TNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSR 450
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
....*
gi 1907151271 451 QLEAA 455
Cdd:TIGR02168 483 ELAQL 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
89-485 |
1.37e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 89 LKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQ---------RQIQKREAENEK-- 157
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKeleekeerlEELKKKLKELEKrl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 158 --LKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSA 235
Cdd:PRK03918 355 eeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 236 S-------------------SDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNscEEILRKLHSLEDEN 296
Cdd:PRK03918 435 KgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 297 EALNIENV--------KLKGTLDALKDEVASVENELVELQEVEKRQKTLVEgyrtQVQKLQEAAEMVKSRCKNLLHENNL 368
Cdd:PRK03918 513 KKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 369 IITNKNKKLEKV--DGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLK-HSDLELKEKAAEY 445
Cdd:PRK03918 589 ELEERLKELEPFynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEY 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907151271 446 TALSRQLEAA------LEEGRQKVSEEVEKMSSRERALQIKILDLE 485
Cdd:PRK03918 669 LELSRELAGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
305-498 |
1.98e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 305 KLKGTLDALKDEVAsvENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEmvksrcknllhENNLIITNKNKKLEKVDGNQ 384
Cdd:COG1196 224 ELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELE-----------ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 385 SLLTK--LSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEEclkhSDLELKEKAAEYTALSRQLEAALEEGRQK 462
Cdd:COG1196 291 YELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907151271 463 VSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 498
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-526 |
2.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 249 EKTELEVQIETMKKQIANLLEDLRKMEThgknsceeILRKLHSLEDENEALN--IENVKLKGTLDALKDEVASVENELvE 326
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALED--------AREQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQR-R 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 327 LQEVEKRQKTLvegyRTQVQKLQEAAEMVKSRCKNLLhennliitnknkklEKVDGNQSLLTKLSLEEEnhliqlkcENL 406
Cdd:COG4913 290 LELLEAELEEL----RAELARLEAELERLEARLDALR--------------EELDELEAQIRGNGGDRL--------EQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 407 KEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQikilDLEA 486
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRR 419
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907151271 487 ELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETR 526
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
108-351 |
4.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 108 EKETYIRELSCLFQNEKESALKANRLSQSVkvvhdrLQRQIQKREAENEKLkehVQSLETQIAKwnLQVKMNKQEAVAIK 187
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAEAY------LEQNLELRREEARKA---LEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 188 EASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSE-------------TVSAS---SDWKSQFEKIAIEKT 251
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraqlgsgpdalpELLQSpviQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 252 ELEV-------QIETMKKQIANLLEDLRkmethgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENEL 324
Cdd:COG3206 281 ELSArytpnhpDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*..
gi 1907151271 325 VELQEVEKRQKTLVEGYRTQVQKLQEA 351
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-494 |
5.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 247 AIEKTELEVQIETMKKQIANLLEDLRKMethgKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVE 326
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 327 LQEVEKRQKtlvegyrtqvqklQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDgNQSLLTKLSLEEENHLIQLK--CE 404
Cdd:COG4942 95 LRAELEAQK-------------EELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRadLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 405 NLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKaaeytalsRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDL 484
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAER--------QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|
gi 1907151271 485 EAELRKKNEE 494
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-541 |
8.85e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 88 LLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDR---LQRQIQKREAENEKLKEHVQS 164
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 165 LETQIAKWNLQVKMNKQEAVAIKE--ASRQKAVALKKASKVYRQRLRhftgDIERLASQVRDQEAKLSETVSASSDWKSQ 242
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELR----EIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 243 FEKIAIEKTELEVQIETMKK------QIANLLEDLRKMETH-GKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKD 315
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 316 EVASVENELVELQEV------------EKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENnliitnknKKLEKVDGN 383
Cdd:PRK03918 420 EIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL--------RELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 384 QSLLTKL--------SLEEENHLIQLK--------CENLKEKLEQMDAENKELEKKLADQEEcLKHSDLELKEKAAEyta 447
Cdd:PRK03918 492 ESELIKLkelaeqlkELEEKLKKYNLEelekkaeeYEKLKEKLIKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDE--- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 448 LSRQLEAALEEGRQKVSEEVEKMSSRERALQ------IKILDLEAELRKKNEEQNQLVDKmntktqhqaicLKEIQHSLE 521
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE-----------LDKAFEELA 636
|
490 500
....*....|....*....|
gi 1907151271 522 KSETRNESIKNYLQFLQISY 541
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKY 656
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
327-493 |
1.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 327 LQEVEKRQKTLVEGYRTQVQKLQEAAEM-VKSRCKNLLHENNLIITNKNKKLEKVdgnqslltklsleeENHLIQlKCEN 405
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKL--------------EKRLLQ-KEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 406 LKEKLEQMDAENKELEKKladqEECLKHSDLELKEKAAEYTALSRQLEAALE--------EGRQKVSEEVEKMSSRERAL 477
Cdd:PRK12704 98 LDRKLELLEKREEELEKK----EKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAV 173
|
170
....*....|....*.
gi 1907151271 478 QIKILDLEAELRKKNE 493
Cdd:PRK12704 174 LIKEIEEEAKEEADKK 189
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-501 |
1.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 123 EKESALKANRLSQSVKVVHDRLQRQIQKREAEN------EKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVA 196
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkkaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 197 LKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEkiaIEKTELEVQIETMKKQIANLLEDLRKmet 276
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRK--- 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 277 hgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENElvELQEVEKRQKTLVEGYRTQVQKLQEAAEMVK 356
Cdd:PTZ00121 1583 ------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 357 SRcknllhENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQ--LKCENLKEKLEQM---DAENKELEKKLADQEECL 431
Cdd:PTZ00121 1655 AE------EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalKKEAEEAKKAEELkkkEAEEKKKAEELKKAEEEN 1728
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 432 KHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDK 501
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
262-545 |
1.33e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 262 KQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEV------ASVENELVELQEVEKRQK 335
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiylqsaQRVELAERQLQELKIDVK 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 336 TLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLI---ITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQ 412
Cdd:COG5022 893 SISSLKLVNLELESEIIELKKSLSSDLIENLEFKtelIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 413 MDAENKELEKKladqEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQkvSEEVEKMSSRERALQIKILDLEAELRKKN 492
Cdd:COG5022 973 YEDLLKKSTIL----VREGNKANSELKNFKKELAELSKQYGALQESTKQ--LKELPVEVAELQSASKIISSESTELSILK 1046
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151271 493 EEQNQ--LVDKMNTKTQHQAICL---KEIQHSLEKSETRNESIKNYLQFLQISYVTMF 545
Cdd:COG5022 1047 PLQKLkgLLLLENNQLQARYKALklrRENSLLDDKQLYQLESTENLLKTINVKDLEVT 1104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
18-534 |
2.12e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 18 LIRERGSAPQCAPEKHLSRLKQDVANTKMELKATLK---------EAQLASCSVELLLPLFKNTVEGISLENIGDSLLCL 88
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRmyedkieelEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 89 LKDLSDNESE-------NRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKV-VHDRLQRQIQKREAENEKLkE 160
Cdd:pfam15921 383 LADLHKREKElslekeqNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNESL-E 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 161 HVQSLETQIAKWNLQVKMNKQEAVAIK---EASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASS 237
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 238 ---DWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKmetHGKNSCEEILRKLHSLEDENEA-LNIENVK-LKGTLDA 312
Cdd:pfam15921 542 hlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ---HGRTAGAMQVEKAQLEKEINDRrLELQEFKiLKDKKDA 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 313 ----LKDEVASVENELVEL-----------QEVEKRQKTL---VEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIiTNKN 374
Cdd:pfam15921 619 kireLEARVSDLELEKVKLvnagserlravKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT-TNKL 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 375 K---KLEKVDGNQSLLTKLSLE-EENHLIQLKC---ENLKEKLEQMDAenkeLEKKLADQEECLKHSDLELKEKAAEYTA 447
Cdd:pfam15921 698 KmqlKSAQSELEQTRNTLKSMEgSDGHAMKVAMgmqKQITAKRGQIDA----LQSKIQFLEEAMTNANKEKHFLKEEKNK 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 448 LSRQLEAALEEgRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQhQAICLKeIQHSLEKSE--- 524
Cdd:pfam15921 774 LSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ-ESVRLK-LQHTLDVKElqg 850
|
570
....*....|...
gi 1907151271 525 ---TRNESIKNYL 534
Cdd:pfam15921 851 pgyTSNSSMKPRL 863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-498 |
2.18e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 279 KNSCEEILRKLHSLEDENEALNIEnvklkgtLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 358
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 359 CKNLLHENNLIITNKNKKLEKVDGNQSLL-----TKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKH 433
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151271 434 SDLELKEKAAEYTALSRQLEaaleegrqKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 498
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIE--------ELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-358 |
2.51e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 183 AVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKK 262
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 263 QIANLLED----LRKMETHGKNSCEEIL----------RKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQ 328
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLlspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190
....*....|....*....|....*....|
gi 1907151271 329 EVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 358
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-537 |
3.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 112 YIRELSCLFQNEKESALKANRLsQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASR 191
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAEL-EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 192 QKavaLKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKiaiEKTELEVQIETMKKQIANLLEDL 271
Cdd:COG4913 355 EE---RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 272 RKMETHGKNsceeILRKLHSLEDE-NEALNIENVKLKgtldalkdeVASvenELVELQEVEKRQKTLVEGY-RTQ----- 344
Cdd:COG4913 429 ASLERRKSN----IPARLLALRDAlAEALGLDEAELP---------FVG---ELIEVRPEEERWRGAIERVlGGFaltll 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 345 --VQKLQEAAEMVKSR-CKNLLHENNLIITNKNKKLEKVDGNqSLLTKLSLEE-------ENHLIQ----LKCENLKE-- 408
Cdd:COG4913 493 vpPEHYAAALRWVNRLhLRGRLVYERVRTGLPDPERPRLDPD-SLAGKLDFKPhpfrawlEAELGRrfdyVCVDSPEElr 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 409 ---------------------------------------KLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALS 449
Cdd:COG4913 572 rhpraitragqvkgngtrhekddrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 450 R------------QLEAALEEGRQKVsEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQ 517
Cdd:COG4913 652 RlaeyswdeidvaSAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
490 500
....*....|....*....|
gi 1907151271 518 HSLEKSETRNESIKNYLQFL 537
Cdd:COG4913 731 ELQDRLEAAEDLARLELRAL 750
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
78-541 |
4.79e-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: 43.09 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 78 LENIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESalKANRLSQSVKVVHDRLQRQIQKREAENEK 157
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 158 LKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRhftgDIERLASQVRDQEAKLSETVSASS 237
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ----EIKNLESQINDLESKIQNQEKLNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 238 DWKSQFEKIAIEKTELEVQIETMKKQI---ANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALK 314
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIiknNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 315 DEVASVENELVELqeveKRQKTLVEGyrtQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLEE 394
Cdd:TIGR04523 489 KELKSKEKELKKL----NEEKKELEE---KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 395 EnhliqlkCENLKEKLEQMDAENKELEKKLADQEEclkhsdlELKEKAAEYTALSRQLEaALEEGRQKVSEEVEKMSSRE 474
Cdd:TIGR04523 562 E-------IDEKNKEIEELKQTQKSLKKKQEEKQE-------LIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKEN 626
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907151271 475 RALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQISY 541
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHY 693
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
83-322 |
5.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 83 DSLLCLLKDLSDNESENRNLEEKV--LEKetyIRELSCLFQNEKESALKANRLSQsvKVVHDRLQRQIQKREAENEKLKE 160
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIelLEP---IRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 161 HVQSLETQIAkwnlqvkmnkqeavaikEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWK 240
Cdd:COG4913 303 ELARLEAELE-----------------RLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 241 SQFEKIAIEKTELEVQIETMKKQIANLLEDLrkmethgknscEEILRKLHSLEDENEAlniENVKLKGTLDALKDEVASV 320
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEAL-----------EEELEALEEALAEAEA---ALRDLRRELRELEAEIASL 431
|
..
gi 1907151271 321 EN 322
Cdd:COG4913 432 ER 433
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
68-500 |
7.92e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 68 LFKNTVEGISLENIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELS-CLFQNEKESALKANRLSQSVKVVHDRLQR 146
Cdd:PRK01156 154 ILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKkQIADDEKSHSITLKEIERLSIEYNNAMDD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 147 QIQKREAENE--KLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHF------TGDIERL 218
Cdd:PRK01156 234 YNNLKSALNElsSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkykndIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 219 ASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEvqieTMKKQIANLLEDLRKMETHgKNSCEEILRKLHSLEDENEA 298
Cdd:PRK01156 314 LSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD----DLNNQILELEGYEMDYNSY-LKSIESLKKKIEEYSKNIER 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 299 LNIENVKLKGTLDALKDEVASVENEL-VELQEVEKRQKTLVEGYRTQVQKLQEA---AEMVKSR-----CKNLLHEN--N 367
Cdd:PRK01156 389 MSAFISEILKIQEIDPDAIKKELNEInVKLQDISSKVSSLNQRIRALRENLDELsrnMEMLNGQsvcpvCGTTLGEEksN 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 368 LIITNKNKKL----EKVDGNQSLLTKLSlEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEEcLKHSDLELKEKAA 443
Cdd:PRK01156 469 HIINHYNEKKsrleEKIREIEIEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKINELKDKHD 546
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151271 444 EYTALSRQLEAA-LEEGRQKVSEEVEKMSsreralQIKILDLEAELRKKNEEQNQLVD 500
Cdd:PRK01156 547 KYEEIKNRYKSLkLEDLDSKRTSWLNALA------VISLIDIETNRSRSNEIKKQLND 598
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
31-362 |
1.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 31 EKHLSRLKQDVANTKMELKATLKEAQLASCSVELL------LPLFKNTVEGIsLENIGDSLLCLLKDLSDNESENRNLEE 104
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqLEQEEEKLKER-LEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 105 KVLEKETYI----RELSCLFQNEKESALK-ANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIakwnlQVKMN 179
Cdd:TIGR02169 766 RIEELEEDLhkleEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-----QELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 180 KQEAVAIKEASRQKAVALKKAskvyrqRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIET 259
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 260 MKKQIANLLEDLRKMETHGKnsceEILRKLHSLEDENEALNIENvKLKGTLDALKDEVASVE--NELV--ELQEVEKRQK 335
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEpvNMLAiqEYEEVLKRLD 989
|
330 340
....*....|....*....|....*..
gi 1907151271 336 TLVEgyrtQVQKLQEAAEMVKSRCKNL 362
Cdd:TIGR02169 990 ELKE----KRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-507 |
1.15e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 71 NTVEGISLENIGDSLLCLLKDLsdnESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRlsqsvkvvhDRLQRQIQK 150
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILREL---DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQ---------DRIEQLISE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 151 REAENEKLKEHVQSLETQIAKWNLQVKMNKQEAvaikeasrqkavalKKASKVYRQRLRHFTGDIERLASQVRDQ----E 226
Cdd:pfam15921 276 HEVEITGLTEKASSARSQANSIQSQLEIIQEQA--------------RNQNSMYMRQLSDLESTVSQLRSELREAkrmyE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 227 AKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMEthgknsceeilRKLHSLEDENEALNIENVKL 306
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE-----------KELSLEKEQNKRLWDRDTGN 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 307 KGTLDALKDEVasvenelvelqevekrqktlvEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSL 386
Cdd:pfam15921 411 SITIDHLRREL---------------------DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 387 L----------------TKLSLEEENHLIQLKCENLKEKLEQMDAENKELEK-----KLADQE-ECLKHSDLELKEKAAE 444
Cdd:pfam15921 470 LestkemlrkvveeltaKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvDLKLQElQHLKNEGDHLRNVQTE 549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907151271 445 YTALSRQL---EAALEEGRQKVSEEVEKMSSRER---ALQIKILDLEAELRKKNEEQNQ---LVDKMNTKTQ 507
Cdd:pfam15921 550 CEALKLQMaekDKVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIR 621
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
90-476 |
1.36e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 90 KDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSqsvkvvhdrlqrqIQKREAENEKLKEHVQSLETQI 169
Cdd:PLN02939 57 KQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRAS-------------MQRDEAIAAIDNEQQTNSKDGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 170 AKWNLQVkmnkQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETvSASSDWKSQfEKIAIE 249
Cdd:PLN02939 124 QLSDFQL----EDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSET-DARIKLAAQ-EKIHVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 250 KteLEVQIETMKKQIANLLEDLRKMEthgknsceeilrklHSLEDENEALNIENVKLKGTLDALKDevasvenELVELQE 329
Cdd:PLN02939 198 I--LEEQLEKLRNELLIRGATEGLCV--------------HSLSKELDVLKEENMLLKDDIQFLKA-------ELIEVAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 330 VEKRqktlvegyrtqVQKLQEAAEMVKSRCKNLlhENNLIITNKN-KKL---------EKVDGNQSLLTKLSLEEENHLI 399
Cdd:PLN02939 255 TEER-----------VFKLEKERSLLDASLREL--ESKFIVAQEDvSKLsplqydcwwEKVENLQDLLDRATNQVEKAAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 400 QL-KCENLKEKLEQMDAENKE-------------LEKKLADQEECLKHSDLELKekaaEYTALSRQLEAALEEGRQKVSE 465
Cdd:PLN02939 322 VLdQNQDLRDKVDKLEASLKEanvskfssykvelLQQKLKLLEERLQASDHEIH----SYIQLYQESIKEFQDTLSKLKE 397
|
410
....*....|.
gi 1907151271 466 EVEKMSSRERA 476
Cdd:PLN02939 398 ESKKRSLEHPA 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
20-510 |
1.69e-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: 41.49 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 20 RERGSAPQCAPEKHLSRLKQDVANTKMELKATLKEAQLASCSVELLLPLFKNTVEGISLENIGDSLLCLLKDLSDNESEN 99
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 100 RNLEEKVLEKETYIRELsclfQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKwnlqvkmn 179
Cdd:TIGR00618 368 REISCQQHTLTQHIHTL----QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL-------- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 180 KQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETvsassdwKSQFEKIAIEKTELEVQIET 259
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK-------KAVVLARLLELQEEPCPLCG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 260 MKKQIANLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVE 339
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPL-TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 340 GYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLE--EENHLIQLKCENLKEKLEQMDAEN 417
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELalKLTALHALQLTLTQERVREHALSI 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 418 KELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQ 497
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
490
....*....|...
gi 1907151271 498 LVDKMNTKTQHQA 510
Cdd:TIGR00618 748 LMHQARTVLKART 760
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
402-503 |
1.93e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 402 KCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEkaaeytalsrqleaALEEGRQKVSEEvEKMSSRERalqiKI 481
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90 100
....*....|....*....|..
gi 1907151271 482 LDLEAELRKKNEEQNQLVDKMN 503
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
83-493 |
1.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 83 DSLLCLLKDLSDNESEnrnLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHV 162
Cdd:PRK02224 310 EAVEARREELEDRDEE---LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 163 QSLETQIAkwnlqvkmNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRD------------------ 224
Cdd:PRK02224 387 EELEEEIE--------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 225 QEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIaNLLEDLRKMEthgknsceeilRKLHSLEDENEALNIENV 304
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAE-----------DRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 305 KLKGTLDALKDEVASVENELVELqEVEKRQKtlvegyRTQVQKLQEAAEMVKSRCKNLlhennliitnkNKKLEKVDGNQ 384
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAEL-EAEAEEK------REAAAEAEEEAEEAREEVAEL-----------NSKLAELKERI 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 385 SLLTKL--SLEEENHLIQlKCENLKEKLEQMDAENKELEKKLADQEEclKHSDLELKEKAAEYTALSRQLEAAlEEGRQK 462
Cdd:PRK02224 589 ESLERIrtLLAAIADAED-EIERLREKREALAELNDERRERLAEKRE--RKRELEAEFDEARIEEAREDKERA-EEYLEQ 664
|
410 420 430
....*....|....*....|....*....|.
gi 1907151271 463 VSEEVEKMSSRERALQIKILDLEAELRKKNE 493
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
89-502 |
2.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 89 LKDLSDNESENRNLEEKVLEKETYIRELSclfqnEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQ 168
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELE-----AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 169 IAKW-NLQVKMNKQEAvAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQfekia 247
Cdd:COG4717 155 LEELrELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 248 IEKTELEVQIETMKKQIANLLEDLRkmethgknsceeILRKLHSLEDENEALNIENVKLKGTLdALKDEVASVENELVEL 327
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLL------------IAAALLALLGLGGSLLSLILTIAGVL-FLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 328 QEVEKRQKTLVEGYRTQVQKLQEaaEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLK 407
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 408 EKLEQMDAENKELEKKLADQEEclkhsdlELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKmssrerALQIKILDLEAE 487
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAE-------EYQELKEELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEE 440
|
410
....*....|....*
gi 1907151271 488 LRKKNEEQNQLVDKM 502
Cdd:COG4717 441 LEELEEELEELREEL 455
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
406-489 |
2.67e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.06 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 406 LKEKLEQMDAENKELEKKLA------DQEECLK----HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRE 474
Cdd:PRK00591 4 MLDKLEALEERYEELEALLSdpevisDQKRFRKlskeYAELEpIVEAYREYKQAQEDLEEAKEMLEEESDPEMREMAKEE 83
|
90
....*....|....*.
gi 1907151271 475 -RALQIKILDLEAELR 489
Cdd:PRK00591 84 lKELEERLEELEEELK 99
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-467 |
5.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 284 EILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKsrcknll 363
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 364 heNNLIITNKNKKLEKVDGNQSLLTKLSLEeenhliqlkcenLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAA 443
Cdd:COG1579 87 --NNKEYEALQKEIESLKRRISDLEDEILE------------LMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....
gi 1907151271 444 EYTALSRQLEAALEEGRQKVSEEV 467
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-531 |
5.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 94 DNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSvkvvhDRLQRQIQKREAENEKLKEHVQSLE-----TQ 168
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-----DELKKAEEKKKADEAKKAEEKKKADeakkkAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 169 IAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAi 248
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK- 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 249 EKTELEVQIETMKKQIANL--LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVE 326
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 327 LQEVEKR--QKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSllTKLSLEEENHLIQLKCE 404
Cdd:PTZ00121 1472 ADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 405 NLKEKLEQMDAEnkelEKKLADQeeclKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSrERALQIKILDL 484
Cdd:PTZ00121 1550 ELKKAEELKKAE----EKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKI 1620
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907151271 485 EAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIK 531
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
283-429 |
5.59e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 283 EEILRKLHSLEDENEALNIE-NVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKN 361
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151271 362 LLHENNLIITNKNKKLEKVDGNQ-----SLLT-----KLsLEEEnhliqlkcenlKEKLEQMDaenKELEKKLADQEE 429
Cdd:COG0542 494 LAELEEELAELAPLLREEVTEEDiaevvSRWTgipvgKL-LEGE-----------REKLLNLE---EELHERVIGQDE 556
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
405-489 |
5.74e-03 |
|
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439986 [Multi-domain] Cd Length: 356 Bit Score: 39.21 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 405 NLKEKLEQMDAENKELEKKLADQE---------ECLK-HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSR 473
Cdd:COG0216 1 SMLDKLEALEERYEELEALLSDPEvisdqkrfrKLSKeYAELEpIVEAYREYKKLLEDIEEAKELLEEESDPEMREMAKE 80
|
90
....*....|....*..
gi 1907151271 474 E-RALQIKILDLEAELR 489
Cdd:COG0216 81 ElEELEARLEELEEELK 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-531 |
5.80e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 91 DLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETqiA 170
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA--A 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 171 KWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQrlrhfTGDIERLASQVRD--------QEAKLSETVSASSDWKSQ 242
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK-----ADEAKKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 243 FEKiAIEKTELEVQIETMKKQI--ANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVK----LKGTLDALKDE 316
Cdd:PTZ00121 1459 AEE-AKKKAEEAKKADEAKKKAeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeAKKAEEAKKAD 1537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 317 VASVENELVELQEVEK--------------RQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLH----------------EN 366
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKaeelkkaeekkkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyeeekkmkaeeakkaEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 367 NLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEecLKHSDlELKEKAAEYT 446
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAE-EDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 447 ALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEaELRKKNEEQNQLVDKMNTKTQHQaiclKEIQHSLEKSETR 526
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKK 1769
|
....*
gi 1907151271 527 NESIK 531
Cdd:PTZ00121 1770 AEEIR 1774
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
175-494 |
5.85e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.28 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 175 QVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELE 254
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 255 VQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI---ENVKLKGTLDALKDEVASVENELVELQEVE 331
Cdd:pfam19220 125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALleqENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 332 KRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCE------N 405
Cdd:pfam19220 205 DATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAiraaerR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 406 LKE---KLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQL---EAALEEGRQKVSEEVEKMSSRERALQI 479
Cdd:pfam19220 285 LKEasiERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALaakDAALERAEERIASLSDRIAELTKRFEV 364
|
330
....*....|....*
gi 1907151271 480 KILDLEAELRKKNEE 494
Cdd:pfam19220 365 ERAALEQANRRLKEE 379
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-502 |
6.84e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 244 EKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLK----GTLDALKDEVAS 319
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 320 VENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHEnnliITNKNKKLEKvdgnqslltklsLEEENHLI 399
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDK------------LTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 400 QLKCENLKEKLEQMDAENKELEKKLADQE---ECLKHSDLELKEKAAEYTALSRQLEAALEEGRQkvseEVEKMSSRERA 476
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINE 438
|
250 260
....*....|....*....|....*.
gi 1907151271 477 LQIKILDLEAELRKKNEEQNQLVDKM 502
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
142-353 |
7.57e-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: 38.98 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 142 DRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKmnkqeavaikeASRQKAVALKKASKVYRQRLRHFTGDIERLASQ 221
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----------ALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151271 222 VRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMEthgknscEEILRKLHSLEDENEALNI 301
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907151271 302 ENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAE 353
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| |
