|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-392 |
2.10e-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: 57.37 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 127 SLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQ 206
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 207 SLETQIAkwNLQVKMNKQEAVAIKEASRQKAVALKKASKvyRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQF 286
Cdd:TIGR02168 751 QLSKELT--ELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 287 EKIAIEKTELEVQIETMKKQIANLLEDLRKME---THGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASV 363
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260
....*....|....*....|....*....
gi 1907151264 364 ENELVELQEVEKRQKTLVEGYRTQVQKLQ 392
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-503 |
2.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 166 EKESALKANRLSQSVKVVHDRLQ-RQIQKREAENEKLKEHVQSLETQIAKWNLQVkmnkQEAVAIKEASRQKAVALKKAS 244
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 245 KVYRQRLRHFTGDIERLASQVRDQEAKLSEtvsassdwksqfekIAIEKTELEVQIETMKKQIANLLEDLrkmethgkns 324
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEEL---------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 325 cEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKN 404
Cdd:COG1196 340 -EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 405 LLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEenhliqlkcENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEK 484
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|....*....
gi 1907151264 485 AAEYTALSRQLEAALEEGR 503
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-575 |
7.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 353 LDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEmvksRCKNLLHENNLIITNKNKKLEKVDGNQSLLTK 432
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 433 LSLEEENHLIQLK--CENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEV 510
Cdd:COG1196 310 RRRELEERLEELEeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151264 511 EKMSSRERALQiKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKN 575
Cdd:COG1196 390 EALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-528 |
1.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 88 LKKIFEQNDILSKELDTFNRVKLALEHLIKQTdyEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEK 167
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIREL--EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 168 ESALKANRLSQSVKVVHDRLQ---------RQIQKREAENEK----LKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASR 234
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeerlEELKKKLKELEKrleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 235 QKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSAS-------------------SDWKSQFEKIAIEKTE 295
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 296 LEVQIETMKKQIANLLEDLRKMETHGKNscEEILRKLHSLEDENEALNIENV--------KLKGTLDALKDEVASVENEL 367
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 368 VELQEVEKRQKTLVEgyrtQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKV--DGNQSLLTKLSLEEENHLIQLK 445
Cdd:PRK03918 549 EKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPFynEYLELKDAEKELEREEKELKKL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 446 CENLKEKLEQMDAENKELEKKLADQEECLK-HSDLELKEKAAEYTALSRQLEAA------LEEGRQKVSEEVEKMSSRER 518
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELE 704
|
490
....*....|
gi 1907151264 519 ALQIKILDLE 528
Cdd:PRK03918 705 EREKAKKELE 714
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-577 |
3.06e-05 |
|
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: 47.04 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 96 DILSKELDTFNRVKLALEHLIKQTDYEQIGDsllcLLKDLSDNESENRNLEEkvleketyIRELSCLFQNEKESALKANR 175
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQ----MERQMAAIQGKNESLEK--------VSSLTAQLESTKEMLRKVVE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 176 LSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIK-------------EASRQKAVALKK 242
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegdhlrnvqtecEALKLQMAEKDK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 243 ASKVYRQRLRHFT---GDIERLASQVRDQEAKLSETVSassDWKSQFEKIAIEKTELEVQIETMKKQIANLleDLRKMET 319
Cdd:pfam15921 563 VIEILRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEIN---DRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKL 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 320 hgKNSCEEILRKLHSLEDENealnienvklkgtlDALKDEVASVENELVELQEvekRQKTLVEGYRTQVQKLQEAAEMVK 399
Cdd:pfam15921 638 --VNAGSERLRAVKDIKQER--------------DQLLNEVKTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKLK 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 400 SRCKNLLHEnnliITNKNKKLEKVDGNQSLLTKLSLEEEnhliqlkcENLKEKLEQMDAenkeLEKKLADQEECLKHSDL 479
Cdd:pfam15921 699 MQLKSAQSE----LEQTRNTLKSMEGSDGHAMKVAMGMQ--------KQITAKRGQIDA----LQSKIQFLEEAMTNANK 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 480 ELKEKAAEYTALSRQLEAALEEgRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQhQAICLKeI 559
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ-ESVRLK-L 839
|
490 500
....*....|....*....|....
gi 1907151264 560 QHSLEKSE------TRNESIKNYL 577
Cdd:pfam15921 840 QHTLDVKElqgpgyTSNSSMKPRL 863
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
370-536 |
1.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 370 LQEVEKRQKTLVEGYRTQVQKLQEAAEM-VKSRCKNLLHENNLIITNKNKKLEKVdgnqslltklsleeENHLIQlKCEN 448
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKL--------------EKRLLQ-KEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 449 LKEKLEQMDAENKELEKKladqEECLKHSDLELKEKAAEYTALSRQLEAALE--------EGRQKVSEEVEKMSSRERAL 520
Cdd:PRK12704 98 LDRKLELLEKREEELEKK----EKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAV 173
|
170
....*....|....*.
gi 1907151264 521 QIKILDLEAELRKKNE 536
Cdd:PRK12704 174 LIKEIEEEAKEEADKK 189
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
322-541 |
2.12e-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: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 322 KNSCEEILRKLHSLEDENEALNIEnvklkgtLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 401
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 402 CKNLLHENNLIITNKNKKLEKVDGNQSLL-----TKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKH 476
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151264 477 SDLELKEKAAEYTALSRQLEaaleegrqKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 541
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIE--------ELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
266-536 |
5.15e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 266 RDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKN---SCEEILRKLHSLEDENEAL 342
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKElsaSSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 343 NIENVKLKGTLDALKDEVASVENELVELQEVEKR---QKTLVEGYRTQVQ-KLQEAAEMVKSRCKNLLHENNLIITNKNK 418
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKagaQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 419 KLEKVDGNQSLLTKLSL----EEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKE---KAAEYTAL 491
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQ 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907151264 492 SRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNE 536
Cdd:pfam07888 288 LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-392 |
2.10e-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: 57.37 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 127 SLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQ 206
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 207 SLETQIAkwNLQVKMNKQEAVAIKEASRQKAVALKKASKvyRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQF 286
Cdd:TIGR02168 751 QLSKELT--ELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 287 EKIAIEKTELEVQIETMKKQIANLLEDLRKME---THGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASV 363
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260
....*....|....*....|....*....
gi 1907151264 364 ENELVELQEVEKRQKTLVEGYRTQVQKLQ 392
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-503 |
2.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 166 EKESALKANRLSQSVKVVHDRLQ-RQIQKREAENEKLKEHVQSLETQIAKWNLQVkmnkQEAVAIKEASRQKAVALKKAS 244
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 245 KVYRQRLRHFTGDIERLASQVRDQEAKLSEtvsassdwksqfekIAIEKTELEVQIETMKKQIANLLEDLrkmethgkns 324
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEEL---------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 325 cEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKN 404
Cdd:COG1196 340 -EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 405 LLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEenhliqlkcENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEK 484
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|....*....
gi 1907151264 485 AAEYTALSRQLEAALEEGR 503
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-531 |
1.13e-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: 55.06 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 208 LETQIAKWNLQVKMNKQEAVAikEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFE 287
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 288 KIAIEKTELEVQIETMKKQIANLLEDLrkmethgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENEL 367
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 368 VELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLltKLSLEEENHLIQLKCE 447
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE--RASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 448 NLKEKLEQMDAENKELEKKLADQEEclKHSDLELKEKAAEYTaLSRQLEAALEEGR---QKVSEEVEKMSSRERALQIKI 524
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELRE--KLAQLELRLEGLEVR-IDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRL 974
|
....*..
gi 1907151264 525 LDLEAEL 531
Cdd:TIGR02168 975 KRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-517 |
2.66e-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: 53.92 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 163 FQNEKESALK----ANRLSQSVKVVHDRLQRQIQKREAENEKlKEHVQSLETQIAKWNLQVKMNKqeavaIKEASRQKAV 238
Cdd:TIGR02169 168 FDRKKEKALEeleeVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKEKREYEGYELLKE-----KEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 239 ALKKASKVyRQRLRHFTGDIERLASQVRDQEAKLSEtVSASSDWKSQFEKIAIEKT--ELEVQIETMKKQIANLLEDLRK 316
Cdd:TIGR02169 242 IERQLASL-EEELEKLTEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKigELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 317 METHGKNSCEEI---LRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELvelQEVEKRQKTLvegyRTQVQKLQE 393
Cdd:TIGR02169 320 AEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAET----RDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 394 AAEMVKSRCKNLLHENNLIITNKNKKLEKV-DGNQSLLTKLS----LEEENHLIQLKCENLKEKLEQMDAENKELEKKLA 468
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELaDLNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907151264 469 DQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRE 517
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-575 |
7.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 353 LDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEmvksRCKNLLHENNLIITNKNKKLEKVDGNQSLLTK 432
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 433 LSLEEENHLIQLK--CENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEV 510
Cdd:COG1196 310 RRRELEERLEELEeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151264 511 EKMSSRERALQiKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKN 575
Cdd:COG1196 390 EALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-528 |
1.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 88 LKKIFEQNDILSKELDTFNRVKLALEHLIKQTdyEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEK 167
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIREL--EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 168 ESALKANRLSQSVKVVHDRLQ---------RQIQKREAENEK----LKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASR 234
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeerlEELKKKLKELEKrleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 235 QKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSAS-------------------SDWKSQFEKIAIEKTE 295
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 296 LEVQIETMKKQIANLLEDLRKMETHGKNscEEILRKLHSLEDENEALNIENV--------KLKGTLDALKDEVASVENEL 367
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKEL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 368 VELQEVEKRQKTLVEgyrtQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKV--DGNQSLLTKLSLEEENHLIQLK 445
Cdd:PRK03918 549 EKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPFynEYLELKDAEKELEREEKELKKL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 446 CENLKEKLEQMDAENKELEKKLADQEECLK-HSDLELKEKAAEYTALSRQLEAA------LEEGRQKVSEEVEKMSSRER 518
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELE 704
|
490
....*....|
gi 1907151264 519 ALQIKILDLE 528
Cdd:PRK03918 705 EREKAKKELE 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-533 |
2.30e-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: 50.84 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 248 RQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKME--------- 318
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkse 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 319 -THGKNSCEEILRKLHSLEDENEALNIENV-----KLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQ 392
Cdd:TIGR02169 760 lKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 393 EAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLtkLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLadqeE 472
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL--RDLESRLGDLKKERDELEAQLRELERKIEELEAQI----E 913
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907151264 473 CLKHSDLELKEKAAeytALSRQLEAALEEGRQKVSEEVEKMSsrERALQIKILDLEAELRK 533
Cdd:TIGR02169 914 KKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-498 |
5.56e-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: 49.67 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 257 DIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLE 336
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 337 DENEALNienvklkgtldALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLI---I 413
Cdd:TIGR02168 334 ELAEELA-----------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 414 TNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSR 493
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
....*
gi 1907151264 494 QLEAA 498
Cdd:TIGR02168 483 ELAQL 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-580 |
8.65e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 89 KKIFEQNDILSKELDTFNRVKLALEHLIKQTDyeqigdsllcLLKDLSDNESENRNLEEKVLEKEtYIRELSCLFQNEKE 168
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE----------LLEPIRELAERYAAARERLAELE-YLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 169 SALKANRLsQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKavaLKKASKVYR 248
Cdd:COG4913 290 LELLEAEL-EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE---RERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 249 QRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKiaiEKTELEVQIETMKKQIANLLEDLRKMETHGKNsceeI 328
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSN----I 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 329 LRKLHSLEDE-NEALNIENVKLKgtldalkdeVASvenELVELQEVEKRQKTLVEGY-RTQ-------VQKLQEAAEMVK 399
Cdd:COG4913 439 PARLLALRDAlAEALGLDEAELP---------FVG---ELIEVRPEEERWRGAIERVlGGFaltllvpPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 400 SR-CKNLLHENNLIITNKNKKLEKVDGNqSLLTKLSLEE-------ENHLIQ----LKCENLKE---------------- 451
Cdd:COG4913 507 RLhLRGRLVYERVRTGLPDPERPRLDPD-SLAGKLDFKPhpfrawlEAELGRrfdyVCVDSPEElrrhpraitragqvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 452 -------------------------KLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSR------------Q 494
Cdd:COG4913 586 ngtrhekddrrrirsryvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 495 LEAALEEGRQKVsEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIK 574
Cdd:COG4913 666 AEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
....*.
gi 1907151264 575 NYLQFL 580
Cdd:COG4913 745 LELRAL 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-584 |
1.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 98 LSKELDTFNRVKLALEHLIKQTdyEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLs 177
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 178 qsvkvvhdrlQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKE--ASRQKAVALKKASKVYRQRLRhft 255
Cdd:PRK03918 244 ----------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELR--- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 256 gDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKK------QIANLLEDLRKMETH-GKNSCEEI 328
Cdd:PRK03918 311 -EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRlTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 329 LRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEV------------EKRQKTLVEGYRTQVQKLQEAAE 396
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 397 MVKSRCKNLLHENnliitnknKKLEKVDGNQSLLTKL--------SLEEENHLIQLK--------CENLKEKLEQMDAEN 460
Cdd:PRK03918 470 EIEEKERKLRKEL--------RELEKVLKKESELIKLkelaeqlkELEEKLKKYNLEelekkaeeYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 461 KELEKKLADQEEcLKHSDLELKEKAAEytaLSRQLEAALEEGRQKVSEEVEKMSSRERALQ------IKILDLEAELRKK 534
Cdd:PRK03918 542 KSLKKELEKLEE-LKKKLAELEKKLDE---LEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELERE 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907151264 535 NEEQNQLVDKmntktqhqaicLKEIQHSLEKSETRNESIKNYLQFLQISY 584
Cdd:PRK03918 618 EKELKKLEEE-----------LDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-541 |
1.86e-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: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 348 KLKGTLDALKDEVAsvENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEmvksrcknllhENNLIITNKNKKLEKVDGNQ 427
Cdd:COG1196 224 ELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELE-----------ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 428 SLLTK--LSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEEclkhSDLELKEKAAEYTALSRQLEAALEEGRQK 505
Cdd:COG1196 291 YELLAelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907151264 506 VSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 541
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-569 |
2.22e-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: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 292 EKTELEVQIETMKKQIANLLEDLRKMEThgknsceeILRKLHSLEDENEALN--IENVKLKGTLDALKDEVASVENELvE 369
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALED--------AREQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQR-R 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 370 LQEVEKRQKTLvegyRTQVQKLQEAAEMVKSRCKNLLhennliitnknkklEKVDGNQSLLTKLSLEEEnhliqlkcENL 449
Cdd:COG4913 290 LELLEAELEEL----RAELARLEAELERLEARLDALR--------------EELDELEAQIRGNGGDRL--------EQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 450 KEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQikilDLEA 529
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRR 419
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907151264 530 ELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETR 569
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-577 |
3.06e-05 |
|
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: 47.04 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 96 DILSKELDTFNRVKLALEHLIKQTDYEQIGDsllcLLKDLSDNESENRNLEEkvleketyIRELSCLFQNEKESALKANR 175
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQ----MERQMAAIQGKNESLEK--------VSSLTAQLESTKEMLRKVVE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 176 LSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIK-------------EASRQKAVALKK 242
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegdhlrnvqtecEALKLQMAEKDK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 243 ASKVYRQRLRHFT---GDIERLASQVRDQEAKLSETVSassDWKSQFEKIAIEKTELEVQIETMKKQIANLleDLRKMET 319
Cdd:pfam15921 563 VIEILRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEIN---DRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKL 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 320 hgKNSCEEILRKLHSLEDENealnienvklkgtlDALKDEVASVENELVELQEvekRQKTLVEGYRTQVQKLQEAAEMVK 399
Cdd:pfam15921 638 --VNAGSERLRAVKDIKQER--------------DQLLNEVKTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKLK 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 400 SRCKNLLHEnnliITNKNKKLEKVDGNQSLLTKLSLEEEnhliqlkcENLKEKLEQMDAenkeLEKKLADQEECLKHSDL 479
Cdd:pfam15921 699 MQLKSAQSE----LEQTRNTLKSMEGSDGHAMKVAMGMQ--------KQITAKRGQIDA----LQSKIQFLEEAMTNANK 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 480 ELKEKAAEYTALSRQLEAALEEgRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQhQAICLKeI 559
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ-ESVRLK-L 839
|
490 500
....*....|....*....|....
gi 1907151264 560 QHSLEKSE------TRNESIKNYL 577
Cdd:pfam15921 840 QHTLDVKElqgpgyTSNSSMKPRL 863
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
151-394 |
4.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 151 EKETYIRELSCLFQNEKESALKANRLSQSVkvvhdrLQRQIQKREAENEKLkehVQSLETQIAKwnLQVKMNKQEAVAIK 230
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAEAY------LEQNLELRREEARKA---LEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 231 EASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSE-------------TVSAS---SDWKSQFEKIAIEKT 294
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraqlgsgpdalpELLQSpviQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 295 ELEV-------QIETMKKQIANLLEDLRkmethgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENEL 367
Cdd:COG3206 281 ELSArytpnhpDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*..
gi 1907151264 368 VELQEVEKRQKTLVEGYRTQVQKLQEA 394
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-537 |
5.10e-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: 45.91 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 290 AIEKTELEVQIETMKKQIANLLEDLRKMethgKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVE 369
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 370 LQEVEKRQKtlvegyrtqvqklQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDgNQSLLTKLSLEEENHLIQLK--CE 447
Cdd:COG4942 95 LRAELEAQK-------------EELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRadLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 448 NLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKaaeytalsRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDL 527
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAER--------QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|
gi 1907151264 528 EAELRKKNEE 537
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-544 |
9.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 166 EKESALKANRLSQSVKVVHDRLQRQIQKREAEN------EKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVA 239
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkkaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 240 LKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEkiaIEKTELEVQIETMKKQIANLLEDLRKmet 319
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRK--- 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 320 hgknscEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENElvELQEVEKRQKTLVEGYRTQVQKLQEAAEMVK 399
Cdd:PTZ00121 1583 ------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 400 SRcknllhENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQ--LKCENLKEKLEQM---DAENKELEKKLADQEECL 474
Cdd:PTZ00121 1655 AE------EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalKKEAEEAKKAEELkkkEAEEKKKAEELKKAEEEN 1728
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 475 KHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDK 544
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
370-536 |
1.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 370 LQEVEKRQKTLVEGYRTQVQKLQEAAEM-VKSRCKNLLHENNLIITNKNKKLEKVdgnqslltklsleeENHLIQlKCEN 448
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKL--------------EKRLLQ-KEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 449 LKEKLEQMDAENKELEKKladqEECLKHSDLELKEKAAEYTALSRQLEAALE--------EGRQKVSEEVEKMSSRERAL 520
Cdd:PRK12704 98 LDRKLELLEKREEELEKK----EKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAV 173
|
170
....*....|....*.
gi 1907151264 521 QIKILDLEAELRKKNE 536
Cdd:PRK12704 174 LIKEIEEEAKEEADKK 189
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
305-588 |
1.68e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 305 KQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEV------ASVENELVELQEVEKRQK 378
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiylqsaQRVELAERQLQELKIDVK 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 379 TLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLI---ITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQ 455
Cdd:COG5022 893 SISSLKLVNLELESEIIELKKSLSSDLIENLEFKtelIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 456 MDAENKELEKKladqEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQkvSEEVEKMSSRERALQIKILDLEAELRKKN 535
Cdd:COG5022 973 YEDLLKKSTIL----VREGNKANSELKNFKKELAELSKQYGALQESTKQ--LKELPVEVAELQSASKIISSESTELSILK 1046
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151264 536 EEQNQ--LVDKMNTKTQHQAICL---KEIQHSLEKSETRNESIKNYLQFLQISYVTMF 588
Cdd:COG5022 1047 PLQKLkgLLLLENNQLQARYKALklrRENSLLDDKQLYQLESTENLLKTINVKDLEVT 1104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
322-541 |
2.12e-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: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 322 KNSCEEILRKLHSLEDENEALNIEnvklkgtLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 401
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKA-------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 402 CKNLLHENNLIITNKNKKLEKVDGNQSLL-----TKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKH 476
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907151264 477 SDLELKEKAAEYTALSRQLEaaleegrqKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQL 541
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIE--------ELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-401 |
2.40e-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: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 226 AVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKK 305
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 306 QIANLLED----LRKMETHGKNSCEEIL----------RKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQ 371
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLlspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190
....*....|....*....|....*....|
gi 1907151264 372 EVEKRQKTLVEGYRTQVQKLQEAAEMVKSR 401
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
93-584 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 93 EQNDILSKELDTFNRVKLALEHLIK--QTDYEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESa 170
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISntQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 171 lKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQR 250
Cdd:TIGR04523 304 -KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 251 LRhftgDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQI---ANLLEDLRKMETHGKNSCEE 327
Cdd:TIGR04523 383 KQ----EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIiknNSEIKDLTNQDSVKELIIKN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 328 ILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELqeveKRQKTLVEGyrtQVQKLQEAAEMVKSRCKNLLH 407
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL----NEEKKELEE---KVKDLTKKISSLKEKIEKLES 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 408 ENNLIITNKNKKLEKVDGNQSLLTKLSLEEEnhliqlkCENLKEKLEQMDAENKELEKKLADQEEclkhsdlELKEKAAE 487
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKENLEKE-------IDEKNKEIEELKQTQKSLKKKQEEKQE-------LIDQKEKE 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 488 YTALSRQLEaALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSE 567
Cdd:TIGR04523 598 KKDLIKEIE-EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
490
....*....|....*..
gi 1907151264 568 TRNESIKNYLQFLQISY 584
Cdd:TIGR04523 677 DIIELMKDWLKELSLHY 693
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-405 |
6.54e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 117 KQTDYEQIGDSLLCLLKDLSDNESEnrnLEEKVLEKETYIRELSCLFQNEKESALK-ANRLSQSVKVVHDRLQRQIQKRE 195
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEAR---IEELEEDLHKLEEALNDLEARLSHSRIPeIQAELSKLEEEVSRIEARLREIE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 196 AENEKLKEHVQSLETQIakwnlQVKMNKQEAVAIKEASRQKAVALKKAskvyrqRLRHFTGDIERLASQVRDQEAKLSET 275
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEI-----QELQEQRIDLKEQIKSIEKEIENLNG------KKEELEEELEELEAALRDLESRLGDL 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 276 VSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKnsceEILRKLHSLEDENEALNIENvKLKGTLDA 355
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLE-DVQAELQR 962
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907151264 356 LKDEVASVE--NELV--ELQEVEKRQKTLVEgyrtQVQKLQEAAEMVKSRCKNL 405
Cdd:TIGR02169 963 VEEEIRALEpvNMLAiqEYEEVLKRLDELKE----KRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
88-274 |
8.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 88 LKKIFEQNDILSKELDTFNRVKLALEHLIKQTDYEQigdsllcLLKDLSDNESENRNLEEKVLEKETYIRELsclfqNEK 167
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL-------LEAELEELRAELARLEAELERLEARLDAL-----REE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 168 ESALKANRLSQSVKVVhDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVY 247
Cdd:COG4913 325 LDELEAQIRGNGGDRL-EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180
....*....|....*....|....*..
gi 1907151264 248 RQRLRHFTGDIERLASQVRDQEAKLSE 274
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
126-536 |
1.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 126 DSLLCLLKDLSDNESEnrnLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHV 205
Cdd:PRK02224 310 EAVEARREELEDRDEE---LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 206 QSLETQIAkwnlqvkmNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRD------------------ 267
Cdd:PRK02224 387 EELEEEIE--------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 268 QEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIaNLLEDLRKMEthgknsceeilRKLHSLEDENEALNIENV 347
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAE-----------DRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 348 KLKGTLDALKDEVASVENELVELqEVEKRQKtlvegyRTQVQKLQEAAEMVKSRCKNLlhennliitnkNKKLEKVDGNQ 427
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAEL-EAEAEEK------REAAAEAEEEAEEAREEVAEL-----------NSKLAELKERI 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 428 SLLTKL--SLEEENHLIQlKCENLKEKLEQMDAENKELEKKLADQEEclKHSDLELKEKAAEYTALSRQLEAAlEEGRQK 505
Cdd:PRK02224 589 ESLERIrtLLAAIADAED-EIERLREKREALAELNDERRERLAEKRE--RKRELEAEFDEARIEEAREDKERA-EEYLEQ 664
|
410 420 430
....*....|....*....|....*....|.
gi 1907151264 506 VSEEVEKMSSRERALQIKILDLEAELRKKNE 536
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
133-519 |
1.53e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 133 KDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSqsvkvvhdrlqrqIQKREAENEKLKEHVQSLETQI 212
Cdd:PLN02939 57 KQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRAS-------------MQRDEAIAAIDNEQQTNSKDGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 213 AKWNLQVkmnkQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETvSASSDWKSQfEKIAIE 292
Cdd:PLN02939 124 QLSDFQL----EDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSET-DARIKLAAQ-EKIHVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 293 KteLEVQIETMKKQIANLLEDLRKMEthgknsceeilrklHSLEDENEALNIENVKLKGTLDALKDevasvenELVELQE 372
Cdd:PLN02939 198 I--LEEQLEKLRNELLIRGATEGLCV--------------HSLSKELDVLKEENMLLKDDIQFLKA-------ELIEVAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 373 VEKRqktlvegyrtqVQKLQEAAEMVKSRCKNLlhENNLIITNKN-KKL---------EKVDGNQSLLTKLSLEEENHLI 442
Cdd:PLN02939 255 TEER-----------VFKLEKERSLLDASLREL--ESKFIVAQEDvSKLsplqydcwwEKVENLQDLLDRATNQVEKAAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 443 QL-KCENLKEKLEQMDAENKE-------------LEKKLADQEECLKHSDLELKekaaEYTALSRQLEAALEEGRQKVSE 508
Cdd:PLN02939 322 VLdQNQDLRDKVDKLEASLKEanvskfssykvelLQQKLKLLEERLQASDHEIH----SYIQLYQESIKEFQDTLSKLKE 397
|
410
....*....|.
gi 1907151264 509 EVEKMSSRERA 519
Cdd:PLN02939 398 ESKKRSLEHPA 408
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
445-546 |
1.85e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 445 KCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEkaaeytalsrqleaALEEGRQKVSEEvEKMSSRERalqiKI 524
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90 100
....*....|....*....|..
gi 1907151264 525 LDLEAELRKKNEEQNQLVDKMN 546
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-545 |
2.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 132 LKDLSDNESENRNLEEKVLEKETYIRELSclfqnEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQ 211
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELE-----AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 212 IAKW-NLQVKMNKQEAvAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQfekia 290
Cdd:COG4717 155 LEELrELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 291 IEKTELEVQIETMKKQIANLLEDLRkmethgknsceeILRKLHSLEDENEALNIENVKLKGTLdALKDEVASVENELVEL 370
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLL------------IAAALLALLGLGGSLLSLILTIAGVL-FLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 371 QEVEKRQKTLVEGYRTQVQKLQEaaEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLK 450
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 451 EKLEQMDAENKELEKKLADQEEclkhsdlELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKmssrerALQIKILDLEAE 530
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAE-------EYQELKEELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEE 440
|
410
....*....|....*
gi 1907151264 531 LRKKNEEQNQLVDKM 545
Cdd:COG4717 441 LEELEEELEELREEL 455
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
449-532 |
2.75e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 40.45 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 449 LKEKLEQMDAENKELEKKLA------DQEECLK----HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRE 517
Cdd:PRK00591 4 MLDKLEALEERYEELEALLSdpevisDQKRFRKlskeYAELEpIVEAYREYKQAQEDLEEAKEMLEEESDPEMREMAKEE 83
|
90
....*....|....*.
gi 1907151264 518 -RALQIKILDLEAELR 532
Cdd:PRK00591 84 lKELEERLEELEEELK 99
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-574 |
3.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 134 DLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETqiA 213
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA--A 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 214 KWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQrlrhfTGDIERLASQVRD--------QEAKLSETVSASSDWKSQ 285
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK-----ADEAKKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 286 FEKiAIEKTELEVQIETMKKQI--ANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVK----LKGTLDALKDE 359
Cdd:PTZ00121 1459 AEE-AKKKAEEAKKADEAKKKAeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeAKKAEEAKKAD 1537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 360 VASVENELVELQEVEK--------------RQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLH----------------EN 409
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKaeelkkaeekkkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyeeekkmkaeeakkaEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 410 NLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEecLKHSDlELKEKAAEYT 489
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAE-EDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 490 ALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEaELRKKNEEQNQLVDKMNTKTQHQaiclKEIQHSLEKSETR 569
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKK 1769
|
....*
gi 1907151264 570 NESIK 574
Cdd:PTZ00121 1770 AEEIR 1774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
137-574 |
3.54e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 137 DNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSvkvvhDRLQRQIQKREAENEKLKEHVQSLE-----TQ 211
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-----DELKKAEEKKKADEAKKAEEKKKADeakkkAE 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 212 IAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAi 291
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK- 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 292 EKTELEVQIETMKKQIANL--LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVE 369
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 370 LQEVEKR--QKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSllTKLSLEEENHLIQLKCE 447
Cdd:PTZ00121 1472 ADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 448 NLKEKLEQMDAEnkelEKKLADQeeclKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSrERALQIKILDL 527
Cdd:PTZ00121 1550 ELKKAEELKKAE----EKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKI 1620
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907151264 528 EAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIK 574
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
327-510 |
4.28e-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: 39.14 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 327 EILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKsrcknll 406
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 407 heNNLIITNKNKKLEKVDGNQSLLTKLSLEeenhliqlkcenLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAA 486
Cdd:COG1579 87 --NNKEYEALQKEIESLKRRISDLEDEILE------------LMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....
gi 1907151264 487 EYTALSRQLEAALEEGRQKVSEEV 510
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
326-573 |
4.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 326 EEILRKLHSLED-ENEALNIENVK--LKGTLDALKDEVASVENELVELQEVEKR---QKTLVEGYRTQVQKLQEAAEMVK 399
Cdd:PRK03918 148 EKVVRQILGLDDyENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 400 SRCKNLlHENNLIITNKNKKLEKVDGNqslltKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDL 479
Cdd:PRK03918 228 KEVKEL-EELKEEIEELEKELESLEGS-----KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 480 ---------ELKEKAAEYTALSRQLEAALEEGRQKvSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQ 550
Cdd:PRK03918 302 yeeyldelrEIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260
....*....|....*....|...
gi 1907151264 551 HQAICLKEIQHSLEKSETRNESI 573
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEI 403
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
122-543 |
4.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 122 EQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELS-CLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENE- 199
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEl 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 200 -KLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHF------TGDIERLASQVRDQEAKL 272
Cdd:PRK01156 245 sSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkykndIENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 273 SETVSASSDWKSQFEKIAIEKTELEvqieTMKKQIANLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIENVKLKGT 352
Cdd:PRK01156 325 HAIIKKLSVLQKDYNDYIKKKSRYD----DLNNQILELEGYEMDYNSY-LKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 353 LDALKDEVASVENEL-VELQEVEKRQKTLVEGYRTQVQKLQEA---AEMVKSR-----CKNLLHEN--NLIITNKNKKL- 420
Cdd:PRK01156 400 QEIDPDAIKKELNEInVKLQDISSKVSSLNQRIRALRENLDELsrnMEMLNGQsvcpvCGTTLGEEksNHIINHYNEKKs 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 421 ---EKVDGNQSLLTKLSlEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEEcLKHSDLELKEKAAEYTALSRQLEA 497
Cdd:PRK01156 480 rleEKIREIEIEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907151264 498 A-LEEGRQKVSEEVEKMSsreralQIKILDLEAELRKKNEEQNQLVD 543
Cdd:PRK01156 558 LkLEDLDSKRTSWLNALA------VISLIDIETNRSRSNEIKKQLND 598
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
218-537 |
4.65e-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: 39.67 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 218 QVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELE 297
Cdd:pfam19220 45 QAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 298 VQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI---ENVKLKGTLDALKDEVASVENELVELQEVE 374
Cdd:pfam19220 125 RQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALleqENRRLQALSEEQAAELAELTRRLAELETQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 375 KRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKVDGNQSLLTKLSLEEENHLIQLKCE------N 448
Cdd:pfam19220 205 DATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAiraaerR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 449 LKE---KLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQL---EAALEEGRQKVSEEVEKMSSRERALQI 522
Cdd:pfam19220 285 LKEasiERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALaakDAALERAEERIASLSDRIAELTKRFEV 364
|
330
....*....|....*
gi 1907151264 523 KILDLEAELRKKNEE 537
Cdd:pfam19220 365 ERAALEQANRRLKEE 379
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
266-536 |
5.15e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 266 RDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKN---SCEEILRKLHSLEDENEAL 342
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKElsaSSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 343 NIENVKLKGTLDALKDEVASVENELVELQEVEKR---QKTLVEGYRTQVQ-KLQEAAEMVKSRCKNLLHENNLIITNKNK 418
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKagaQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 419 KLEKVDGNQSLLTKLSL----EEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKE---KAAEYTAL 491
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQ 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907151264 492 SRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNE 536
Cdd:pfam07888 288 LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
448-532 |
5.47e-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: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 448 NLKEKLEQMDAENKELEKKLADQE---------ECLK-HSDLE-LKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSR 516
Cdd:COG0216 1 SMLDKLEALEERYEELEALLSDPEvisdqkrfrKLSKeYAELEpIVEAYREYKKLLEDIEEAKELLEEESDPEMREMAKE 80
|
90
....*....|....*..
gi 1907151264 517 E-RALQIKILDLEAELR 532
Cdd:COG0216 81 ElEELEARLEELEEELK 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
287-545 |
5.52e-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: 39.67 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 287 EKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLK----GTLDALKDEVAS 362
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 363 VENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHEnnliITNKNKKLEKvdgnqslltklsLEEENHLI 442
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDK------------LTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 443 QLKCENLKEKLEQMDAENKELEKKLADQE---ECLKHSDLELKEKAAEYTALSRQLEAALEEGRQkvseEVEKMSSRERA 519
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRLSEELADLNA----AIAGIEAKINE 438
|
250 260
....*....|....*....|....*.
gi 1907151264 520 LQIKILDLEAELRKKNEEQNQLVDKM 545
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
326-472 |
5.94e-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: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907151264 326 EEILRKLHSLEDENEALNIE-NVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKN 404
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907151264 405 LLHENNLIITNKNKKLEKVDGNQ-----SLLT-----KLsLEEEnhliqlkcenlKEKLEQMDaenKELEKKLADQEE 472
Cdd:COG0542 494 LAELEEELAELAPLLREEVTEEDiaevvSRWTgipvgKL-LEGE-----------REKLLNLE---EELHERVIGQDE 556
|
|
| |
