|
Name |
Accession |
Description |
Interval |
E-value |
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
22-749 |
0e+00 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 1106.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 22 VIFTSERCNRVTYGLRTVNGDPSRYKQCGPSGRVWIVPCAPQMTFDPEDRVCKERLDSRIVKPMRKYETSRTIITTPAPI 101
Cdd:pfam17380 1 VIFTSERCNRVTYGLRTVNGDPSRYKQCGPSGRVWIVPCAPQMTFDPEDRVCKERLDSRVFKPMRKYETAKTIITTPAPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 102 PSSYPVSAEVIAPGAPAAshaAPEEFVFSTIRPKSRKPKAKTRGKFRKTTTAMIQTTTP-MTVESFESMEMTTTPKIVIF 180
Cdd:pfam17380 81 PSSYPVSAEVSPPGAPAA---APEEFVFSTIRPKSRKPKARTRGKKRKTTTTMIQTTTPmMVTTSSSALEMTTTPKIVIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 181 ASKKNMNNTNRSGESRTQlIRNRNRERGNAPAFTRPGRVRTTTPMSVTHATRFVPGIQHKvTVAPKEVQGMPHTLAPYEK 260
Cdd:pfam17380 158 ASKKNASGGNRSGEQRKQ-IQLIRRRRGNHSAFTRPGRPRTTTPMPVTHATRFVPGIQMS-TVAPKEVQGMPHTLAPYEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 261 MDRRPDSFGV-EELTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERR 339
Cdd:pfam17380 236 MERRKESFNLaEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 340 RKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVR 419
Cdd:pfam17380 316 RKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 420 QELEAARKYKLQEEERQRKIQQQKVEMEQIR-QQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKK 498
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRaEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 499 KLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQ 578
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 579 QQIMIATEERSRLDAMEREREMLRQIKESEKQRKELErqellATTPITTIKPIYRPDISEYRPPDVESHMIRFTTQSPEW 658
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE-----ATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPEW 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 659 ATPSP-TWNPAWNTVTAEEETPGIPIIHSQCQVNGECELKYDVDSFCAHPRSPSMYLQCAPLYGRLGRWTERYCPDTLIF 737
Cdd:pfam17380 631 ATPSPaTWNPEWNTVTAEEETPGIPIIHSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIF 710
|
730
....*....|..
gi 86562857 738 IVSIGRCEKGEE 749
Cdd:pfam17380 711 IVSIGRCEKGEE 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-623 |
5.42e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.83 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQA--TIYAEQERMAMERNRELERIRLEEK 382
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 383 KRENER----VRQEEIAMEISKIRELERLQL---ERQRKNERVRQELEA---ARKYKLQEEERQRKIQQQKVEMEQIRQQ 452
Cdd:PTZ00121 1570 KKAEEDknmaLRKAEEAKKAEEARIEEVMKLyeeEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 453 EEARQEQlrvleEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMI 532
Cdd:PTZ00121 1650 EELKKAE-----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 533 EEKNKRKMLE---KEMEDRQNAiyeeeerriaeeeRRKQIEIEERRRIQQqimIATEERSRLDAMEREREMLrqIKESEK 609
Cdd:PTZ00121 1725 EEENKIKAEEakkEAEEDKKKA-------------EEAKKDEEEKKKIAH---LKKEEEKKAEEIRKEKEAV--IEEELD 1786
|
330
....*....|....
gi 86562857 610 QRKELERQELLATT 623
Cdd:PTZ00121 1787 EEDEKRRMEVDKKI 1800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-618 |
4.69e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELD-RQATIYAEQERMAMERNRELERIRLEEKK 383
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 384 RENERVRQEEIAMEISKIRELERL-QLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEmeQIRQQEEAR-QEQLR 461
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE--EAKKAEEARiEEVMK 1599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 462 VLEEERARELERVRQEELERQhQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMK--ENKQKMIEEKNKRK 539
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKI-KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaaEEAKKAEEDKKKAE 1678
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86562857 540 MLEKEMEDRQNAiyeeeerriaeeERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMlRQIKESEKQRKELERQE 618
Cdd:PTZ00121 1679 EAKKAEEDEKKA------------AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKKEAEEDKK 1744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
298-552 |
1.29e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 298 LLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRklEESETARQAELDRQATIY---AEQERMAMERNREL 374
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--LELEELELELEEAQAEEYellAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 375 ERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEE 454
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 455 ARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEE 534
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250
....*....|....*...
gi 86562857 535 KNKRKMLEKEMEDRQNAI 552
Cdd:COG1196 469 LEEAALLEAALAELLEEL 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-621 |
1.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEKEEKARELER-RRKLEESETARQAELDRQATIYAEQERMAMERNREleRIRLEEKKRENERV 389
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEElEAELEELEAELEELEAELAELEAELEELRLELEEL--ELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 390 RQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERAR 469
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 470 ELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEmkENKQKMIEEKNKRKMLEKEMEDRQ 549
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE--EALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86562857 550 NAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-619 |
5.24e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKE--EKAREL---ERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAME 397
Cdd:COG1196 203 EPLERQAEkaERYRELkeeLKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 398 ISK--------IRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleeeRAR 469
Cdd:COG1196 283 LEEaqaeeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-----EAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 470 ELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQ 549
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 550 NAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQEL 619
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-621 |
7.31e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 314 QEKFEKMEQ--ERLrqekEEKARELERRRK-LE-ESETARQA-ELDRQATIYAEQERMAMERNRELERIRLEEKKRENER 388
Cdd:COG1196 178 ERKLEATEEnlERL----EDILGELERQLEpLErQAEKAERYrELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 389 VRQEEIAMEISKIRELERLQLERQRKnervRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLrvleeera 468
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 469 relervrQEELERQHQMEILRQQEEDQKKKKLEKdreqreqqeaeelnrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDR 548
Cdd:COG1196 322 -------EEELAELEEELEELEEELEELEEELEE-----------------AEEELEEAEAELAEAEEALLEAEAELAEA 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86562857 549 QNAIyeeeERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG1196 378 EEEL----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
295-549 |
8.89e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEK------ARELERRRKLEESETARQAELDRQATIYAEQERMAM 368
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 369 ERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAA--RKYKLQEEERQRKIQQQKVEM 446
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 447 EQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRmiIEKEMKE 526
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--LEAALAE 481
|
250 260
....*....|....*....|...
gi 86562857 527 NKQKMIEEKNKRKMLEKEMEDRQ 549
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
302-618 |
1.30e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 302 VQHQKTVSERQQQEKFEKMEQERLRQE--------KEEKARELERRRKLEE---SETARQAELDRQAtiyaEQERMAMER 370
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEvrkaeelrKAEDARKAEAARKAEEerkAEEARKAEDAKKA----EAVKKAEEA 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 371 NRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIR 450
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 451 QQEEARQEqlrvleEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNrmiiEKEMKENKQK 530
Cdd:PTZ00121 1316 KADEAKKK------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE----AKKKADAAKK 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 531 MIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQ 610
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
....*...
gi 86562857 611 RKELERQE 618
Cdd:PTZ00121 1466 AEEAKKAD 1473
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-618 |
1.71e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEekaRELERRRKLEESETARQAEldRQATIYAEQERMAmERNRELERIRLEEK 382
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFAR--RQAAIKAEEARKA-DELKKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 383 KRENERVRQEEiamEISKIRELERLQLERQRKNERVRQELEAARKyklQEEERQRKIQQQKVEMEQIRQQEEARQEQLRV 462
Cdd:PTZ00121 1295 AKKAEEKKKAD---EAKKKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 463 LEEERARELER--VRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKM 540
Cdd:PTZ00121 1369 AEKKKEEAKKKadAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 541 LEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRiqqqimiATEERSRLDAMEREREMLRQIKESEKQRKELERQE 618
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-------ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
306-618 |
5.97e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 306 KTVSERQQQEKFEKMEQERLRQE--KEEKARELERRRKLEES---ETARQAELDRQA--TIYAEQERMAmERNRELERIR 378
Cdd:PTZ00121 1128 RKAEEARKAEDARKAEEARKAEDakRVEIARKAEDARKAEEArkaEDAKKAEAARKAeeVRKAEELRKA-EDARKAEAAR 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 379 LEEKKRENERVRQEEIAMEISKIRELERLQ--------LERQRKNERVRQELEA-----ARKYKLQEEERQRKIQQQKvE 445
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKkdaeeakkAEEERNNEEIRKFEEArmahfARRQAAIKAEEARKADELK-K 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 446 MEQIRQQEEARQ-EQLRVLEEERARELERVRQEELERQHQmEILRQQEEDQKK--KKLEKDREQREQQEAEELNRMIIEK 522
Cdd:PTZ00121 1286 AEEKKKADEAKKaEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 523 EMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLR 602
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
330
....*....|....*.
gi 86562857 603 QIKESEKQRKELERQE 618
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAE 1460
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
310-620 |
6.79e-15 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 77.27 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKMEQERLRQEKEEKARELERRRKLEEsETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERV 389
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEE-EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 390 RQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQR----KIQQQKVEMEQIRQQEEARQEQLRVLEE 465
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 466 ERARELERVRQEELERQHQMEILR----QQEEDQKKKKLEKDREQREQQEAEELNR----MIIEKEMKENKQKMIEEKNK 537
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRaklyQEEQERKERQKEREEAEKKARQRQELQQareeQIELKERRLAEEAEREEEEF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 538 RKMLEKEMEDRQnaiyeeeerrIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKEL--- 614
Cdd:pfam13868 264 ERMLRKQAEDEE----------IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERiee 333
|
....*.
gi 86562857 615 ERQELL 620
Cdd:pfam13868 334 ERQKKL 339
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
305-616 |
3.67e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.32 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKR 384
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLrvle 464
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE---- 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 465 eerareleRVRQEELERQHQM--EILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKrKMLE 542
Cdd:pfam02463 829 --------KIKEEELEELALElkEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE-KEEK 899
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86562857 543 KEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELER 616
Cdd:pfam02463 900 KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-617 |
1.19e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQAtiyaeQERMAMERNRELERIRLEEK 382
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-----EDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 383 KRENERVRQEEIAMEISKIRELERLqlerqRKNERVRQeLEAARKYklqEEERQ----RKIQQQKvEMEQIRQQEEARQE 458
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARK-AEAARKA---EEERKaeeaRKAEDAK-KAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 459 QLRVLEEERARELERVRQEELERQHQM---------EILRQQEEDQK---KKKLEKDREQREQQEAEELNRMIIE-KEMK 525
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFarrqaaikaEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAEEaKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 526 ENKQKMIEEKNKRKMLEKEMEDRQNAiyeEEERRIAEEERRKQIEIEERRRIQQQIMiATEERSRLDAMEREREMLRQIK 605
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKA---AEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKAD 1394
|
330
....*....|..
gi 86562857 606 ESEKQRKELERQ 617
Cdd:PTZ00121 1395 EAKKKAEEDKKK 1406
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
292-620 |
5.43e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 292 NEFLNQLLHIVQHQKTvserqqQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQErmamERN 371
Cdd:pfam02463 685 AESELAKEEILRRQLE------IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE----EEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 372 RELERIRLEEKKRENErvrQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQ 451
Cdd:pfam02463 755 SRLKKEEKEEEKSELS---LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 452 QEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKE-------M 524
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeesqklnL 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 525 KENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERR-KQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQ 603
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
330
....*....|....*..
gi 86562857 604 IKESEKQRKELERQELL 620
Cdd:pfam02463 992 KDELEKERLEEEKKKLI 1008
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
311-501 |
2.39e-12 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 70.75 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEKEEkarelERRRKLEESETARQAEldrqatiyaeqERMAMERNRELERIRLEEKKRENERVR 390
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEE-----QRRLQQEQLERAEKMR-----------EELELEQQRRFEEIRLRKQRLEEERQR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 391 QEEiameiskirELERLQLERQRKNERVRQELEAARKyKLQeeERQRKIQQ---QKVEMEQIRQQEEARQ---EQLRVLE 464
Cdd:pfam15709 403 QEE---------EERKQRLQLQAAQERARQQQEEFRR-KLQ--ELQRKKQQeeaERAEAEKQRQKELEMQlaeEQKRLME 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 86562857 465 EERARELERVRQ---EELERQHQMEILRQQEEDQKKKKLE 501
Cdd:pfam15709 471 MAEEERLEYQRQkqeAEEKARLEAEERRQKEEEAARLALE 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
282-619 |
2.91e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 282 VRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERlrqeKEEKARELERRRKLEE----SETARQAELDRQA 357
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK----KADEAKKAEEKKKADEakkkAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 358 TIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEiSKIRELERLQLERQRKNERVRQELEAARKyklqEEERQR 437
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKK----ADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 438 KIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNR 517
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 518 MIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQieIEERRRIQQqiMIATEERSRLDAMERE 597
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADE--AKKAEEKKKADELKKA 1554
|
330 340
....*....|....*....|....
gi 86562857 598 REMLR--QIKESEKQRKELERQEL 619
Cdd:PTZ00121 1555 EELKKaeEKKKAEEAKKAEEDKNM 1578
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
283-620 |
3.15e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 283 RYNGQTMTENEFLNQL---------LHIVQHQKtVSERQQQEKfekmEQERLRQEKE-----EKARELERRRKLEESETA 348
Cdd:pfam02463 110 YINGKNVTKKEVAELLesqgispeaYNFLVQGG-KIEIIAMMK----PERRLEIEEEaagsrLKRKKKEALKKLIEETEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 349 RQAELDRQATIYAEQERMAMERNRELeriRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERvrQELEAARKY 428
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKAL---EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ--EEIESSKQE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 429 KLQEEERQRKIQQQKVEMEQIRQQEEARQEQLrvleeERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQRE 508
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 509 QQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQImiatEER 588
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA----QLL 410
|
330 340 350
....*....|....*....|....*....|..
gi 86562857 589 SRLDAMEREREMLRQIKESEKQRKELERQELL 620
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-618 |
7.32e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERlRQEKEEKARELERRRKLEESETARQAEldrQATIYAEQERMAMERNRELERIRL---EE 381
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEA-AADEAEAAEEKAEAAEKKKEEAKKKAD---AAKKKAEEKKKADEAKKKAEEDKKkadEL 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 382 KKRENERVRQEEI---AMEISKIRELERlQLERQRKNERVRQELEAARKYK--LQEEERQRKIQQQKVEMEQIRQQEEAR 456
Cdd:PTZ00121 1411 KKAAAAKKKADEAkkkAEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 457 ---QEQLRVLEEERARELERVRQEEL---ERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQK 530
Cdd:PTZ00121 1490 kkaEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 531 MIEEKNKRKMLEKEMEDRQ---------NAIYEEEERRIAEEERRKQ----------IEIEERRRIQQQIMIATEERSRL 591
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMKAEEAKKAEeakikaeelkKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340
....*....|....*....|....*..
gi 86562857 592 DAMEREREMLRQIKESEKQRKELERQE 618
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
317-639 |
1.02e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 69.23 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 317 FEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAM 396
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 397 EISKIRELERLQLERQRKNERVRQELEaarkyKLQEEERQRKIQQQKVEMEQirqqEEARQEQLRVLEEERARELERVRQ 476
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQ-----DKINEELKLLKQKIDEEEEE----EEKSRLKKEEKEEEKSELSLKEKE 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 477 EELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIyeEE 556
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL--AE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 557 ERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLATTPITTIKPIYRPDI 636
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
...
gi 86562857 637 SEY 639
Cdd:pfam02463 934 EEE 936
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-607 |
1.21e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKAREL-----ERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERI 377
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVRQEEI---AMEISKIRELERLQLERQRKNERVRQELEAARKyklqEEERQRKIQQQKVEMEQIRQQEE 454
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK----ADEAKKKAEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 455 ARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEElnRMIIEKEMKENKQKMIEE 534
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAKKKADEAKKAEE 1520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 535 KNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEI---EERRRIQQqimiATEERSRLDAMEREREMLRQIKES 607
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEA 1592
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
290-588 |
5.03e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.92 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 290 TENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAME 369
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 370 RNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAA---RKYKLQEEERQRKIQQQKVEM 446
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEqklEKLAEEELERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 447 EQ--IRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEM 524
Cdd:pfam02463 870 QEllLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86562857 525 KENKQKMIEEKNKRKMLEKEMEDR-----QNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEER 588
Cdd:pfam02463 950 KEENNKEEEEERNKRLLLAKEELGkvnlmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-621 |
7.63e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEES---------ETARQAELDRQ--------ATIYAEQER 365
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadeaeaaeEKAEAAEKKKEeakkkadaAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 366 MAMERNRELERIRL---EEKKRENERVRQEEI---AMEISKIRELERlQLERQRKNERVRQELEAARKYK--LQEEERQR 437
Cdd:PTZ00121 1392 KADEAKKKAEEDKKkadELKKAAAAKKKADEAkkkAEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKAEeaKKKAEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 438 KIQQQKVEMEQIRQQEEAR---QEQLRVLEEERARELERVRQEEL---ERQHQMEILRQQEEDQKKKKLEKDREQREQQE 511
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 512 AEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQ----NAIYEEEERRIAEEERRKQIEIEERRRIQ-QQIMIATE 586
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEE 1630
|
330 340 350
....*....|....*....|....*....|....*
gi 86562857 587 ERSRLDAMEREREmlRQIKESEKQRKELERQELLA 621
Cdd:PTZ00121 1631 EKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKA 1663
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
318-617 |
2.52e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 318 EKMEQ-ERLRQEKEEKARELERRRKLEESE-TARQAELDRQATIYAEQERMAMERNRELERI--RLEEKKRENERVRQ-- 391
Cdd:TIGR02169 195 EKRQQlERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLteEISELEKRLEEIEQll 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 392 EEIAMEISKIRELERLQLerQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERAREL 471
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRV--KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 472 ERVRQEELERQHQMEILRQQ-EEDQKKKKLEKDREQREQQEAEELNRMIieKEMKENKQKMIEEKNKRKMlekEMEDRQN 550
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAElEEVDKEFAETRDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSE---ELADLNA 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86562857 551 AIyeeeerriaEEERRKQIEIEERRR-IQQQIMIATEERSRLDA-MEREREMLRQIKES----EKQRKELERQ 617
Cdd:TIGR02169 428 AI---------AGIEAKINELEEEKEdKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEydrvEKELSKLQRE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
318-616 |
3.85e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 318 EKMEQERLRQEKEEKARELERrrkLEESETARQAELDRQATIYAEQERMAMERNRELERIrleEKKRENERVRQEEIAME 397
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSS---LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 398 ISKI-RELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEM--EQIRQQEEARQEQLRVLEEERARELERV 474
Cdd:TIGR02169 746 LSSLeQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 475 RQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENK--QKMIEEKNKRKMLEKEMEDRQNAI 552
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 553 yeeeerriaeEERRKQIEIEERR--RIQQQIMIATEERSRLD----AMEREREMLRQIKESEKQRKELER 616
Cdd:TIGR02169 906 ----------EELEAQIEKKRKRlsELKAKLEALEEELSEIEdpkgEDEEIPEEELSLEDVQAELQRVEE 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-614 |
6.87e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 336 LERRRKLEESEtARQAELDRQATIyAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRkN 415
Cdd:TIGR02168 673 LERRREIEELE-EKIEELEEKIAE-LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER-I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 416 ERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleeeRARELERVRQEELERQHQMEILRQQEEDQ 495
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-----EELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 496 KKKKLEKDREQreqqeaeelnrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIyeeeerriaeEERRKQIEIEERR 575
Cdd:TIGR02168 825 RLESLERRIAA-------------TERRLEDLEEQIEELSEDIESLAAEIEELEELI----------EELESELEALLNE 881
|
250 260 270
....*....|....*....|....*....|....*....
gi 86562857 576 RIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKEL 614
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
311-502 |
9.44e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.47 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEkEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIrlEEKKRENERVR 390
Cdd:pfam13868 162 KEKAEREEEREAEREEIE-EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA--EKKARQRQELQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 391 QEEIAMEISKIRELER-LQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEME-QIRQQEEARQEQLRvleeera 468
Cdd:pfam13868 239 QAREEQIELKERRLAEeAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEkQIEEREEQRAAERE------- 311
|
170 180 190
....*....|....*....|....*....|....
gi 86562857 469 releRVRQEELERQHQMEILRQQEEDQKKKKLEK 502
Cdd:pfam13868 312 ----EELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
324-618 |
1.43e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 324 RLRQEKEEKARELER-RRKLEESEtARQAELDRQATIYAEQERMAmERNRELerirleekkRENERVRQEEIAmeiskIR 402
Cdd:COG1196 169 KYKERKEEAERKLEAtEENLERLE-DILGELERQLEPLERQAEKA-ERYREL---------KEELKELEAELL-----LL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 403 ELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleeerareLERVRQEELERQ 482
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY---------ELLAELARLEQD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 483 HQMEILRQQEedqkkkklekdreqreqqEAEELNRmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIyeeeerriae 562
Cdd:COG1196 304 IARLEERRRE------------------LEERLEE--LEEELAELEEELEELEEELEELEEELEEAEEEL---------- 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 563 EERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQE 618
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-616 |
1.87e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 301 IVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQ-ATIYAEQERMAMERNR-ELERIR 378
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQlSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 379 LEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQE 458
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 459 QLRVLEEERARElervrQEELER-QHQMEILRQQEEDQKK--KKLEKDREQREQQEAEELNRMII-EKEMKENKQKMIEE 534
Cdd:TIGR02168 839 RLEDLEEQIEEL-----SEDIESlAAEIEELEELIEELESelEALLNERASLEEALALLRSELEElSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 535 KNKRKMLEKEMEDRQNaiyeeeerriaeeerrKQIEIE-ERRRIQQQIMiateERSRLDAMEREREMLRQIKESEKQRKE 613
Cdd:TIGR02168 914 RRELEELREKLAQLEL----------------RLEGLEvRIDNLQERLS----EEYSLTLEEAEALENKIEDDEEEARRR 973
|
...
gi 86562857 614 LER 616
Cdd:TIGR02168 974 LKR 976
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
326-619 |
3.30e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.55 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 326 RQEKEEKARELERRRKleesETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELE 405
Cdd:pfam13868 1 LRENSDELRELNSKLL----AAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 406 RLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQ--QKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQH 483
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 484 QMEILRQQEEDQKKKKLEKdreqREQQEAEELNRMIIEKEMKENKQKM----------IEEKNKRKMLEKEMEDRQN--- 550
Cdd:pfam13868 157 ILEYLKEKAEREEEREAER----EEIEEEKEREIARLRAQQEKAQDEKaerdelraklYQEEQERKERQKEREEAEKkar 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 551 ---AIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMERER----------EMLRQIKESEKQRKELERQ 617
Cdd:pfam13868 233 qrqELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmkrlehrrELEKQIEEREEQRAAEREE 312
|
..
gi 86562857 618 EL 619
Cdd:pfam13868 313 EL 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-610 |
8.77e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERiRLEEK 382
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-EIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 383 KRENERVRQE--EIAMEISKIRE-LERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQ 459
Cdd:TIGR02168 287 QKELYALANEisRLEQQKQILRErLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 460 LRVleeerARELERVRQEELERQHQMEILRQQEEDQKKKKLE---------KDREQREQQEAEELNRMIIEKEMKENKQK 530
Cdd:TIGR02168 367 LEE-----LESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerlEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 531 MIEEKNKRKMLEKEMEDRQNAIYEEEerriaeeerrkqieiEERRRIQQQIMIATEE----RSRLDAMEREREMLRQIKE 606
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELR---------------EELEEAEQALDAAERElaqlQARLDSLERLQENLEGFSE 506
|
....
gi 86562857 607 SEKQ 610
Cdd:TIGR02168 507 GVKA 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-461 |
9.15e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEE-KARELERRRKLEE----SETARQAELDRQATiyAEQERMAMERNRELERI 377
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKA--AEALKKEAEEAKKAEEL 1707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 R---LEEKKREnERVRQEEIAMEIsKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEE 454
Cdd:PTZ00121 1708 KkkeAEEKKKA-EELKKAEEENKI-KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
....*..
gi 86562857 455 ARQEQLR 461
Cdd:PTZ00121 1786 DEEDEKR 1792
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
273-550 |
1.11e-08 |
|
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: 59.21 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 273 LTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQE------KEEKARELERRRKLEESE 346
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlkqlraRIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 347 TARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAAR 426
Cdd:TIGR00618 286 INRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 427 KYK------LQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleeerarelervrqeelERQHQMEILRQQEEDQKKKKL 500
Cdd:TIGR00618 366 SIReiscqqHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ------------------REQATIDTRTSAFRDLQGQLA 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 86562857 501 EKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQN 550
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
338-622 |
1.99e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 338 RRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERL-QLERQRKNE 416
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 417 RVRQELEAARKYKLQEEERQRKIQQQKvEMEQIRQQEEARQ-EQLRVLEEERARELERVRQEE--LERQHQMEILRQQEE 493
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAK-KAEAARKAEEVRKaEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 494 DQKKKKLEKDREQREQQEAEELNRMIIEKEMKE-----NKQKMIEEKNKRKMLE-KEMEDRQNAIYEEEERRIAEEERRK 567
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfaRRQAAIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAK 1308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 568 QiEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLAT 622
Cdd:PTZ00121 1309 K-KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
311-457 |
3.83e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.27 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQ--ERLRQEKEEKARELERRRKLEESETARQAELDRQAtiyAEQERMAMERNR-----------ELERI 377
Cdd:pfam15709 362 RLQQEQLERAEKmrEELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQ---RLQLQAAQERARqqqeefrrklqELQRK 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEE--KKRENERVRQEEIAMEISK-------IRELERLQLERQRKNERVRQELEAarkyklqEEERQRKIQQQKVEMEQ 448
Cdd:pfam15709 439 KQQEeaERAEAEKQRQKELEMQLAEeqkrlmeMAEEERLEYQRQKQEAEEKARLEA-------EERRQKEEEAARLALEE 511
|
170
....*....|.
gi 86562857 449 IRQQ--EEARQ 457
Cdd:pfam15709 512 AMKQaqEQARQ 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-622 |
4.03e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 345 SETARQAELDrQATIYAEQERMAmERNRELERIR--LEEKKRENERVRQEEIameiSKIRELERLQLERQRKNERVRQEL 422
Cdd:TIGR02169 659 SRAPRGGILF-SRSEPAELQRLR-ERLEGLKRELssLQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 423 EAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleeeRARELERVRQEELERQHQMEILRQ-QEEDQKKKKLE 501
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-----EDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 502 KDREQREQQEAEELNRM-----IIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIyeeeerrIAEEERRKQIEIEERRR 576
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLtlekeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-------EELEEELEELEAALRDL 880
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 86562857 577 IQQQIMIAtEERSRLDAMEREREMLRQIKESEKQRKELERQELLAT 622
Cdd:TIGR02169 881 ESRLGDLK-KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
333-533 |
4.23e-08 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 55.37 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 333 ARELERRRKLEES-ETARQAELDRQATIYAEQERM-AMERNRELERIRLEEKKRenervrqeeiameiskiRELerLQLE 410
Cdd:pfam12037 35 ARELESSPHAKKAlELMKKQEQTRQAELQAKIKEYeAAQEQLKIERQRVEYEER-----------------RKT--LQEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 411 RQRKNERVRQELEAARKYKLQEEERQRKIQQqkvemEQIRQQEE--ARQEQLRVleeerARELERVRQEELERQHQMEIL 488
Cdd:pfam12037 96 TKQKQQRAQYQDELARKRYQDQLEAQRRRNE-----ELLRKQEEsvAKQEAMRI-----QAQRRQTEEHEAELRRETERA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86562857 489 RQQEEDQKKKKLEKDREQREQqeaeelnRMIIEKeMKENKQKMIE 533
Cdd:pfam12037 166 KAEAEAEARAKEERENEDLNL-------EQLREK-ANEERETVLE 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-615 |
4.40e-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: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 321 EQERLRQEKEE-KARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEIS 399
Cdd:TIGR02168 678 EIEELEEKIEElEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 400 KIRELERLQLERQRKNERVRQELEAARkyklqeEERQRKIQQQKVEMEQIRQQ-EEARQEqlrVLEEERARELERVRQEE 478
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEI------EELEAQIEQLKEELKALREAlDELRAE---LTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 479 LERQHQMEILRQQEEDQKKKKLEKDREQreqqeaeelnrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEER 558
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 559 RIAEEERRKQIEiEERRRIQQQIMIATEERSRLDA-MEREREMLRQIKE--SEKQRKELE 615
Cdd:TIGR02168 896 LEELSEELRELE-SKRSELRRELEELREKLAQLELrLEGLEVRIDNLQErlSEEYSLTLE 954
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
291-621 |
4.87e-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: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 291 ENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEkaRELERRRKLEESETARQAELDRQATIYAEQERMAMER 370
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE--LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 371 NRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARK-----------------YKLQEE 433
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayEAALEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 434 ERQRKIQQQKVEMEQIRQQEEARQEQL---RVLEEERARELERVRQEELERQHQMEILRQQEEDQkkkkLEKDREQREQQ 510
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAAALARGAIGAAVDLVASD----LREADARYYVL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 511 EAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAiyeEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSR 590
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG---GSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
330 340 350
....*....|....*....|....*....|.
gi 86562857 591 LDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-629 |
7.50e-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: 56.60 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 381 EKKRENERVRQEeIAMEISKIRELERLQLERQRKNERVRQELEAARKyklQEEERQRKIQQQKVEMEQirqqEEARQEQL 460
Cdd:TIGR02168 674 ERRREIEELEEK-IEELEEKIAELEKALAELRKELEELEEELEQLRK---ELEELSRQISALRKDLAR----LEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 461 RVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKE----------NKQK 530
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllneeaanLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 531 MIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEiEERRRIQQQIMIATEERSRLD-----AMEREREMLRQIK 605
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-ELIEELESELEALLNERASLEealalLRSELEELSEELR 904
|
250 260
....*....|....*....|....
gi 86562857 606 ESEKQRKELERQELLATTPITTIK 629
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLE 928
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
303-617 |
8.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKfekmEQERLRQEKEEKARELERRRKLEESETARQ--AELDRQATIYAEQERMAMERNRELERIRLE 380
Cdd:COG4717 89 EYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 381 EKKRENERVR-QEEIAMEISKIRELERLQLERQRKN-ERVRQELEAARK--YKLQEEERQRKIQQQKVEMEQIRQQEEAR 456
Cdd:COG4717 165 LEELEAELAElQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEelEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 457 QEQLRV----------------------------------------LEEERARELERVRQEELERQHQMEILRQQEEDQK 496
Cdd:COG4717 245 LKEARLllliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 497 KKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKnKRKMLEKEME---DRQNAIYEEEERRIAEEERRKQIEIEE 573
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAallAEAGVEDEEELRAALEQAEEYQELKEE 403
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 86562857 574 RRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQ 617
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
281-581 |
1.09e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 281 TVRYNGQTMTENEFLNQLLHIVQHQKTVSER---QQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQA--ELDR 355
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIESSKQeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllKLER 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 356 QATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQElEAARKYKLQEEER 435
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE-ELLAKKKLESERL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 436 QRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQhqmEILRQQEEDQKKKKLEKDREQREQQEAEEL 515
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE---EEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 516 NRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQI 581
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
297-617 |
1.97e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 297 QLLHIVQHQKTVSER-QQQEKFEKMEQERLRqEKEEKARELE----------RRRKLEESETARQAELDRQATIYAE--- 362
Cdd:PRK03918 246 ELESLEGSKRKLEEKiRELEERIEELKKEIE-ELEEKVKELKelkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEein 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 363 --QERM--AMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERlQLERQRKN------ERVRQELEAARKYKLQE 432
Cdd:PRK03918 325 giEERIkeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRltgltpEKLEKELEELEKAKEEI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 433 EERQRKIQQQKVEMEQIRQQEEARQEQLRvleeeRARELERVRQEELERQHQMEILRQQEEDQKKkklekdreqreqqea 512
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELK-----KAKGKCPVCGRELTEEHRKELLEEYTAELKR--------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 513 eelnrmiIEKEMKENKQKMIEEKNKRKMLEKEM--EDRQNAIYEEEERRIAEEERRKQIEIEERRR-------------- 576
Cdd:PRK03918 464 -------IEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKLKKYNLEELEKkaeeyeklkeklik 536
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 86562857 577 IQQQIMIATEERSRLDAMERE-REMLRQIKESEKQRKELERQ 617
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKlAELEKKLDELEEELAELLKE 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
303-494 |
2.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEK 382
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 383 KRENERVRQEEIAMEISKIRELERL-------QLER-----QRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIR 450
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86562857 451 QQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEED 494
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
344-617 |
2.38e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.57 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 344 ESETARQAELDRQATIYA-EQERMAMERNRELeriRLEEKKRENERVRQEEiameiskiRELERLQLERQRKNERVRQEL 422
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKrEQEKASRDRLRAE---RAEMRRLEVERKRREQ--------EEQRRLQQEQLERAEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 423 EAARKyKLQEEERQRKiqqQKVEMEQIRQQEEARQEQLRvleeerareleRVRQEELERQHQMEILRQQEEDQKKKKlek 502
Cdd:pfam15709 379 ELEQQ-RRFEEIRLRK---QRLEEERQRQEEEERKQRLQ-----------LQAAQERARQQQEEFRRKLQELQRKKQ--- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 503 dreqreqqeaeelnrmiiekemKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEErriaeeerrkqieiEERRRIQQQIM 582
Cdd:pfam15709 441 ----------------------QEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--------------EERLEYQRQKQ 484
|
250 260 270
....*....|....*....|....*....|....*....
gi 86562857 583 IAtEERSRLDAMEREREMLRQIK----ESEKQRKELERQ 617
Cdd:pfam15709 485 EA-EEKARLEAEERRQKEEEAARlaleEAMKQAQEQARQ 522
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
312-526 |
3.01e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 312 QQQEKFEKMEQERLRQEKEEKARELER----RRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENE 387
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEfneeQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 388 RVRQEeIAMEISKIRELERLQLER---QRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLE 464
Cdd:pfam13868 188 RLRAQ-QEKAQDEKAERDELRAKLyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 465 EERARELERVRQEELER------QHQMEILRQQEEDQKKKKLEK-------DREQREQQEAEELNRMIIEKEMKE 526
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKrrmkrlEHRRELEKQIEEREEQRAAEReeeleegERLREEEAERRERIEEERQKKLKE 341
|
|
| Cep57_CLD |
pfam14073 |
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ... |
295-448 |
3.55e-07 |
|
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.
Pssm-ID: 464080 [Multi-domain] Cd Length: 178 Bit Score: 51.47 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQKTVSERQQQEKF-EKMEQERLRQEKEEKARELERRRKLEEsetaRQAELDRQatiyaeqermaMERNRE 373
Cdd:pfam14073 27 LKQLSRETSHYKEVLQKENDARDpSRGEVSKQNQELISQLAAAESRCSLLE----KQLEYMRK-----------MVENAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 374 LERIRLEEKKRENERVRQEEIAMEISKIRELERLQLE------RQRKNERVRQELEAarkyKLQEEERQRKIQQQKVEME 447
Cdd:pfam14073 92 KERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEylrltrTQSLAETKIKELEE----KLQEEEHQRKLVQEKAAQL 167
|
.
gi 86562857 448 Q 448
Cdd:pfam14073 168 Q 168
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
416-539 |
3.89e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.31 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 416 ERVRQELEAARKyklQEEERQRKIQQQKVEMEQIRQQEEARQEQL--RVLEEERARELERVRQEELERQHQMEILRQQEE 493
Cdd:TIGR02794 53 NRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 86562857 494 DQKKKKLEKDReqreqqeaeelnrmiiEKEMKENKQKMIEEKNKRK 539
Cdd:TIGR02794 130 AEAKAKAEAEA----------------ERKAKEEAAKQAEEEAKAK 159
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
310-619 |
4.81e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKME---QERLRQEKEEKARELERRRKLEESETARQAELDrqatiyaeqerMAMERNRELERIR--LEEKKR 384
Cdd:PRK03918 177 RIERLEKFIKRTeniEELIKEKEKELEEVLREINEISSELPELREELE-----------KLEKEVKELEELKeeIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQEEIAMEIsKIRELE------RLQLERQRKNERVRQELE-AARKY-KLQEEERQRKIQQQKVEMEQIRQQEEAR 456
Cdd:PRK03918 246 ELESLEGSKRKLEE-KIRELEerieelKKEIEELEEKVKELKELKeKAEEYiKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 457 QEQLRVLEEERARELERVRQEELER-QHQMEILRQ-----QEEDQKKKKLEKDREQREQQEAEELNRMI---------IE 521
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKElEKRLEELEErhelyEEAKAKKEELERLKKRLTGLTPEKLEKELeelekakeeIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 522 KEMKENKQKMIEEKNKRKMLEKEM-------------------EDRQNAIYEEEERRIAEEERRKQIEIEER--RRIQQQ 580
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERklRKELRE 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 86562857 581 IMIATEERSRLdamEREREMLRQIKESEKQRKELERQEL 619
Cdd:PRK03918 485 LEKVLKKESEL---IKLKELAEQLKELEEKLKKYNLEEL 520
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
305-461 |
6.10e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEkfekmEQERLRQEkeekaRELERRRKLEEsetarQAELD-RQATIYAEQERmamernrelERIRLEEKK 383
Cdd:COG2268 213 EIAIAQANREA-----EEAELEQE-----REIETARIAEA-----EAELAkKKAEERREAET---------ARAEAEAAY 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 384 RENERVRQEEIAMEISKIRELERLQLERQRKnERVRQELEAARKyKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLR 461
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEA-EREEAELEADVR-KPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKR 344
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
316-423 |
6.87e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 53.59 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 316 KFEKMEQERLRQEKEEKARE------LERRRkLEESETARQAELDRQATIYAEQERMAMERnreLERIRLEEKKRENERV 389
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKalemkiLEKKR-IERLEREERERLERERMERIERERLERER---LERERLERDRLERDRL 504
|
90 100 110
....*....|....*....|....*....|....
gi 86562857 390 RQeeiaMEISKIRELERLQLERQRKNERVRQELE 423
Cdd:PTZ00266 505 DR----LERERVDRLERDRLEKARRNSYFLKGME 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-494 |
7.10e-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: 53.52 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQK--TVSERQQQEKFEKM---EQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAME 369
Cdd:TIGR02168 293 LANEISRLEQQKqiLRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 370 RNRELERIRLEEKKRENERVRQEE-IAMEISKIR-ELERLQLERQRKNERVRQELEAARKYKLQE-----EERQRKIQQQ 442
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIAsLNNEIERLEaRLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEEL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 443 KVEMEQIRQQEEARQEQLRVLEEERARELE---RVRQeeleRQHQMEILRQQEED 494
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERelaQLQA----RLDSLERLQENLEG 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-443 |
8.22e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKaRELERRRKLEESETARqaeldrqatiyAEQERMAMERNreleRIRLEEK 382
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKK-----------AEELKKAEEEN----KIKAEEA 1735
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86562857 383 KR--ENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQK 443
Cdd:PTZ00121 1736 KKeaEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-499 |
8.68e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 321 EQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAE--QERMAMERNRELERIRLEEKKRENER----VRQEEI 394
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELaelpERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 395 AMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQrkIQQQKVEMEQIRQQEEARQEQLRvleeerarelerV 474
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEELEELQQRLAELEEELE------------E 217
|
170 180
....*....|....*....|....*.
gi 86562857 475 RQEELER-QHQMEILRQQEEDQKKKK 499
Cdd:COG4717 218 AQEELEElEEELEQLENELEAAALEE 243
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
299-549 |
1.18e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 51.96 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 299 LHIVQHQKT--VSERQQQEKFEKMEQERLRQEKEEKArELERRRKLEESETARQAELD-RQATIYAEQERMA--MERNRE 373
Cdd:pfam15558 12 LMLARHKEEqrMRELQQQAALAWEELRRRDQKRQETL-ERERRLLLQQSQEQWQAEKEqRKARLGREERRRAdrREKQVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 374 LERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEME-QIRQQ 452
Cdd:pfam15558 91 EKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREeQKKVQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 453 EEARQEQLRVLEeerarelervrqeeleRQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMiiEKEMKENKQKMI 532
Cdd:pfam15558 171 ENNLSELLNHQA----------------RKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEER--HRELREKAQKEE 232
|
250
....*....|....*..
gi 86562857 533 EEKNKRKMLEKEMEDRQ 549
Cdd:pfam15558 233 EQFQRAKWRAEEKEEER 249
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
311-436 |
1.19e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.27 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQatiyaEQERmameRNRELERIRLEEKKRENERVR 390
Cdd:pfam05672 21 RQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRL-----EEER----RREEEERQRKAEEEAEEREQR 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 86562857 391 QEEIAMEISKIRELErlqlERQRKNERVRQELEAARKYKLQEEERQ 436
Cdd:pfam05672 92 EQEEQERLQKQKEEA----EAKAREEAERQRQEREKIMQQEEQERL 133
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-623 |
1.20e-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: 52.76 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKM-EQERLRQEKEEKARELERRRKLEESETARQAELDRQATiYAEQERMAMERNRELERIRLEEKKRENER 388
Cdd:TIGR02169 698 RRIENRLDELSqELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 389 VRQEEIAME-------ISKIRELERLQLERQRKNERVRQELEAARKYKLQEEER-QRKIQQQKVEMEQIRQQEEARQEQL 460
Cdd:TIGR02169 777 LEEALNDLEarlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYlEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 461 rvleeerarELERVRQEELERQHQMEILRQQEEDQKKKKLEKDreqreqqeaeelnRMIIEKEMKENKQKMIEEKNKRKM 540
Cdd:TIGR02169 857 ---------ENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------------RDELEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 541 LEKEMEDRQNAIYEEEERRIAEEERRKQIE------------IEERRRIQQQIMiATEERSRLDAMEREREMLRQIKESE 608
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelsledvQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKE 993
|
330
....*....|....*.
gi 86562857 609 KQRK-ELERQELLATT 623
Cdd:TIGR02169 994 KRAKlEEERKAILERI 1009
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
270-460 |
1.31e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 52.45 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 270 VEELTTMTPEYTVRYNGQTMTENEFLNQLlhiVQHQKTvserqqqeKFEKMEQERLRQEKEEKARelerrrkLEESETAR 349
Cdd:pfam09731 260 QQELVSIFPDIIPVLKEDNLLSNDDLNSL---IAHAHR--------EIDQLSKKLAELKKREEKH-------IERALEKQ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 350 QAELDRQatiyaeqermamernRELERIRLEEKKRENERVRQEEIAMEISKIRE----LERLQLERQRK--NERVRQELe 423
Cdd:pfam09731 322 KEELDKL---------------AEELSARLEEVRAADEAQLRLEFEREREEIREsyeeKLRTELERQAEahEEHLKDVL- 385
|
170 180 190
....*....|....*....|....*....|....*..
gi 86562857 424 aarkyKLQEEERQRKiQQQKVEmEQIRQQEEARQEQL 460
Cdd:pfam09731 386 -----VEQEIELQRE-FLQDIK-EKVEEERAGRLLKL 415
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-612 |
2.05e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQE--RLRQEKEEKARELERRrkleesetarQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENE- 387
Cdd:COG4372 34 RKALFELDKLQEEleQLREELEQAREELEQL----------EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 388 -RVRQEEIAMEiskiRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEE 466
Cdd:COG4372 104 eSLQEEAEELQ----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 467 RARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEME 546
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 547 DRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRK 612
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
315-498 |
2.73e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 315 EKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRElerirlEEKKRENERVRQEEI 394
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 395 AMEISKIRELERLQLERQRK-NERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELER 473
Cdd:TIGR02794 124 AKAKQAAEAKAKAEAEAERKaKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*
gi 86562857 474 VRQEELERQHQMEILRQQEEDQKKK 498
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
295-605 |
2.77e-06 |
|
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: 51.51 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHqktvsERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNREL 374
Cdd:TIGR00618 589 LQNITVRLQD-----LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 375 ERIRLEEKKRENERVRQEEIAMEiSKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQirqQEE 454
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQ-SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA---RED 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 455 ARQEqlrvleeerarelervRQEELERQhQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEK---------EMK 525
Cdd:TIGR00618 740 ALNQ----------------SLKELMHQ-ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlreedthLLK 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 526 ENKQKmIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEI-------EERRRIQQQimiATEERSRLDAMERER 598
Cdd:TIGR00618 803 TLEAE-IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIthqllkyEECSKQLAQ---LTQEQAKIIQLSDKL 878
|
....*..
gi 86562857 599 EMLRQIK 605
Cdd:TIGR00618 879 NGINQIK 885
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
311-537 |
2.78e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQER--LRQEKEEKARELERRRKLEESetaRQAELDRQATIYAEQERMaMERNRELERIRLEEKKRENE- 387
Cdd:pfam05483 366 RTEQQRLEKNEDQLkiITMELQKKSSELEEMTKFKNN---KEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQEl 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 388 ----RVRQEEI---AMEISKIRELERL------QLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEE 454
Cdd:pfam05483 442 ifllQAREKEIhdlEIQLTAIKTSEEHylkeveDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 455 ----ARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQK 530
Cdd:pfam05483 522 iincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
....*..
gi 86562857 531 MIEEKNK 537
Cdd:pfam05483 602 QIENKNK 608
|
|
| MFAP1 |
pfam06991 |
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ... |
309-437 |
2.94e-06 |
|
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.
Pssm-ID: 462060 [Multi-domain] Cd Length: 215 Bit Score: 49.09 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 309 SERQQQEKFEKMEQERLRQEKEEKARELERRrklEESETARQAELDRQAtiyaeQERMAMERNRELERIrlEEKKRENEr 388
Cdd:pfam06991 20 SKRGTIAEREKLEAEEEEEEEEAKKEAEERK---KEADKLVEEEIRREA-----AAKEAGDEDENEEDV--DDTDGLDP- 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 86562857 389 vrqeEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQR 437
Cdd:pfam06991 89 ----EAEYEAWKLRELKRIKRDREEREAREKEREEIERRRNMTEEERLA 133
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
305-547 |
3.13e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELdrqatiyaeqermamernrELERIRLEEKKR 384
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA-------------------EEELERLEEEIT 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLE 464
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 465 EERARELERVRQEELERQHQMEilRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKE 544
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLL--LAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
...
gi 86562857 545 MED 547
Cdd:pfam02463 1023 LEL 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-543 |
3.58e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKEEKAREL----ERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEekkreneRVRQEEIAMEI 398
Cdd:COG1196 564 EYLKAAKAGRATFLpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR-------TLVAARLEAAL 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 399 SKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEE 478
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 479 LERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEK 543
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
401-621 |
4.25e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 401 IRELERLQLERQRKNERVRQELEAARKYKLQEEER------QRKIQQQKVEMEQIRQQEEARQEQLRvleeerarelerv 474
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEkeeerkEERKRYRQELEEQIEEREQKRQEEYE------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 475 rQEELERQHQMEILRQ-QEEDQKKKKLEKDREQREQQEAEELNRMIIE-KEMKENKQKMIEEKNKRKMLEKEMEDRQNAi 552
Cdd:pfam13868 95 -EKLQEREQMDEIVERiQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwKELEKEEEREEDERILEYLKEKAEREEERE- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86562857 553 yeeeeRRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:pfam13868 173 -----AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
319-458 |
7.10e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 319 KMEQERLRQEKEEKARE--LERRRKLEESETARQAELDRqatiyaeQERMAMERNRELERiRLEEKKRENERVRQEEIAM 396
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEeiHKLRNEFEKELRERRNELQK-------LEKRLLQKEENLDR-KLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 397 EiSKIRELERLQLERQRKNERVRQELEAARKYKlQEEERQRKIQQQKVEMEQ-----IRQ-QEEARQE 458
Cdd:PRK12704 120 E-QKQQELEKKEEELEELIEEQLQELERISGLT-AEEAKEILLEKVEEEARHeaavlIKEiEEEAKEE 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-444 |
7.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 287 QTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERM 366
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 367 AMERNRELERIRLEEKKRENERVRQEEIAMEISKI---RELERLQLERQRKNERVRQELEAARKYKLQE---EERQRKIQ 440
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLeedGELAELLQELEELKAELRELAEEWAALKLALellEEAREEYR 510
|
....
gi 86562857 441 QQKV 444
Cdd:COG4717 511 EERL 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
295-462 |
7.93e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQKTVseRQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIyAEQERMAMERnrel 374
Cdd:COG4913 251 IELLEPIRELAERY--AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER-LEARLDALRE---- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 375 ERIRLEEKKRENERVRQEEIAmeiskiRELERLQLERQRKNERVRQELEAARKYKLQE-------EERQRKIQQQKVEME 447
Cdd:COG4913 324 ELDELEAQIRGNGGDRLEQLE------REIERLERELEERERRRARLEALLAALGLPLpasaeefAALRAEAAALLEALE 397
|
170
....*....|....*
gi 86562857 448 QIRQQEEARQEQLRV 462
Cdd:COG4913 398 EELEALEEALAEAEA 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
318-498 |
9.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 318 EKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAmERNRELERIRLEEKKRENERVRQEEIAME 397
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 398 ISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQE 477
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180
....*....|....*....|.
gi 86562857 478 ELERQHQMEILRQQEEDQKKK 498
Cdd:COG4717 208 LAELEEELEEAQEELEELEEE 228
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
406-539 |
1.22e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 406 RLQLERQRKNERVR-----QELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVR----- 475
Cdd:TIGR02794 56 QQQKKPAAKKEQERqkkleQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeakak 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 476 -QEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEelnRMIIEKEMKENKQKMIEEKNKRK 539
Cdd:TIGR02794 136 aEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKK---AEAEAKAKAEAEAKAKAEEAKAK 197
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
311-552 |
1.25e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEKEEKA----RELERR-RKLEESETARQAELDRQATIYAEQERMamernreleRIRLEEKKRE 385
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAeselKELEKKhQQLCEEKNALQEQLQAETELCAEAEEM---------RARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 386 NERVRQEeiaMEISKIRELER---LQLERQRKNERVrQELEAarkyKLQEEERQRkiqqQKVEMEQIRQQEEARQEQLRV 462
Cdd:pfam01576 73 LEEILHE---LESRLEEEEERsqqLQNEKKKMQQHI-QDLEE----QLDEEEAAR----QKLQLEKVTTEAKIKKLEEDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 463 LEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMiiekeMKENKQKMIEEKNKRKmLE 542
Cdd:pfam01576 141 LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERL-----KKEEKGRQELEKAKRK-LE 214
|
250
....*....|
gi 86562857 543 KEMEDRQNAI 552
Cdd:pfam01576 215 GESTDLQEQI 224
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
303-437 |
1.28e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQaELDRQAtiyAEQERMAMERNRELErirlEEK 382
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQA---EEAAKQAALKQKQAE----EAA 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86562857 383 KRENERVR-----QEEIAMEISKIRELE---RLQLERQRKNE-RVRQELEAARKYKLQEEERQR 437
Cdd:PRK09510 139 AKAAAAAKakaeaEAKRAAAAAKKAAAEakkKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKK 202
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
295-619 |
1.41e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQKTVSErqQQEKFEKMEQERLRQEKEEKARELERRRKL-------EESETARQAELDRQATIYAEQERMA 367
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLT--QKLQSLCKELDILQREQATIDTRTSAFRDLqgqlahaKKQQELQQRYAELCAAAITCTAQCE 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 368 MERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERV----RQELEAARKYKLQEEERQRKIQQQK 443
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRMQRGE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 444 VEMEQIRQQEEARQEQLrvleEERARELERVRQEELERQHQMEILRQQ----EEDQKKKKLEKDREQREQQEAEELNRMI 519
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQL----TSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 520 IEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMERERE 599
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
330 340
....*....|....*....|
gi 86562857 600 MLRQIKESEKQRKELERQEL 619
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELE 710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
305-498 |
1.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEkeEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKR 384
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQ----EEIAMEISKIRELERLQLERQRKNERVRQELEAARKY--KLQEEERQRKIQQQKVEMEQIRQQEEARQE 458
Cdd:COG4717 374 ALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELRE 453
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 86562857 459 QLRvleeerareLERVRQEELERQHQMEILRQQEEDQKKK 498
Cdd:COG4717 454 ELA---------ELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
302-601 |
1.52e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.71 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 302 VQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQAT-----IYAEQERMAMERNRELER 376
Cdd:pfam02029 38 PNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIAdekesVAERKENNEEEENSSWEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 377 irleEKKRENERVRQEEIAMEIS-------KIRELERLQLERQRKNERVRQELEAARKYKLQEEE----RQRKIQQQKVE 445
Cdd:pfam02029 118 ----EEKRDSRLGRYKEEETEIRekeyqenKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEvkdeKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 446 MEQIRQQEEARQEQlrvLEEERARELERVRQEELERQHQMEILRQQEEDQKK-----KKLEKDREQREQQEaeelnrmii 520
Cdd:pfam02029 194 SKVFLDQKRGHPEV---KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQEKE--------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 521 EKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQImiateERSRLDAMEREREM 600
Cdd:pfam02029 262 SEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEI-----ERRRAEAAEKRQKL 336
|
.
gi 86562857 601 L 601
Cdd:pfam02029 337 P 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
315-629 |
1.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 315 EKFEKMEQERLRQEKEEKA--------RELERRRKLEESETARQAELDrqatiyaeqermamERNRELERiRLEEKKREN 386
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAyknlgeviKEIKRRIERLEKFIKRTENIE--------------ELIKEKEK-ELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 387 ERVRQEEIameiSKIRELERLQlERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvleee 466
Cdd:PRK03918 210 NEISSELP----ELREELEKLE-KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 467 RARELERVRQEELERQHQMEILRQQEEDqKKKKLEKdREQREQQEAEELNRMIIEKEMKENKQKMIEEKnkrkmlEKEME 546
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLD-ELREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKK------LKELE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 547 DRQNaiyeeeerriaeeerrkqiEIEERRRIQQQIMIATEERSRLDAMERER---EMLRQIKESEKQRKELERQELLATT 623
Cdd:PRK03918 352 KRLE-------------------ELEERHELYEEAKAKKEELERLKKRLTGLtpeKLEKELEELEKAKEEIEEEISKITA 412
|
....*.
gi 86562857 624 PITTIK 629
Cdd:PRK03918 413 RIGELK 418
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
379-501 |
1.95e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.80 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 379 LEEKKR--ENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAAR---KYKLQEEERQRKIQQQKVEMEQIRQQE 453
Cdd:pfam05672 16 LAEKRRqaREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRleeERRREEEERQRKAEEEAEEREQREQEE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 86562857 454 EARQEQLRVLEEERARELERVRQEELERQHQMEilrQQEEDQKKKKLE 501
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEAERQRQEREKIMQQE---EQERLERKKRIE 140
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
372-503 |
2.07e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 372 RELERIRLEEKKRENERVRQEEIAMEiSKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQ 451
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 86562857 452 QEEARQEQLRVLEeerarelervrqEELERQHQMEiLRQQEEDQKKKKLEKD 503
Cdd:COG2268 271 AEANAEREVQRQL------------EIAEREREIE-LQEKEAEREEAELEAD 309
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
305-593 |
2.69e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQER-LRQEKEEKARELERRRKLEESETARQAE----------LDRQATIYAEQERMAMERNR- 372
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKrAAAEAEQKAKEEAEEERLAELEAKRQAEeeareakaeaEQRAAELAAEAAKKLAEAEKa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 373 --ELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIR 450
Cdd:COG3064 86 aaEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 451 QQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQK 530
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86562857 531 MIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDA 593
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
307-461 |
2.78e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.28 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 307 TVSERQQQEKFEKM--EQERLRQEKEEKAREL---------ERRRKLEESETARQAELDRQAT----------------- 358
Cdd:NF041483 516 TTLRRQAEETLERTraEAERLRAEAEEQAEEVraaaeraarELREETERAIAARQAEAAEELTrlhteaeerltaaeeal 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 359 --IYAEQERMAMERNRELERIRLEEKKR----------ENERVRqEEIAMEISKIR----------------ELERLQLE 410
Cdd:NF041483 596 adARAEAERIRREAAEETERLRTEAAERirtlqaqaeqEAERLR-TEAAADASAARaegenvavrlrseaaaEAERLKSE 674
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 411 RQRKNERVRQEL---------EAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLR 461
Cdd:NF041483 675 AQESADRVRAEAaaaaervgtEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
301-458 |
2.83e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 301 IVQHQKTVSERQQQekfekmeQERLRQEKEEKARELERRRklEESETAR-QAELDRQATIYAEQERMAMERNRE-LERIR 378
Cdd:PRK02224 525 IAERRETIEEKRER-------AEELRERAAELEAEAEEKR--EAAAEAEeEAEEAREEVAELNSKLAELKERIEsLERIR 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 379 LEEKKRENERVRQEEIAMEISKIRELERLQLER-QRKNERVRQ---ELEAARKYKLQEEERQRKIQQQKVEmEQIRQQEE 454
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRERlAEKRERKREleaEFDEARIEEAREDKERAEEYLEQVE-EKLDELRE 674
|
....
gi 86562857 455 ARQE 458
Cdd:PRK02224 675 ERDD 678
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
303-462 |
3.09e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.34 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRK------LEESETARQAELDRQatIYAEQERMAM-ERNRELE 375
Cdd:pfam15558 84 RREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKqcqeqrLKEKEEELQALREQN--SLQLQERLEEaCHKRQLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 376 RIRLEEKKRENER-------VRQEEIAMEISKIRELERLQLE-RQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEmE 447
Cdd:pfam15558 162 EREEQKKVQENNLsellnhqARKVLVDCQAKAEELLRRLSLEqSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAK-W 240
|
170
....*....|....*
gi 86562857 448 QIRQQEEARQEQLRV 462
Cdd:pfam15558 241 RAEEKEEERQEHKEA 255
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
378-498 |
3.10e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKI--QQQKVEMEQIRQQEEA 455
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalKQKQAEEAAAKAAAAA 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 86562857 456 R----QEQLRVleeeraRELERVRQEELERQHQMEILRQQEEDQKKK 498
Cdd:PRK09510 146 KakaeAEAKRA------AAAAKKAAAEAKKKAEAEAAKKAAAEAKKK 186
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
309-442 |
3.24e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.02 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 309 SERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYaeqermamernrelerirlEEKkrener 388
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEL-------------------EEK------ 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 86562857 389 vrQEEIAMEISKIRElERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQ 442
Cdd:PRK11448 193 --QQELEAQLEQLQE-KAAETSQERKQKRKEITDQAAKRLELSEEETRILIDQQ 243
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
310-618 |
3.26e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKMEQERLRQEKEEKARELERRRklEESETARQAELDRQATIY----AEQERMAMERNRELERIRLEEKKRE 385
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTES--VEPNEHNSYEEDSELKPSgqggLDEEEAFLDRTAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 386 NERVRQ-EEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEE---RQRKIQQQKVEMEQIRQQEEARQEQLR 461
Cdd:pfam02029 83 LERQKEfDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteiREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 462 VLEEERARELERVRQEELERQHQMEILRQQE----EDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNK 537
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYEskvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 538 RKMLEKEMED--RQNAiyeeeerriaeeerrkQIEIEERRRIQQQIMIATEErsrLDAMEREREMLRQIKESEKQRKELE 615
Cdd:pfam02029 243 FLEAEQKLEElrRRRQ----------------EKESEEFEKLRQKQQEAELE---LEELKKKREERRKLLEEEEQRRKQE 303
|
...
gi 86562857 616 RQE 618
Cdd:pfam02029 304 EAE 306
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
348-628 |
3.85e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 348 ARQAELDRQaTIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARK 427
Cdd:pfam05557 2 AELIESKAR-LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 428 YKLQEEERQRKIQQQKVEMEQIRQ-----QEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEK 502
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREvisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 503 DREQREQQeaeelnrmiiEKEMKENKQKmIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEErrkqiEIEERRRIQQQIM 582
Cdd:pfam05557 161 QQSSLAEA----------EQRIKELEFE-IQSQEQDSEIVKNSKSELARIPELEKELERLRE-----HNKHLNENIENKL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 86562857 583 IATEE----RSRLDAMEREREMLRQIK-ESEKQRKELERQELLATTPITTI 628
Cdd:pfam05557 225 LLKEEvedlKRKLEREEKYREEAATLElEKEKLEQELQSWVKLAQDTGLNL 275
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
323-551 |
4.73e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKEEKARElERRRKLEESETARQAELDRQAtiyaEQERMAmernreleriRLEEKKRENERVRQEEIAmeiskir 402
Cdd:TIGR02794 53 NRIQQQKKPAAKK-EQERQKKLEQQAEEAEKQRAA----EQARQK----------ELEQRAAAEKAAKQAEQA------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 403 elerlqleRQRKNERVRQELEAARKyklQEEERQRKIQQ---QKVEMEQIRQQEEARQEQlrvleeerarelervRQEEL 479
Cdd:TIGR02794 111 --------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAeaeRKAKEEAAKQAEEEAKAK---------------AAAEA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86562857 480 ERQhQMEILRQQEEDQKKKKLEKDREQREQQEaeelnrmiieKEMKENKQKMIEEKNKRKMLEKEMEDRQNA 551
Cdd:TIGR02794 165 KKK-AEEAKKKAEAEAKAKAEAEAKAKAEEAK----------AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-622 |
4.88e-05 |
|
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: 47.36 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 369 ERNRELERiRLEEKKRENERVrqEEIAMEISkiRELERLQLERQRKNE--RVRQELEAARKYKL-----QEEERQRKIQQ 441
Cdd:TIGR02168 172 ERRKETER-KLERTRENLDRL--EDILNELE--RQLKSLERQAEKAERykELKAELRELELALLvlrleELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 442 QKVEMEQIRQQEEARQ-------EQLRVLEEERARELERVRQEELERQHQMEILRQQEE--DQKKKKLEKDREQREQQEA 512
Cdd:TIGR02168 247 ELKEAEEELEELTAELqeleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 513 EELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLD 592
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270
....*....|....*....|....*....|....*
gi 86562857 593 A----MEREREMLRQIKES-EKQRKELERQELLAT 622
Cdd:TIGR02168 407 ArlerLEDRRERLQQEIEElLKKLEEAELKELQAE 441
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
317-613 |
5.54e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 317 FEKMEQERLRQEKEE-KARELERRRKLEESETARQAeLDRQATIYAEQERMAMERNREL--ERIRLE------EKKRENE 387
Cdd:PRK02224 304 LDDADAEAVEARREElEDRDEELRDRLEECRVAAQA-HNEEAESLREDADDLEERAEELreEAAELEseleeaREAVEDR 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 388 RVRQEEIAMEISKIRE---------------LERLQLERQRKNERVRqELEAARKyklQEEERQRKIQQ----------- 441
Cdd:PRK02224 383 REEIEELEEEIEELRErfgdapvdlgnaedfLEELREERDELREREA-ELEATLR---TARERVEEAEAlleagkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 442 QKVEMEQIRQQEEARQEqlRVLEEERARELERVRQEELERQHqmeilrqqEEDQKKKKLEKDREQREQQEAEELNRMIIE 521
Cdd:PRK02224 459 QPVEGSPHVETIEEDRE--RVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEELIAER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 522 KEMKENKQKMIEEKNKRKM-LEKEMEDRQNAIYEEEERRIAEEERRKQIE---------IEERRRIQQQIMIATEERSRL 591
Cdd:PRK02224 529 RETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEAREEVAELNsklaelkerIESLERIRTLLAAIADAEDEI 608
|
330 340
....*....|....*....|..
gi 86562857 592 damEREREMLRQIKESEKQRKE 613
Cdd:PRK02224 609 ---ERLREKREALAELNDERRE 627
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-584 |
5.58e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQ 457
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 458 EQLRVLEEERARELERVRQEELERQhqMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNK 537
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEER--LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86562857 538 RKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIA 584
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-494 |
5.59e-05 |
|
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: 47.36 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 293 EFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEK-----EEKARELERRRKLEESE-TARQAELDRQATIYAEQE-- 364
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieelEAQIEQLKEELKALREAlDELRAELTLLNEEAANLRer 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 365 RMAMERNRELERIRLE--EKKRENERVRQEEIAMEISKIRE-LERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQ 441
Cdd:TIGR02168 826 LESLERRIAATERRLEdlEEQIEELSEDIESLAAEIEELEElIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 86562857 442 QKVEMEQIRQQEEARQEQLrvleeerARELERVRQEELERQHQMEILRQQEED 494
Cdd:TIGR02168 906 LESKRSELRRELEELREKL-------AQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
324-498 |
6.96e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 324 RLRQEKEEKARELERRRKLEEsetaRQAELDRQATIyAEQERMamernRELERIRLEEKKrenERVRQEEIAmeiskire 403
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQ----QQAEELQQKQA-AEQERL-----KQLEKERLAAQE---QKKQAEEAA-------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 404 leRLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEME-QIRQQEEARQEQLRVLEEERARELERVRQEELERQ 482
Cdd:PRK09510 125 --KQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170
....*....|....*.
gi 86562857 483 HQMEILRQQEEDQKKK 498
Cdd:PRK09510 203 AEAEAKKKAAAEAKKK 218
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
322-603 |
7.17e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 322 QERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIR--LEEKKRENERVRQEEIAMEIS 399
Cdd:pfam01576 277 QEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaLEEETRSHEAQLQEMRQKHTQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 400 KIRELERlQLERQRKN----ERVRQELEAARKyKLQEEerQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVR 475
Cdd:pfam01576 357 ALEELTE-QLEQAKRNkanlEKAKQALESENA-ELQAE--LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 476 QEELERQHQMEILRQ--QEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKEN-----KQKMIEEKNKRKMLEKEMEDR 548
Cdd:pfam01576 433 EKLSKLQSELESVSSllNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAK 512
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 549 QNAIYEEEERRIAEEERRKQIE--------IEE-RRRIQQQIMIAT----EERSRLDAMEREREMLRQ 603
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEedagtleaLEEgKKRLQRELEALTqqleEKAAAYDKLEKTKNRLQQ 580
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
315-386 |
8.08e-05 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 44.66 E-value: 8.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86562857 315 EKFEKMEQERLRQEKEEKAReLERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKREN 386
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAER-LEEERREEEEEERLAAEQDRRAEELEELKHLLEERKEALEKLRAEAREEAE 71
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
378-621 |
8.96e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVRQEEIAMEISKIR-ELERLQLERQRK------NERVRQELEAaRKYKLQEEERQRKIQQQKvemeQIR 450
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRRdQKRQETLERERRlllqqsQEQWQAEKEQ-RKARLGREERRRADRREK----QVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 451 QQEEARQEQLRVLEEERARELERVRQEELER-QHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIieKEMKEnkQ 529
Cdd:pfam15558 91 EKESRWREQAEDQENQRQEKLERARQEAEQRkQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQL--KEREE--Q 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 530 KMIEEKNKRKMLEKEMEDRQNAiyeeeeRRIAEEERRKQIEIEER----RRIQQQIMIATEERSRLDAMeREREMLRQIK 605
Cdd:pfam15558 167 KKVQENNLSELLNHQARKVLVD------CQAKAEELLRRLSLEQSlqrsQENYEQLVEERHRELREKAQ-KEEEQFQRAK 239
|
250
....*....|....*...
gi 86562857 606 E--SEKQRKELERQELLA 621
Cdd:pfam15558 240 WraEEKEEERQEHKEALA 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-552 |
1.11e-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: 45.53 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 321 EQERLRQEKEEKARELERRRKLEESETARQAELDRQatiYAEQERMAMERNRELERIrleEKKRENERVRQEEIAMEISK 400
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRAL---EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 401 IRElerlQLERQRKN--ERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEE 478
Cdd:COG4942 95 LRA----ELEAQKEElaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86562857 479 LERQHQMEILRQQEEDQKKKKLEKDREQREQQEaeelnrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAI 552
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLAR--------LEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
313-685 |
1.31e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 313 QQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQErmAMErnrELERIRLEEKKRENErvRQE 392
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ--AEE---EAREAKAEAEQRAAE--LAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 393 EIAMEISKI-RELERLQLERQRKNERVRQELEAARKY-KLQEEERQRKIQQQKVEMEQ--IRQQEEARQEQLRVLEEERA 468
Cdd:COG3064 74 EAAKKLAEAeKAAAEAEKKAAAEKAKAAKEAEAAAAAeKAAAAAEKEKAEEAKRKAEEeaKRKAEEERKAAEAEAAAKAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 469 RELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDR 548
Cdd:COG3064 154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 549 QNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKEsEKQRKELERQELLATTPITTI 628
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAA-AAGLVLDDSAALAAELLGAVA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 86562857 629 KPIYRPDISEYRPPDVESHMIRFTTQSPEWATPSPTWNPAWNTVTAEEETPGIPIIH 685
Cdd:COG3064 313 AEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAA 369
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
305-461 |
1.43e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKleesETARQAELDRQATIYAEQERMAMERNR----ELERIRLE 380
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA----EQAAKQAEEKQKQAEEAKAKQAAEAKAkaeaEAERKAKE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 381 EKKRENERVRQEEIAMEISKIRELERLQLERQRKnervrQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQL 460
Cdd:TIGR02794 147 EAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK-----AKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
.
gi 86562857 461 R 461
Cdd:TIGR02794 222 A 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
424-623 |
1.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 424 AARKYKLQEEERQRKIQQQKVEMEQIRQQE--EARQEQLRvleeERARELERVRQEELERQHQMEILRQQEE--DQKKKK 499
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEAllEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEEnlDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 500 LEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRkmLEKEMedrqnaiyeeeerriaeeerrkQIEIEERRriqQ 579
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE--LERIS----------------------GLTAEEAK---E 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 86562857 580 QIMIATEERSRLDAMererEMLRQIKESEKQRKELERQELLATT 623
Cdd:PRK12704 158 ILLEKVEEEARHEAA----VLIKEIEEEAKEEADKKAKEILAQA 197
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
384-635 |
1.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 384 RENERVRQEEIAMEISKIRElerlQLERQRKN-ERVRQELEA-ARKYKL--------QEEERQRKIQQQKVEMEQIRQQE 453
Cdd:COG3206 163 EQNLELRREEARKALEFLEE----QLPELRKElEEAEAALEEfRQKNGLvdlseeakLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 454 EARQEQLRVLEEERARELERVRQEELERQhqmeiLRQQEEDQKKKKLEkdreqreqqeaeelnrmiIEKEMKENKQKMIE 533
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAE------------------LSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 534 EKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKES-EKQRK 612
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLE 375
|
250 260
....*....|....*....|...
gi 86562857 613 ELERQELLATTPITTIKPIYRPD 635
Cdd:COG3206 376 EARLAEALTVGNVRVIDPAVVPL 398
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
361-457 |
1.60e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 43.14 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 361 AEQERMAMERNRELERIR--LEEKKRENERVRQEEIAM------EISKIRELERLQLERQRKNERVRQELEAARKYKLQE 432
Cdd:pfam11600 11 EEKEKQRLEKDKERLRRQlkLEAEKEEKERLKEEAKAEkerakeEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKE 90
|
90 100
....*....|....*....|....*
gi 86562857 433 EERQRKIQQQKVEMEQIRQQEEARQ 457
Cdd:pfam11600 91 EKRKEKQEALEAKLEEKRKKEEEKR 115
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
361-623 |
1.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 361 AEQERMAMERNRELERiRLEEKKRENERVRQEEIAMEiskiRELERLQLERQRKNERVRQ---ELEAARKYKLQEEERQR 437
Cdd:COG4372 30 SEQLRKALFELDKLQE-ELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEElneQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 438 KIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEdQKKKKLEKDREQREQQEAEELNR 517
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE-SLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 518 MIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMERE 597
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260
....*....|....*....|....*.
gi 86562857 598 REMLRQIKESEKQRKELERQELLATT 623
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALE 289
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-415 |
2.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSER----QQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQAtiyAEQERMAMERNRELERI- 377
Cdd:PRK12704 72 EFEKELRERrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERIs 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 86562857 378 ---RLEEKKRENERVRQE---EIAMEISKIRELERLQLERQRKN 415
Cdd:PRK12704 149 gltAEEAKEILLEKVEEEarhEAAVLIKEIEEEAKEEADKKAKE 192
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
305-392 |
2.20e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.20 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELE-RRRKLEESETARQAELDR-QATIYAEQERMAMERNRELERIRLEEK 382
Cdd:pfam02841 203 EKAIEAERAKAEAAEAEQELLREKQKEEEQMMEaQERSYQEHVKQLIEKMEAeREQLLAEQERMLEHKLQEQEELLKEGF 282
|
90
....*....|
gi 86562857 383 KRENERVRQE 392
Cdd:pfam02841 283 KTEAESLQKE 292
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
323-459 |
2.32e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKE---EKARELERRRKLEESETARQA-----ELDRQATIYAEQERMA--MERNRELERIRLEEKKRENERV--- 389
Cdd:pfam05262 184 EALREDNEkgvNFRRDMTDLKERESQEDAKRAqqlkeELDKKQIDADKAQQKAdfAQDNADKQRDEVRQKQQEAKNLpkp 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 390 -----RQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQ 459
Cdd:pfam05262 264 adtssPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ 338
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
285-623 |
2.61e-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: 45.01 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 285 NGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEkarelERRRKLEESETARQAELDRQATIYAEQE 364
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ-----DWNKELKSELKNQEKKLEEIQNQISQNN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 365 RMAMERNRELERIRLEEKKRENERV-RQEEIAmeiSKIRELERLQLERQRKNervrQELEaarKYKLQEEERQRKIQQQK 443
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSeKQRELE---EKQNEIEKLKKENQSYK----QEIK---NLESQINDLESKIQNQE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 444 VEMEQIRQQEEARQEQLRVLEEERARELERVRQ-------------------EELER-----QHQMEILR------QQEE 493
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvkeliiKNLDNtreslETQLKVLSrsinkiKQNL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 494 DQKKKKLEKDREQREQQEAEELNrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIE- 572
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKE---LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEk 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 86562857 573 ERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQ--RKELERQELLATT 623
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlIKEIEEKEKKISS 614
|
|
| tape_meas_lam_C |
TIGR01541 |
phage tail tape measure protein, lambda family; This model represents a relatively ... |
348-455 |
2.63e-04 |
|
phage tail tape measure protein, lambda family; This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273681 [Multi-domain] Cd Length: 332 Bit Score: 44.44 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 348 ARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQ--------RKNERVR 419
Cdd:TIGR01541 7 TQQIADRKLKKLNTADEKSLQSRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQldrfglgdKQRERLD 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 86562857 420 QELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEA 455
Cdd:TIGR01541 87 ARLQIDRTFRKQQRDLNKAMTAKGLAGSDLYKEQLA 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
291-601 |
3.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 291 ENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIY---------- 360
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavligve 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 361 -------------AEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQEL--EAA 425
Cdd:COG1196 534 aayeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLreADA 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 426 RKYKLQEEERQRKIQQQKVEMEqIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDRE 505
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 506 QREQQEaeelnrmiiEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIAT 585
Cdd:COG1196 693 LELEEA---------LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
330
....*....|....*.
gi 86562857 586 EERSRLDAMEREREML 601
Cdd:COG1196 764 ELERELERLEREIEAL 779
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
310-460 |
3.50e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.15 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKMEQERLRQ-EKEEKARELERRRKLEESEtarqaeldrqatiyaEQERMAMERNRELerirLEEKKRENER 388
Cdd:pfam13904 50 ERQPLEAYENWLAAKQRQrQKELQAQKEEREKEEQEAE---------------LRKRLAKEKYQEW----LQRKARQQTK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86562857 389 VRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKvemEQIRQQEEARQEQL 460
Cdd:pfam13904 111 KREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQRE---QLKKEEEEQERKQL 179
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
263-619 |
3.94e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 263 RRPDSFGVEEL--TTMTPEYTVRYNGQTMTENEFLNQLLhIVQHQKTVSERQQQEKF---EKMEQERLRQ---EKEEKAR 334
Cdd:pfam05483 344 KAAHSFVVTEFeaTTCSLEELLRTEQQRLEKNEDQLKII-TMELQKKSSELEEMTKFknnKEVELEELKKilaEDEKLLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 335 ELERRRKLEESETARQAEL-----DRQATIYAEQERMAMERNRE---LERIRLEEKKRENERVRQEEIAMEISKI----- 401
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQELifllqAREKEIHDLEIQLTAIKTSEehyLKEVEDLKTELEKEKLKNIELTAHCDKLllenk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 402 ---RELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEE 478
Cdd:pfam05483 503 eltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 479 LERQHQMEI-------LRQQEEDQKK--KKLEKDREQREQQEAEElNRMIIEKEMKENKQKMIEEKNKRKMLE------K 543
Cdd:pfam05483 583 LKKEKQMKIlenkcnnLKKQIENKNKniEELHQENKALKKKGSAE-NKQLNAYEIKVNKLELELASAKQKFEEiidnyqK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 544 EMEDRQNAIYE-----EEERRIAEEERRKQIEIEER--RRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELER 616
Cdd:pfam05483 662 EIEDKKISEEKlleevEKAKAIADEAVKLQKEIDKRcqHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK 741
|
...
gi 86562857 617 QEL 619
Cdd:pfam05483 742 AAL 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
305-552 |
4.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERrrkLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKR 384
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQ---LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQEEIAMEI-SKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVL 463
Cdd:COG4372 121 QKERQDLEQQRKQLeAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 464 EEERARELERVRQEELERQHQMEILR---------------QQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENK 528
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSleaklglalsalldaLELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260
....*....|....*....|....
gi 86562857 529 QKMIEEKNKRKMLEKEMEDRQNAI 552
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNL 304
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-619 |
4.27e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 369 ERNRELERIR--LEEKKRENERVRqeeiAMEISKIRELERLQLER---------QRKNERVRQ-----ELEAARKYK--- 429
Cdd:TIGR02169 167 EFDRKKEKALeeLEEVEENIERLD----LIIDEKRQQLERLRRERekaeryqalLKEKREYEGyellkEKEALERQKeai 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 430 ------LQEE--ERQRKIQQQKVEMEQIRQ-------------QEEARQEQLRVLEEERARELERVRQEELERQ-HQMEI 487
Cdd:TIGR02169 243 erqlasLEEEleKLTEEISELEKRLEEIEQlleelnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERElEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 488 LRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKM------IEEKNKR--------KMLEKEMEDRQNAIY 553
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeLEEVDKEfaetrdelKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86562857 554 EEEERRIAEEERRKQIEiEERRRIQQQIMIATEE-----------RSRLDAMEREREMLRQIKESEKQRKELERQEL 619
Cdd:TIGR02169 403 ELKRELDRLQEELQRLS-EELADLNAAIAGIEAKineleeekedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-539 |
5.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 334 RELERRRKLEESETARQAELDRQAtIYAEQERMAMERNRELERIRLEEKKRENERvRQEEIAMEISKIRElERLQLERQR 413
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKE-LKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELRE-ELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 414 KNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMeILRQQEE 493
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL-AEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 86562857 494 DQKKKKLEKDREQREQqeaeelNRMIIEKEMKENKQKMIEEKNKRK 539
Cdd:COG4717 205 QQRLAELEEELEEAQE------ELEELEEELEQLENELEAAALEER 244
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
311-609 |
6.13e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.13 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLR-------QEKE-----EKARELERRRKLEESETAR-QAELDRQATIYAEQERMAMERNRELERI 377
Cdd:pfam15742 9 YQQQEEVQQLRQNLQRlqilctsAEKElryerGKNLDLKQHNSLLQEENIKiKAELKQAQQKLLDSTKMCSSLTAEWKHC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVR-----------QEEIAMEISKIRELERLQLERQRKNERVRQ----------------------ELEA 424
Cdd:pfam15742 89 QQKIRELELEVLKqaqsiksqnslQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilekkqleerikeasENEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 425 ARKYKLQEEERQRKIQQQKVE--MEQIR--QQEEARQEQLRVLEEERARELERVRQE-ELERQHQMEILR-QQEEDQKKK 498
Cdd:pfam15742 169 KLKQQYQEEQQKRKLLDQNVNelQQQVRslQDKEAQLEMTNSQQQLRIQQQEAQLKQlENEKRKSDEHLKsNQELSEKLS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 499 KLEKDREQREQQEAEELNRMiiEKEMKENKQKMIEEKNK----RKMLEKEMEDRQNAIyeeEERRIAEEERRKQIEIEER 574
Cdd:pfam15742 249 SLQQEKEALQEELQQVLKQL--DVHVRKYNEKHHHHKAKlrraKDRLVHEVEQRDERI---KQLENEIGILQQQSEKEKA 323
|
330 340 350
....*....|....*....|....*....|....*
gi 86562857 575 RriQQQIMiatEERSRLdaMEREREMLRQIKESEK 609
Cdd:pfam15742 324 F--QKQVT---AQNEIL--LLEKRKLLEQLTEQEE 351
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-503 |
6.21e-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: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 339 RRKLEESETARQAELDRQATIYAEQERMAMERnRELERIRLEEKKRENERVRQEEIAMEISKIRELERlQLERQRKN--- 415
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEIDVASAEREIAELEA-ELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 416 -ERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQmEILRQQEED 494
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-AALGDAVER 765
|
....*....
gi 86562857 495 QKKKKLEKD 503
Cdd:COG4913 766 ELRENLEER 774
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
304-460 |
6.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 304 HQKTVSERQqqEKFEKMEQER--LRQEKEEKARELERRRKLEESETARQAELDRQATIyaeQERMAMERNR-ELERIRLE 380
Cdd:PRK02224 466 HVETIEEDR--ERVEELEAELedLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL---EELIAERRETiEEKRERAE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 381 EKkreneRVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQL 460
Cdd:PRK02224 541 EL-----RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKR 615
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
330-496 |
6.72e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.87 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 330 EEKARELERRRKLEESETARQaeldrqatiyaeQERMAMERNREleRIRLEEKKRENERVRQEEiameiskireleRLQL 409
Cdd:PRK10811 583 GEETKPQEQPAPKAEAKPERQ------------QDRRKPRQNNR--RDRNERRDTRDNRTRREG------------RENR 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 410 ERQRKNERVRQELEAARKYKLQEEE------RQRKIQQQKVEmEQIRQQEEARQEQLRVLEEERARELERVRQEELERQH 483
Cdd:PRK10811 637 EENRRNRRQAQQQTAETRESQQAEVtekartQDEQQQAPRRE-RQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQ 715
|
170
....*....|...
gi 86562857 484 QMEILRQQEEDQK 496
Cdd:PRK10811 716 VQPRRKQRQLNQK 728
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
303-621 |
6.77e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKAR-ELERRRKLEESETARQAEldrqatiYAEQERMAMERNRELERIRLEE 381
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKRQAEEEAREAKaEAEQRAAELAAEAAKKLA-------EAEKAAAEAEKKAAAEKAKAAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 382 KKRENERVRQEEIAMEISKIRELERlQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLR 461
Cdd:COG3064 103 EAEAAAAAEKAAAAAEKEKAEEAKR-KAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 462 VLEEERARELERVRQEELERQHQMEILRqQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKML 541
Cdd:COG3064 182 LVAAAAAAVEAADTAAAAAAALAAAAAA-AAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 542 EKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG3064 261 GAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAA 340
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
301-617 |
7.18e-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: 43.47 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 301 IVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELER-RRKLEESEtarqaelDRQATIYAEQERMAMERNREL-ERIR 378
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnNKKIKELE-------KQLNQLKSEISDLNNQKEQDWnKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 379 LEEKKRENE-RVRQEEIAMEISKIRELERL--QLERQRKNERvrqeleaarkykLQEEERQRKIQQQKVEMEQIRQQEEA 455
Cdd:TIGR04523 314 SELKNQEKKlEEIQNQISQNNKIISQLNEQisQLKKELTNSE------------SENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 456 RQEQLrvleeerarelervrqEELERqhQMEILRQQEEDQKKKKLEKDREQREQQEaeelNRMIIEKEMKENKQKMIEEK 535
Cdd:TIGR04523 382 YKQEI----------------KNLES--QINDLESKIQNQEKLNQQKDEQIKKLQQ----EKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 536 NKRKMLEKEMEDRQNAIyeeEERRIAEEERRKQIEIEER--RRIQQQIMIATEErsrLDAMEREREML-RQIKESEKQRK 612
Cdd:TIGR04523 440 SEIKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKE---LKSKEKELKKLnEEKKELEEKVK 513
|
....*
gi 86562857 613 ELERQ 617
Cdd:TIGR04523 514 DLTKK 518
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
328-601 |
7.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 328 EKEEKARELERRR-KLEESETARQAELDRqATIYAEQERmamERNRELERIRLEEKKRENERVRQEEiameiskirelER 406
Cdd:PRK02224 472 EDRERVEELEAELeDLEEEVEEVEERLER-AEDLVEAED---RIERLEERREDLEELIAERRETIEE-----------KR 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 407 LQLERQRKN-ERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRvlEEERARELERVRQEELERQHQM 485
Cdd:PRK02224 537 ERAEELRERaAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--RIRTLLAAIADAEDEIERLREK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 486 EILRQQEEDQKKKKLekdreqreqqeaeelnrmiieKEMKENKQKMiEEKNKRKMLEKEMEDRQNAiyeeeeRRIAEEER 565
Cdd:PRK02224 615 REALAELNDERRERL---------------------AEKRERKREL-EAEFDEARIEEAREDKERA------EEYLEQVE 666
|
250 260 270
....*....|....*....|....*....|....*..
gi 86562857 566 RKQIEIEERR-RIQQQIMIATEERSRLDAMEREREML 601
Cdd:PRK02224 667 EKLDELREERdDLQAEIGAVENELEELEELRERREAL 703
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
333-622 |
8.46e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 333 ARELERRRKLEESETARQAELDRQAtiyAEQERMAmernreLERIRLEEKKRENERVRQeeiAMEISKIReLERLQLERQ 412
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQA---AAEEQLV------QANGELEKASREETFART---ALKNARLD-LRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 413 RKNERVRQELEAARKYKlqEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQE---ELERQHQMEILR 489
Cdd:pfam12128 664 SEKDKKNKALAERKDSA--NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAldaQLALLKAAIAAR 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 490 QQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQI 569
Cdd:pfam12128 742 RSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 570 EIEERRriQQQIMIATEERSRLDAMEREREMLR--QIKESEKQRKELERQELLAT 622
Cdd:pfam12128 822 AISELQ--QQLARLIADTKLRRAKLEMERKASEkqQVRLSENLRGLRCEMSKLAT 874
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
282-460 |
1.01e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 282 VRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEkfekMEQERLRQEKEEKARELERRRKLEESETARQAELD-----RQ 356
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLDKKHQA----WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKaaiaaRR 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 357 ATIYAEQERMAMERNREL-------ERIRLEEKKRENERVRQEEIAMEISKIRELERLQLER--QRKNERVRQELEAARK 427
Cdd:pfam12128 743 SGAKAELKALETWYKRDLaslgvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETwlQRRPRLATQLSNIERA 822
|
170 180 190
....*....|....*....|....*....|...
gi 86562857 428 YKLQEEERQRKIQQQKVEMEQIRQQEEARQEQL 460
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
692-744 |
1.02e-03 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 37.81 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 86562857 692 GECElkYDVDSFCAHPRSPSMYLQCAPlygrlGRWTERYCPDTLIFIVSIGRC 744
Cdd:smart00494 1 NECP--GRGDGLYPHPTDCSKYYQCSN-----GRPIVGSCPAGLVFNPATQTC 46
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
330-384 |
1.14e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.94 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 330 EEKARELERRRKlEESETARQAELDRQatiyAEQERMAMERNRELERIRLEEKKR 384
Cdd:PLN02316 252 EEKRRELEKLAK-EEAERERQAEEQRR----REEEKAAMEADRAQAKAEVEKRRE 301
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
318-502 |
1.15e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 318 EKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQatiYAEQERmAMERNRELERIRLEEKKRENERVRQEEiame 397
Cdd:COG3096 482 CKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQ---LAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAE---- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 398 iskirELERLQLERQRKNERVRQELEAARkyklqeeERQRKIQQQKVEMEQIRQQEEARQ----------EQLRVLEEER 467
Cdd:COG3096 554 -----ELEELLAELEAQLEELEEQAAEAV-------EQRSELRQQLEQLRARIKELAARApawlaaqdalERLREQSGEA 621
|
170 180 190
....*....|....*....|....*....|....*...
gi 86562857 468 ---ARELERVRQEELERQHQMEILRQQEEdQKKKKLEK 502
Cdd:COG3096 622 ladSQEVTAAMQQLLEREREATVERDELA-ARKQALES 658
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
374-552 |
1.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 374 LERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEaarkyKLQEEERQRKIQQQKVEMEQIRQQE 453
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 454 EARQEQLRvleeerareleRVRQEELERQHQMEILRQQEEdQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIE 533
Cdd:COG4717 145 PERLEELE-----------ERLEELRELEEELEELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170
....*....|....*....
gi 86562857 534 EKNKRkmLEKEMEDRQNAI 552
Cdd:COG4717 213 EELEE--AQEELEELEEEL 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
410-618 |
1.22e-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: 42.44 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 410 ERQRKNERVRQELEAARKyKLQEEERQRKIQQQkvEMEQIRQQEEARQEQLRVLEEERARElervrQEELER-QHQMEIL 488
Cdd:COG4942 24 EAEAELEQLQQEIAELEK-ELAALKKEEKALLK--QLAALERRIAALARRIRALEQELAAL-----EAELAElEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 489 RQQEEDQKKKKLEKDREQREQQEAEELNRMIiekemkeNKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQ 568
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLL-------SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 569 IEiEERRRIQQQIMIATEERSRLDAMEREREML-----RQIKESEKQRKELERQE 618
Cdd:COG4942 169 LE-AERAELEALLAELEEERAALEALKAERQKLlarleKELAELAAELAELQQEA 222
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
309-460 |
1.27e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 309 SERQQQEKFEKMEQ-----ERLRQEKEEKARELERRRKleesetarqaeldrqaTIYAEQERMAmernreleRIRLEEKK 383
Cdd:PRK00409 528 LERELEQKAEEAEAllkeaEKLKEELEEKKEKLQEEED----------------KLLEEAEKEA--------QQAIKEAK 583
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 384 RENERVrqeeiameISKIRELERLQLERQRknervRQELEAARK-YKLQEEERQRKIQQQKVEMEQIRQQEEARQEQL 460
Cdd:PRK00409 584 KEADEI--------IKELRQLQKGGYASVK-----AHELIEARKrLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
323-461 |
1.29e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.02 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKEEKARELerrrkLEESEtaRQAE-LDRQATIYAEQE--RMAMERNRELERIRLEEKKRENeRVRQEEIAMEiS 399
Cdd:pfam12072 26 EAKIGSAEELAKRI-----IEEAK--KEAEtKKKEALLEAKEEihKLRAEAERELKERRNELQRQER-RLLQKEETLD-R 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 400 KIRELErlqlERQRKNERVRQELEAARKY-KLQEEERQRKIQQQKVEMEQIR--QQEEARQEQLR 461
Cdd:pfam12072 97 KDESLE----KKEESLEKKEKELEAQQQQlEEKEEELEELIEEQRQELERISglTSEEAKEILLD 157
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-461 |
1.37e-03 |
|
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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 287 QTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELER-RRKLEESETA-RQAELDRQATIyaeqe 364
Cdd:COG4913 269 ERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlREELDELEAQiRGNGGDRLEQL----- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 365 rmamerNRELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRknERVRQELEAARKYKLQEEERQRKIQQQKV 444
Cdd:COG4913 344 ------EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR--AEAAALLEALEEELEALEEALAEAEAALR 415
|
170
....*....|....*..
gi 86562857 445 EMEQIRQQEEARQEQLR 461
Cdd:COG4913 416 DLRRELRELEAEIASLE 432
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
321-501 |
1.66e-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: 41.06 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 321 EQERLR--QEKEEKARELERRRK-LEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAME 397
Cdd:COG1579 5 DLRALLdlQELDSELDRLEHRLKeLPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 398 ISKIRELERLQlerqrknervrQELEAARKYKLQEEERQR----KIQQQKVEMEQIRQQEEARQEQLRVleeerareler 473
Cdd:COG1579 85 VRNNKEYEALQ-----------KEIESLKRRISDLEDEILelmeRIEELEEELAELEAELAELEAELEE----------- 142
|
170 180
....*....|....*....|....*...
gi 86562857 474 vrqEELERQHQMEILRQQEEDQKKKKLE 501
Cdd:COG1579 143 ---KKAELDEELAELEAELEELEAEREE 167
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
310-657 |
1.76e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKMEQERLRQEKEEKARELER---RRKLEESETA--RQAELDRQATIYAEQERM--AMERNREL----ERI- 377
Cdd:COG5022 816 LACIIKLQKTIKREKKLRETEEVEFSLKAevlIQKFGRSLKAkkRFSLLKKETIYLQSAQRVelAERQLQELkidvKSIs 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 -----------RLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEErqRKIQQQKVEM 446
Cdd:COG5022 896 slklvnlelesEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKLKETSEEY 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 447 EQIRQQEEARQEQLRvleeerarelerVRQEELERQHQM--EILRQQEEDQKKKKLEKDREQREQQEAeelNRMIIEKEM 524
Cdd:COG5022 974 EDLLKKSTILVREGN------------KANSELKNFKKElaELSKQYGALQESTKQLKELPVEVAELQ---SASKIISSE 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 525 KENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEER-----RRIQQQIMIATEERSRLDAMERERE 599
Cdd:COG5022 1039 STELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLEStenllKTINVKDLEVTNRNLVKPANVLQFI 1118
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86562857 600 MLRQIKESEKQRKELERQELLATTPI---TTIKPIYRPDISEYRPPDVE-SHMIRFTTQSPE 657
Cdd:COG5022 1119 VAQMIKLNLLQEISKFLSQLVNTLEPvfqKLSVLQLELDGLFWEANLEAlPSPPPFAALSEK 1180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
301-497 |
1.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 301 IVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELErrrKLEESETARQAELDR-QATIYAEQERMAmERNRELERiRL 379
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKlQAEIAEAEAEIE-ERREELGE-RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 380 EEKKRENERVRQEEIAME-------ISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQ 452
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 86562857 453 EEARQEQLRVleeeraRELERVRQEELERQHQMEILRQQEEDQKK 497
Cdd:COG3883 173 LEAQQAEQEA------LLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
402-628 |
1.93e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 402 RELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELER 481
Cdd:COG5278 107 ARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 482 QHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIA 561
Cdd:COG5278 187 ALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAA 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86562857 562 EEERRKQIEIEERRRIQQQIMIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLATTPITTI 628
Cdd:COG5278 267 LLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALAL 333
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
337-461 |
1.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 337 ERRRKLEESETARQAELDRQATIYAEQERmAMERNRELERIRLEEKKREnervrqeeiaMEISKIRelERLQLER----- 411
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYR-LVEMARELAELNEAESDLE----------QDYQAAS--DHLNLVQtalrq 346
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 86562857 412 QRKNERVRQELEAArKYKLQEEERQRKIQQQKVEMEQiRQQEEARQEQLR 461
Cdd:PRK04863 347 QEKIERYQADLEEL-EERLEEQNEVVEEADEQQEENE-ARAEAAEEEVDE 394
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
311-445 |
1.97e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELErirLEEKKRENERVR 390
Cdd:PRK12705 58 KELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELE---ELEKQLDNELYR 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 391 QEEIAMEISKIRELERLQLE-RQRKNERVRQELEAARkykLQEEERQRKIQQQKVE 445
Cdd:PRK12705 135 VAGLTPEQARKLLLKLLDAElEEEKAQRVKKIEEEAD---LEAERKAQNILAQAMQ 187
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
303-425 |
2.03e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.84 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSERQQQEKFEKMEQERLRQEKEEKARELE-RRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEE 381
Cdd:pfam13904 65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEwLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 86562857 382 KKRENERVRQEEiameiSKIRELERLQLERQRKNERVRQELEAA 425
Cdd:pfam13904 145 QEWERKKLEQQQ-----RKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
356-461 |
2.09e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 356 QATIYAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEiskirelERLQLERQRKNERVRQ---ELEAARKYKLQE 432
Cdd:pfam02841 190 EAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEE-------QMMEAQERSYQEHVKQlieKMEAEREQLLAE 262
|
90 100 110
....*....|....*....|....*....|..
gi 86562857 433 EER---QRKIQQQKVEMEQIRQQEEARQEQLR 461
Cdd:pfam02841 263 QERmleHKLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
315-390 |
2.25e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.59 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 315 EKFEKMEQERLRQEKEEKARELERRRKLEE-----SETARQAeldRQAtiyaeQERMAMernreLERIRLEEKKRENERV 389
Cdd:COG0488 235 SAYLEQRAERLEQEAAAYAKQQKKIAKEEEfirrfRAKARKA---KQA-----QSRIKA-----LEKLEREEPPRRDKTV 301
|
.
gi 86562857 390 R 390
Cdd:COG0488 302 E 302
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
310-434 |
2.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFE--KMEQERLRQEKEEKARELERRRKLEESetarqaELDRQATIYAEQERMAMERNRELERIR--LEEKKRE 385
Cdd:PRK12704 59 LLEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEE------NLDRKLELLEKREEELEKKEKELEQKQqeLEKKEEE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 386 NERVRQEEIAmeiskirELER---LQLE--RQRKNERVRQEL--EAARKYKLQEEE 434
Cdd:PRK12704 133 LEELIEEQLQ-------ELERisgLTAEeaKEILLEKVEEEArhEAAVLIKEIEEE 181
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
337-458 |
2.58e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 337 ERRRKLEESETARQAELDRQATIYAEQERMAmERNRElerirLEEKKRenervRQEEIAMEISKIRE-LERLQ--LERQR 413
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLV-EMARE-----LEELSA-----RESDLEQDYQAASDhLNLVQtaLRQQE 347
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 86562857 414 KNERVRQELEAArKYKLQEEERQRKIQQQKVEMEQIRqQEEARQE 458
Cdd:COG3096 348 KIERYQEDLEEL-TERLEEQEEVVEEAAEQLAEAEAR-LEAAEEE 390
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
419-549 |
2.63e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 419 RQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQlrvleeerarelervrqeelERQHQmEILRQQEE--DQK 496
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQ--------------------ERSYE-EHLRQLKEkmEEE 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 86562857 497 KKKLEKDreqreqqeaeelNRMIIEKEMKENKQKMIEE-KNKRKMLEKEMEDRQ 549
Cdd:cd16269 250 RENLLKE------------QERALESKLKEQEALLEEGfKEQAELLQEEIRSLK 291
|
|
| PstA |
COG4985 |
ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and ... |
336-412 |
2.93e-03 |
|
ABC-type phosphate transport system, auxiliary component PstA [Inorganic ion transport and metabolism];
Pssm-ID: 444009 [Multi-domain] Cd Length: 545 Bit Score: 41.44 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 336 LERRRKLEESETAR---QAELDRQATIYAEQERMamER------NRELERIRLEEKKRENERVRQEEIAMEIskirELER 406
Cdd:COG4985 144 KEDGQVVAEGDAAWeelQQRLERALELRDQIDDI--EKgdigaiNYQLERLRLKERRLELDGQLDDEAQADI----EAER 217
|
....*.
gi 86562857 407 LQLERQ 412
Cdd:COG4985 218 AELEAE 223
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
310-451 |
2.97e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.46 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 310 ERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKREnerv 389
Cdd:pfam13904 67 QRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKE---- 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86562857 390 rqeeiameisKIRELERLQLERQrknERVRQELEAARKYKLQEEERQRKIQQQKVE--MEQIRQ 451
Cdd:pfam13904 143 ----------VLQEWERKKLEQQ---QRKREEEQREQLKKEEEEQERKQLAEKAWQkwMKNVKN 193
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
323-616 |
3.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 323 ERLRQEKEEKARELERRRKLEESETARQAELDRQATIYaeqeRMAMERNRELERIRLEEKKRENERV---------RQEE 393
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGLTPEKLekeleelekAKEE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 394 IAMEISKIR-ELERLQLERQRKNERVrQELEAAR------KYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLR-VLEE 465
Cdd:PRK03918 403 IEEEISKITaRIGELKKEIKELKKAI-EELKKAKgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERkLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 466 ERARELERVRQEELERQHQM-EILRQQEEDQKK---KKLEKDRE--------------------------QREQQEAEEL 515
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELaEQLKELEEKLKKynlEELEKKAEeyeklkekliklkgeikslkkeleklEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 516 NRMI--IEKEMKENKQKMIEEKNKRkmlEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRriqqqimIATEERSRLDA 593
Cdd:PRK03918 562 EKKLdeLEEELAELLKELEELGFES---VEELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEEELDKA 631
|
330 340
....*....|....*....|...
gi 86562857 594 MEREREMLRQIKESEKQRKELER 616
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEK 654
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
303-450 |
3.25e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 303 QHQKTVSE--RQQQEKFEKMEQERLRQEKEEKARELERRRKleesetarqaeldrqatiyaeqermaMERNRELERIRLE 380
Cdd:cd16269 177 QSKEAEAEaiLQADQALTEKEKEIEAERAKAEAAEQERKLL--------------------------EEQQRELEQKLED 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 381 EKKRENERVRQEEIAMEiskiRELERLQLERQRKNERVRQELEAarkykLQEEERQRKIQQQKVEMEQIR 450
Cdd:cd16269 231 QERSYEEHLRQLKEKME----EERENLLKEQERALESKLKEQEA-----LLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
315-501 |
3.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 315 EKFEKMEQERLRQEKEEK--ARELERRRKLEESETARQAELDrqatiyaEQERMAMERNRELERIRLEEKKRENERVRQ- 391
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKslKKELEKLEELKKKLAELEKKLD-------ELEEELAELLKELEELGFESVEELEERLKEl 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 392 EEIAMEISKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERAREL 471
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAG 677
|
170 180 190
....*....|....*....|....*....|....*
gi 86562857 472 ERVRQEELERQHQ-----MEILRQQEEDQKKKKLE 501
Cdd:PRK03918 678 LRAELEELEKRREeikktLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-458 |
3.41e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 271 EELTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQ 350
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 351 AELDRQATIYAEQERMAMERNRELERIRLEEKKRENE-RVRQEEIAMEISKIreLERLqLERQRKNERVRQELEAARKYK 429
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNL--QERL-SEEYSLTLEEAEALENKIEDD 966
|
170 180 190
....*....|....*....|....*....|....*...
gi 86562857 430 LQE-EERQRKIQQQKVE--------MEQIRQQEEARQE 458
Cdd:TIGR02168 967 EEEaRRRLKRLENKIKElgpvnlaaIEEYEELKERYDF 1004
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
319-451 |
3.79e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 319 KMEQERLRQEKEEKARELErrrklEESETARQAELDRQATIyaeqERMAMERNR-ELERIRLEEKKRENERVRQEEIAME 397
Cdd:pfam20492 1 REEAEREKQELEERLKQYE-----EETKKAQEELEESEETA----EELEEERRQaEEEAERLEQKRQEAEEEKERLEESA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 86562857 398 ISKIRELERLQLERQRKNERVRQELEAARKyklQEEERQRkiQQQKVEMEQIRQ 451
Cdd:pfam20492 72 EMEAEEKEQLEAELAEAQEEIARLEEEVER---KEEEARR--LQEELEEAREEE 120
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
371-502 |
4.04e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 371 NRELERIRLEEKKRENERVRQEeiameiskireleRLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEME--- 447
Cdd:pfam09731 300 SKKLAELKKREEKHIERALEKQ-------------KEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEekl 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 448 --QIRQQEEARQEQLRvleeerareLERVRQE-ELERQHQMEILRQ--QEEDQKKKKLEK 502
Cdd:pfam09731 367 rtELERQAEAHEEHLK---------DVLVEQEiELQREFLQDIKEKveEERAGRLLKLNE 417
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
306-411 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 306 KTVSERQQQEKFEKMEQ-----ERLR----------QEKEEKARELERRRKLEESETARQAELDRQATIyaeqermameR 370
Cdd:COG2433 401 KEHEERELTEEEEEIRRleeqvERLEaeveeleaelEEKDERIERLERELSEARSEERREIRKDREISR----------L 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 86562857 371 NRELERIrleEKKRENERVRQEEIAMEISKIRELERLQLER 411
Cdd:COG2433 471 DREIERL---ERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
318-462 |
4.19e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 318 EKMEQErLRQEKEEKARELERRRKLEesetARQAELDRQATIYAEQERMAMERNRE-LERIRLEEKKR-ENERVRQEEia 395
Cdd:COG1842 33 RDMEED-LVEARQALAQVIANQKRLE----RQLEELEAEAEKWEEKARLALEKGREdLAREALERKAElEAQAEALEA-- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86562857 396 meiskirelerlQLERQRknervrqelEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRV 462
Cdd:COG1842 106 ------------QLAQLE---------EQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
412-551 |
4.48e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 412 QRKNERVRQELEAARKyklqEEERQRKIQQQKvemEQIRQQEEARQEQLRVleeerarelervrqEELERQHQMEILRQQ 491
Cdd:PRK09510 62 EQYNRQQQQQKSAKRA----EEQRKKKEQQQA---EELQQKQAAEQERLKQ--------------LEKERLAAQEQKKQA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86562857 492 EEDQKKKKLEKDREQREQQEAEELNRMIIEKEMK---ENKQKMIEEKNKRKMLEKEMEDRQNA 551
Cdd:PRK09510 121 EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKraaAAAKKAAAEAKKKAEAEAAKKAAAEA 183
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
292-617 |
4.74e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 292 NEFLNQLLHIVQHQKTVSERQQ-----QEKFEkmEQERLRQEKEEKARELERRRKLEESETAR--------QAELDRQAT 358
Cdd:COG3096 333 SDHLNLVQTALRQQEKIERYQEdleelTERLE--EQEEVVEEAAEQLAEAEARLEAAEEEVDSlksqladyQQALDVQQT 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 359 --IYAEQERMAMERNRELERI----------RLEEKKRE----NERVRQEEIAMEISKI--RELER-LQL--------ER 411
Cdd:COG3096 411 raIQYQQAVQALEKARALCGLpdltpenaedYLAAFRAKeqqaTEEVLELEQKLSVADAarRQFEKaYELvckiagevER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 412 QRKNERVRQELEAARKYKLQEEeRQRKIQQQKVEMEQ-IRQQEEAR--QEQLrvleeERARELERVRQEELERQH-QMEI 487
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQ-RLQQLRAQLAELEQrLRQQQNAErlLEEF-----CQRIGQQLDAAEELEELLaELEA 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 488 LRQQEEDQKKKKLEKdreqreqqeaeelnRMIIEKEMKENKQKMieeknkrkmleKEMEDRQNAiyeeeerriaeeerrk 567
Cdd:COG3096 565 QLEELEEQAAEAVEQ--------------RSELRQQLEQLRARI-----------KELAARAPA---------------- 603
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 86562857 568 QIEIEER-RRIQQQIMIATEERSRLDA-----MEREREMLRQIKESEKQRKELERQ 617
Cdd:COG3096 604 WLAAQDAlERLREQSGEALADSQEVTAamqqlLEREREATVERDELAARKQALESQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-462 |
5.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 330 EEKARELERRRK----LEESETARQAELDRQATIYAEQERMAMERNRelERIRLEEKKRENERVRQEEIAmeiskiRELE 405
Cdd:COG4913 241 HEALEDAREQIEllepIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLE------AELE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 86562857 406 RLQLERQRKNERVRQELEAARKYKLQEEER-QRKIQQQKVEMEQIRQQEEARQEQLRV 462
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAA 370
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
173-393 |
5.64e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 40.88 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 173 TTPKIVIFASKKNMNNTNRsGESRTQLIRNRNRE---RGNAPAFTRPGRVRTTTPMSVTHATrfvpgiqhkvtvapkEVQ 249
Cdd:PTZ00266 332 PGLQLAAMEKAKHAEAANY-GISPNTLINQRNEEqhgRRSSSCASRQSANNVTNITSITSVT---------------SVA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 250 GMPHTLAPYEKMDRRPDSFGVEELTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKTVSERQQQEKFEKMEQERLRQEK 329
Cdd:PTZ00266 396 SVASVASVPSKDDRKYPQDGATHCHAVNGHYGGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREERERLERER 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 330 EEK-ARELERRRKLEESETARQaELDRQATiyaeqERMAMERNRELERIRLEEKKRENERVRQEE 393
Cdd:PTZ00266 476 MERiERERLERERLERERLERD-RLERDRL-----DRLERERVDRLERDRLEKARRNSYFLKGME 534
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
340-443 |
5.81e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 340 RKLEESETARQAELDRQATIYAEQERMaMERNRELERiRLEEKKRENervrQEEIAMEISKI-RELERLQLERQRKNERV 418
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELL-REKQKEEEQ-MMEAQERSY----QEHVKQLIEKMeAEREQLLAEQERMLEHK 270
|
90 100
....*....|....*....|....*..
gi 86562857 419 RQELEAARKYKLQEE--ERQRKIQQQK 443
Cdd:pfam02841 271 LQEQEELLKEGFKTEaeSLQKEIQDLK 297
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
367-618 |
6.31e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 367 AMERNRELERIRLEEKKRENERVRQEEIAmEISKIRElerlqlERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEM 446
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNE-ELKELAE------KRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 447 EQIRQQEEARQEQLRVLEEERARELERVRQ--------EELERQHQMEILRQQEEDQ---KKKKLEKDREQREQQEAeel 515
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidklrkeiERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 516 nrmiIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQI--EIEE-RRRIQQQIMIATEERSRLD 592
Cdd:COG1340 158 ----KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELrkEADElHKEIVEAQEKADELHEEII 233
|
250 260
....*....|....*....|....*..
gi 86562857 593 AMERE-REMLRQIKESEKQRKELERQE 618
Cdd:COG1340 234 ELQKElRELRKELKKLRKKQRALKREK 260
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
330-461 |
6.49e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 330 EEKARELERRRKLEESETARQAELDRQATIYAEQERMamernRELERiRLEEKKRENERVRQEeiameiskIRELERlql 409
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEI-----RRLEE-QVERLEAEVEELEAE--------LEEKDE--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 86562857 410 erqrKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIR---QQEEARQEQLR 461
Cdd:COG2433 442 ----RIERLERELSEARSEERREIRKDREISRLDREIERLErelEEERERIEELK 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-621 |
6.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 295 LNQLLHIVQHQKTVSERQQ--------QEKFEKMEQERL-RQEKEEKARELERRrkLEESETARQAELDRQATIYAEQER 365
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEAleaelaelPERLEELEERLEeLRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 366 MAMErnrELERIRLEEKKRENERVRQEEIAMEISKIRELERLQLERQRKNERVRQELEAAR------------------- 426
Cdd:COG4717 196 DLAE---ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsli 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 427 ---------------KYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLEEERARELERVRQEELERQHQMEILRQQ 491
Cdd:COG4717 273 ltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 492 EEDQKKKKLEKDREQREQQEAEELNRMIIEKEmkENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEI 571
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDE--EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 86562857 572 EERrriqqqimIATEERSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG4717 431 EEE--------LEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
372-442 |
6.91e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 6.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86562857 372 RELERIRLEEKKRENERVRQEEIameiskirELERlQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQ 442
Cdd:PLN02316 244 HSFEDFLLEEKRRELEKLAKEEA--------ERER-QAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQN 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-621 |
7.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 429 KLQEEERQ-RKIQQQKVEM--EQIRQQEEARQEQlrvleEERARELERVRQEELERQHQMEILRQQEE--DQKKKKLEKD 503
Cdd:COG4717 50 RLEKEADElFKPQGRKPELnlKELKELEEELKEA-----EEKEEEYAELQEELEELEEELEELEAELEelREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 504 REQREQQEAEELNRMIIE------KEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERRKQIEIEERRRI 577
Cdd:COG4717 125 LQLLPLYQELEALEAELAelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 86562857 578 QQQIMIATEE----RSRLDAMEREREMLRQIKESEKQRKELERQELLA 621
Cdd:COG4717 205 QQRLAELEEEleeaQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
362-502 |
8.21e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 38.92 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 362 EQERMAMERNRELERIRLEEKKRENERVRQEEIAMEiSKIRELERLQLERQRKNERvRQELEAARKYKLQEEERQRKIQQ 441
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRK-ARQQTKKREESHKQKAAES-ASKSLAKPERKVSQEEAKEVLQE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86562857 442 QkvEMEQIRQQEEARQEqlrvleeerarelervrqeelERQHQMEilRQQEEDQKKKKLEK 502
Cdd:pfam13904 147 W--ERKKLEQQQRKREE---------------------EQREQLK--KEEEEQERKQLAEK 182
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
305-461 |
8.45e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 38.62 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 305 QKTVSERQQQEKFEKMEQERLRQEKEEKARELERRRKLEESETARQAELDRQatiyAEQERMAMERNRELERIRL----- 379
Cdd:pfam14662 28 KATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSL----EEARRSLLAQNKQLEKENQsllqe 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 380 EEKKRENERVRQEEIAMEISKIRELERLQLERQRKNErVRQELEAARKYKLQEEERQRKIQQQKVEmEQIRQQEEARQEQ 459
Cdd:pfam14662 104 IESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLH-SCEDLACNRETILIEKTTQIEELKSTVE-EYSSIEEELRAEK 181
|
..
gi 86562857 460 LR 461
Cdd:pfam14662 182 SR 183
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
378-599 |
8.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 378 RLEEKKRENERVRQEeiameiskIRELERLQLERQRKNERVRQELEAA-----------RKYKLQEEERQRKIQQQKVEM 446
Cdd:COG4942 21 AAAEAEAELEQLQQE--------IAELEKELAALKKEEKALLKQLAALerriaalarriRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 447 EQIRQQEEARQEQLR-------VLEEERARELERVRQEELERQHQMEILRQQEEDQKK--KKLEKDREQREQqeaeelNR 517
Cdd:COG4942 93 AELRAELEAQKEELAellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaEELRADLAELAA------LR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 518 MIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIyeeeerriaeeERRKQIEIEERRRIQQQIMIATEERSRLDAMERE 597
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLL-----------ARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 86562857 598 RE 599
Cdd:COG4942 236 AA 237
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-550 |
9.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 311 RQQQEKFEKMEQE--RLRQEKEEKARELER----RRKLEESETARQAELDRQATIYAEQERMAMERNRELERIRLEEKKR 384
Cdd:COG4372 90 QAAQAELAQAQEEleSLQEEAEELQEELEElqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 385 ENERVRQEEIAmeisKIRELERLQLERQRKNERVRQELEAARKYKLQEEERQRKIQQQKVEMEQIRQQEEARQEQLRVLE 464
Cdd:COG4372 170 EQELQALSEAE----AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 465 EERARELERVRQEELERQHQMEILRQQEEDQKKKKLEKDREQREQQEAEELNRMIIEKEMKENKQKMIEEKNKRKMLEKE 544
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
....*.
gi 86562857 545 MEDRQN 550
Cdd:COG4372 326 KKLELA 331
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
307-410 |
9.48e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 38.44 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 307 TVSERQQQEKfeKMEQERLRQEKEEKAREL--ERRRKLEESETARQAELDRQatIYAEQERMAMERNRELERIRLEEKKR 384
Cdd:PRK02292 5 TVVEDIRDEA--RARASEIRAEADEEAEEIiaEAEADAEEILEDREAEAERE--IEQLREQELSSAKLEAKRERLNARKE 80
|
90 100 110
....*....|....*....|....*....|
gi 86562857 385 ENERVR---QEEIA-MEISKIRELERLQLE 410
Cdd:PRK02292 81 VLEDVRnqvEDEIAsLDGDKREELTKSLLD 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-618 |
9.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 327 QEKEEKARELERRRKLEESETARQAELDRQATIyAEQERMAMERNRELERIRLEEKKRENERVRQEEIAMEiSKIRELER 406
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK-GEIKSLKK 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 407 lQLERQRKNERVRQELEAarkyKLQEEERQRKIQQQKVEMEQIRQQEEARQEQlrvleeerarelervrqEELERQHQME 486
Cdd:PRK03918 547 -ELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERL-----------------KELEPFYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86562857 487 ILRQQEEDQKKKKLEKdreqreqqeaeelnRMIIEKEMKENKQKMIEEKNKRKMLEKEMEDRQNAIYEEEERRIAEEERR 566
Cdd:PRK03918 605 LELKDAEKELEREEKE--------------LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE 670
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 86562857 567 KQIEIEERRRIQQQImiateERSRLDAMEREREMLRQIKESEKQRKELERQE 618
Cdd:PRK03918 671 LSRELAGLRAELEEL-----EKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
|