|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-550 |
6.52e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 339 RKQSLEPDKADHIRAAVyqEWLEKKNVYLHEMHRIKRiESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKK 418
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKA--EEDKKKADELKKAAAAKK-KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 419 RLEEKNKKKTEEENAVRKGEALQAFEKWKeKKLEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKK-EAL 497
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKaDEA 1539
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564336877 498 LKQKEKEKINERRK-EELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKR 550
Cdd:PTZ00121 1540 KKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
438-551 |
1.59e-05 |
|
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: 46.24 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 438 EALQAFEKWKEKKLEYLKEKTRREKEseraKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKIN----ERRKEE 513
Cdd:pfam13904 52 QPLEAYENWLAAKQRQRQKELQAQKE----EREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKqkaaESASKS 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 564336877 514 LKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRH 551
Cdd:pfam13904 128 LAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQRE 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-557 |
2.78e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 352 RAAVYQEWLEKKNVYLHEMhRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEE 431
Cdd:COG1196 211 KAERYRELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 432 NAVRKGEALQAfekwkEKKLEYLKEKtRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRK 511
Cdd:COG1196 290 EYELLAELARL-----EQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564336877 512 EELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRHSFLESE 557
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
374-542 |
2.28e-03 |
|
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: 40.60 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 374 KRIESENLRIQNEQKKAAKREEALASfEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAvRKGEALQAFEKWKEKKLEY 453
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA-KQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 454 LKEKTRREK----ESERAKKQKEE-EAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRKEELKRAEKKDKDKQAIS 528
Cdd:TIGR02794 124 AKAKQAAEAkakaEAEAERKAKEEaAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170
....*....|....
gi 564336877 529 EYEKWLEKKERQER 542
Cdd:TIGR02794 204 KAAAEAAAKAEAEA 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-550 |
6.52e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 339 RKQSLEPDKADHIRAAVyqEWLEKKNVYLHEMHRIKRiESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKK 418
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKA--EEDKKKADELKKAAAAKK-KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 419 RLEEKNKKKTEEENAVRKGEALQAFEKWKeKKLEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKK-EAL 497
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKaDEA 1539
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564336877 498 LKQKEKEKINERRK-EELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKR 550
Cdd:PTZ00121 1540 KKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
438-551 |
1.59e-05 |
|
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: 46.24 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 438 EALQAFEKWKEKKLEYLKEKTRREKEseraKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKIN----ERRKEE 513
Cdd:pfam13904 52 QPLEAYENWLAAKQRQRQKELQAQKE----EREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKqkaaESASKS 127
|
90 100 110
....*....|....*....|....*....|....*...
gi 564336877 514 LKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRH 551
Cdd:pfam13904 128 LAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQRE 165
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
335-548 |
1.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 335 QKPPRKQSLEPDKADHIRAAVYQEWLEKKNV--YLHEMHRIKRIESENLRIQNEQKKAA----------KREEALASFEA 402
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIeeVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkaeeekKKVEQLKKKEA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 403 WKAMKEKEAKKIAAKKRLEEKNKKKTEEENAvRKGEALQAFEKWKEKKLEYLKEKTRREKESERAKKQKEEEA------- 475
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkaeelk 1722
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564336877 476 -VAEKKKDSVTAFERWSEK-----KEALLKQKEKEKINERRKEELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQK 548
Cdd:PTZ00121 1723 kAEEENKIKAEEAKKEAEEdkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
361-557 |
3.94e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 361 EKKNVYLHEMHRIKRIES---ENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKrleeKNKKKTEEENAVRKG 437
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 438 EALQAFEKWKEKKLEYLKEKTRREK-ESERAKKQKEEEavaEKKKDSVTAFERWSEKKEALLKQKEKEKineRRKEELKR 516
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKkKAEEAKKAEEDE---KKAAEALKKEAEEAKKAEELKKKEAEEK---KKAEELKK 1723
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564336877 517 AEKKDKDKQAISEYEKWLEKKERQE-RIDRKQKKRHSFLESE 557
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIAHLKKE 1765
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
485-573 |
7.39e-05 |
|
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: 44.31 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 485 TAFERW-SEKKEallkQKEKEKINERRKEELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRHSFLESETHPPWS 563
Cdd:pfam13904 55 EAYENWlAAKQR----QRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAK 130
|
90
....*....|
gi 564336877 564 PPSRTAPSKV 573
Cdd:pfam13904 131 PERKVSQEEA 140
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
440-519 |
7.88e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 440 LQAFEKWKEKKLEYLKEKTRREKE---SERAKKQKEE-----EAVAEKKKDSVTAFERWSEKKEALLKQKEKEkINERRK 511
Cdd:PRK12704 60 LEAKEEIHKLRNEFEKELRERRNElqkLEKRLLQKEEnldrkLELLEKREEELEKKEKELEQKQQELEKKEEE-LEELIE 138
|
....*...
gi 564336877 512 EELKRAEK 519
Cdd:PRK12704 139 EQLQELER 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
379-550 |
2.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 379 ENLRIQNEQKKA--AKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAVRKGEALQAFEKWKEKKLEYLKE 456
Cdd:PTZ00121 1209 EEERKAEEARKAedAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 457 KtrreKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRKEELKRAE-KKDKDKQAISEYEKWLE 535
Cdd:PTZ00121 1289 K----KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaAKAEAEAAADEAEAAEE 1364
|
170
....*....|....*
gi 564336877 536 KKERQERIDRKQKKR 550
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKK 1379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-557 |
2.78e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 352 RAAVYQEWLEKKNVYLHEMhRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEE 431
Cdd:COG1196 211 KAERYRELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 432 NAVRKGEALQAfekwkEKKLEYLKEKtRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRK 511
Cdd:COG1196 290 EYELLAELARL-----EQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564336877 512 EELKRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKKRHSFLESE 557
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
453-559 |
6.93e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 453 YLKEKTRREKESERAKKQKEEEAVAEKKkdsvtafERWSEKKEALLK-QKEKEKINERRKEELKRAEKK--DKDKQAISE 529
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLE-------AALLEAKELLLReRNQQRQEARREREELQREEERlvQKEEQLDAR 96
|
90 100 110
....*....|....*....|....*....|
gi 564336877 530 YEKWLEKKERQERIDRKQKKRHSFLESETH 559
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEK 126
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
374-546 |
7.20e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 374 KRIESENLRIQNEQKKA-AKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAVRKGEALQAFEKWKEKKLE 452
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 453 YLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAferwSEKKEALLKQKEKEKINERRKEELKRAEKKDKDKQAISEYEK 532
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
170
....*....|....
gi 564336877 533 WLEKKERQERIDRK 546
Cdd:PTZ00121 1485 ADEAKKKAEEAKKK 1498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-550 |
9.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 339 RKQSLEPDKADHIRAAVYQEWLEKKNVyLHEMHRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKK 418
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARM-AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 419 RleEKNKKKTEEENAVRKGEALQAFEKWKEKKLEYLK---EKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKE 495
Cdd:PTZ00121 1315 K--KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564336877 496 ALLKQKEKEKiNERRKEELKRAE----------KKDKDKQAISEYEKWLEKKERQERIDRKQKKR 550
Cdd:PTZ00121 1393 ADEAKKKAEE-DKKKADELKKAAaakkkadeakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
273-550 |
1.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 273 AEPAKKTNEVKTTKNKKTTNNRVSSA-SGRLMTSEFLKRSGPTKRSPSAATSSHYLGSLKVLDQKPPRKQSLEPDKADHI 351
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 352 RAavyQEWLEKKNVYLHEMHRIKRIESENLRIQNEQKKA---AKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKT 428
Cdd:PTZ00121 1372 KK---EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 429 EEENAVRKGEALQAFEKWKE-KKLEYLKEKTRREKESERAKKQKEEeavAEKKKDSVTAFERwSEKKEALLKQ-KEKEKI 506
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAE-AKKKADEAKKaEEAKKA 1524
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 564336877 507 NERRK-EELKRAE--KKDKDKQAISEYEKWLEKKERQERIDRKQKKR 550
Cdd:PTZ00121 1525 DEAKKaEEAKKADeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
374-542 |
2.28e-03 |
|
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: 40.60 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 374 KRIESENLRIQNEQKKAAKREEALASfEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAvRKGEALQAFEKWKEKKLEY 453
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA-KQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 454 LKEKTRREK----ESERAKKQKEE-EAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRKEELKRAEKKDKDKQAIS 528
Cdd:TIGR02794 124 AKAKQAAEAkakaEAEAERKAKEEaAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170
....*....|....
gi 564336877 529 EYEKWLEKKERQER 542
Cdd:TIGR02794 204 KAAAEAAAKAEAEA 217
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
448-538 |
2.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 448 EKKLEYLK-EKTRREKES-----ERAKKQKEEEAVAEKKKDSVTAfeRWSEKKEALLKQKEKEKINERRKEELKRAEKKD 521
Cdd:COG0542 417 ERRLEQLEiEKEALKKEQdeasfERLAELRDELAELEEELEALKA--RWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90
....*....|....*..
gi 564336877 522 KDKQAISEYEKWLEKKE 538
Cdd:COG0542 495 AELEEELAELAPLLREE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
357-547 |
2.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 357 QEWLEKKNVYLHEMHrIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKKIAAKKRLEEKNKKKTEEENAVRK 436
Cdd:COG4717 55 ADELFKPQGRKPELN-LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 437 GEALQAFEKWKEKKLEYLKEKTRREKESERAKKQKEEEaVAEKKKDSVTAFERWSEKKEALLKQ--KEKEKINERR---K 511
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAE-LAELQEELEELLEQLSLATEEELQDlaEELEELQQRLaelE 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 564336877 512 EELKRAEKKDKD-KQAISEYEKWLEKKERQERIDRKQ 547
Cdd:COG4717 213 EELEEAQEELEElEEELEQLENELEAAALEERLKEAR 249
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
492-542 |
2.79e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 40.24 E-value: 2.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 564336877 492 EKKEALLKQKEKEKINERRKEELKRAEKKDKDKQAISEYEKWLEK-KERQER 542
Cdd:pfam07946 271 EKIKKAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKeRKKEQR 322
|
|
| rpsP |
PRK14521 |
30S ribosomal protein S16; Provisional |
434-529 |
4.32e-03 |
|
30S ribosomal protein S16; Provisional
Pssm-ID: 237744 [Multi-domain] Cd Length: 186 Bit Score: 38.60 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 434 VRKG-----EALQAFEKWKEKK---LEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTaferwsEKKEALLKQKEKEK 505
Cdd:PRK14521 89 VAKGafteaQAEAKFEAWKEEKegkVNAKKDKLSKAKKAAKKAALEAEKKVNEARAEAVA------EKKAAEAAAVAAEE 162
|
90 100
....*....|....*....|....
gi 564336877 506 INERRKEELKRAEKKDKDKQAISE 529
Cdd:PRK14521 163 AAAAEEEEAEEAPAEEAPAEESAE 186
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
447-551 |
5.13e-03 |
|
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: 39.95 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 447 KEKKLEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKInERRKEELKRAEKKDKDKQA 526
Cdd:pfam02463 208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-AQVLKENKEEEKEKKLQEE 286
|
90 100
....*....|....*....|....*
gi 564336877 527 ISEYEKWLEKKERQERIDRKQKKRH 551
Cdd:pfam02463 287 ELKLLAKEEEELKSELLKLERRKVD 311
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
448-556 |
7.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 448 EKKLEYLKEKTRR-----EKESERAKKQKEEEAVAEKKK------DSVTAFERWSEKKEALLKQKEkEKInERRKEELKR 516
Cdd:PRK12704 30 EAKIKEAEEEAKRileeaKKEAEAIKKEALLEAKEEIHKlrnefeKELRERRNELQKLEKRLLQKE-ENL-DRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564336877 517 AEKK-DKDKQAISEYEKWLEKKErqERIDRKQKKRHSFLES 556
Cdd:PRK12704 108 REEElEKKEKELEQKQQELEKKE--EELEELIEEQLQELER 146
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
435-549 |
8.05e-03 |
|
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: 38.67 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564336877 435 RKGEALQAFEKWKEKKLEYLKEKTRREKESERAKKQKEEEAVAEKKKDSVTAFERWSEKKEALLKQKEKEKINERRKEEL 514
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110
....*....|....*....|....*....|....*
gi 564336877 515 KRAEKKDKDKQAISEYEKWLEKKERQERIDRKQKK 549
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA 183
|
|
| |
