|
Name |
Accession |
Description |
Interval |
E-value |
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1168-1393 |
1.48e-15 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 81.37 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQWQ--TQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQ 1245
Cdd:NF040676 147 TEKKADEKTKQVAKVQKSVKAKEEAKTQkvAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:NF040676 227 PKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTH 1393
Cdd:NF040676 307 EIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQ 374
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1239-1386 |
4.01e-14 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 76.74 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:NF040676 232 KVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQEIAKA 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQE 1386
Cdd:NF040676 312 KEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1236-1374 |
6.81e-13 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 72.89 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEqtqiEAQGQAQKGAQERAREQ 1315
Cdd:NF040676 245 VQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEE----KAQEIAKAKEEAKAREI 320
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1316 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE 1374
Cdd:NF040676 321 AKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1444 |
8.18e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQG--QAQKGAQE-RAREQ 1315
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEaKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1316 AQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:PTZ00121 1475 AKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1392 THI----EAQGQAQKGAQEWARDRARDQGWEQTQIETQR-----------QTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121 1555 EELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeeeKKMKAEEAKKAEEAKIKA 1622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1245-1480 |
3.10e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1324
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1325 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGA 1404
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1405 QewARDRARDQGW--EQTQIETQRQTQKGAQERAWEQGREQALTSGMAprAWEQPISGIAEGVDAAGRSGGSRSPAPR 1480
Cdd:COG1196 500 E--ADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1241-1406 |
4.33e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.84 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQAQWQTQIKAQKWA--QEQTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKgAQERAREQAQK 1318
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAaeQERLKQLEKERLAAQEQKKQAEEAAKQAA-----LKQKQAEE-AAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKGAQerAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:PRK09510 148 KAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
....*...
gi 767979166 1399 QAQKGAQE 1406
Cdd:PRK09510 226 AAAKAAAE 233
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1167-1431 |
1.27e-11 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 68.35 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1167 HSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE 1246
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1247 EAQGQAQWQTQIKAQKWAQ----EQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:pfam08017 105 RSQGNVLERRQRDAENKSQgnvlERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQTHI 1394
Cdd:pfam08017 185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRDAEN 264
|
250 260 270
....*....|....*....|....*....|....*..
gi 767979166 1395 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKG 1431
Cdd:pfam08017 265 RSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVG 301
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1445 |
9.53e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgaQERAREQAQK 1318
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---EAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAQEQGREQT 1392
Cdd:PTZ00121 1452 KAEEaKKAEEAKKKAEEaKKADEAKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAE 1531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1393 HIEAQGQAQKGAQEWARDRARdqgwEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELK----KAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1177-1388 |
9.81e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.60 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1177 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAqgqvqgqaqKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqt 1256
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQA---------AEQERLKQLEKERLAAQEQKKQAEEAAKQAAL--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1257 qikAQKWAQEQTQKGAQervQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1336
Cdd:PRK09510 130 ---KQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1337 REQAQKGAQERAREQAQKGAQERAREQA--QKGAQERAREQAQKGAQERAQEQG 1388
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAaeAKAAAEKAAAAKAAEKAAAAKAAA 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1245-1445 |
1.09e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1245 QEEAQgQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtQIEAQGQAQKGAQERAR---EQAQKGAQ 1321
Cdd:COG1196 219 KEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA------ELEAELEELRLELEELElelEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1322 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767979166 1402 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:COG1196 372 AELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1244-1444 |
1.54e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 66.08 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQaqkgaqeR 1323
Cdd:PRK12678 54 AIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAA-------Q 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:PRK12678 127 ARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRR 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767979166 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PRK12678 207 DRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDR 247
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1244-1441 |
1.75e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 65.70 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:PRK12678 71 AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGAqerareQAQKGAQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:PRK12678 151 QPATEARAD------AAERTEEEERDERRRRGDREDRQAEAERGERGR-REERGRDGDDRDRRDRREQGDRREERGRRDG 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 767979166 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:PRK12678 224 GDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGR 261
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1442 |
1.82e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAqEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQE-RAREQAQ 1317
Cdd:PTZ00121 1319 EAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE--RAQEQGR 1389
Cdd:PTZ00121 1398 KKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEaKKAEEAKKKAEEakKADEAKK 1477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1390 EQTHIEAQGQAQKGAQEWAR--DRARDQGWEQTQIETQRQTQ---KGAQERAWEQGRE 1442
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEeakKADEAKKAEEAKK 1535
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1135-1403 |
2.61e-10 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 64.50 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1135 QVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQG 1214
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1215 QVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQE 1294
Cdd:pfam08017 105 RSQGNVLE----RRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1295 QTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKGAQERAR----EQAQK 1366
Cdd:pfam08017 181 DAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQgnvlERRQRDAENKSQgnvlERRQR 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767979166 1367 GAQERAR----EQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam08017 261 DAENRSQgnvlERRQRDAENRSQGNVLERRQRDAENKSQVG 301
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1442 |
3.29e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQE-RAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAQ------- 1385
Cdd:PTZ00121 1386 KAEEkKKADEAKKKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEAKKaeeakkk 1465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1386 -EQGREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQE-RAWEQGRE 1442
Cdd:PTZ00121 1466 aEEAKKADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1242-1444 |
7.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1242 KWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERaqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQ 1321
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-----------LELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1322 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767979166 1402 KGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:COG1196 383 ELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1237-1441 |
1.37e-09 |
|
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: 61.79 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR02794 70 QKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERareQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1396
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767979166 1397 QGQAQKGAqewardrARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:TIGR02794 226 ERKADEAE-------LGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1120-1394 |
2.78e-09 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 61.03 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1120 AQGQAQKQVQEWDRGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIE 1199
Cdd:pfam08017 26 SQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1200 AQGQAQEPAQGGAQGQVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQ 1279
Cdd:pfam08017 106 SQGNVLERRQRDAENKSQGNVLE----RRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1280 AQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKG 1355
Cdd:pfam08017 182 AENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRD 261
|
250 260 270
....*....|....*....|....*....|....*....
gi 767979166 1356 AQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:pfam08017 262 AENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQV 300
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1254-1473 |
3.05e-09 |
|
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: 60.63 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1254 WQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1333
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1334 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQAQKGAQ--EWA 1408
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEakkKAEAEAKAKAEAEAKAKAEEAKAkaEAA 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979166 1409 RDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGG 1473
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAA 266
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1237-1435 |
8.75e-09 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 59.49 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:pfam08017 59 QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER----RQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQT 1392
Cdd:pfam08017 135 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQgnvlERRQRDA 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767979166 1393 HIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1435
Cdd:pfam08017 215 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLER 257
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1247-1401 |
1.64e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.73 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1247 EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKgAQERAREQAQkgaQERARE 1326
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETARA 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1327 QAQKG---AQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAQEQGrEQTHIEAQGQAQ 1401
Cdd:COG2268 263 EAEAAyeiAEANAEREVQRQLEIAEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEA-EAEAIRAKGLAE 339
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1244-1443 |
1.79e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQwqtqiKAQKwaqEQTQKGAQERVQGQAQKGAQE-RAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQE 1322
Cdd:PTZ00121 1092 ATEEAFGKAE-----EAKK---TETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1323 RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQThieaqgQAQK 1402
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKK 1237
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767979166 1403 GAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:PTZ00121 1238 DAEE-AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1298-1443 |
2.76e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 58.76 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1298 IEAQGQAQKGAQERAREQ-----AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1372
Cdd:PRK12678 52 IAAIKEARGGGAAAAAATpaapaAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1373 R--EQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:PRK12678 132 ErgEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1445 |
2.97e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEqTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--------------EQAQKGAQERAR-EQAQKGAQER 1383
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklyeeekkmkaEEAKKAEEAKIKaEELKKAEEEK 1632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979166 1384 AQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1444 |
3.52e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQaqeqtqieaqgQAQKGAQE-RAREQAQ 1317
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-----------EAKKKAEEaKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR-EQAQKGAQE---------RAQ 1385
Cdd:PTZ00121 1322 KKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEkkkadeakkKAE 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979166 1386 EQGREQTHIEAQGQAQKGAQEWAR--------DRARDQGWEQTQIETQRqtQKGAQERAWEQGREQA 1444
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKkaeekkkaDEAKKKAEEAKKADEAK--KKAEEAKKAEEAKKKA 1466
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1264-1470 |
3.64e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.13 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1343
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1344 AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIE 1423
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767979166 1424 TQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGR 1470
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAA 207
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1272-1389 |
5.97e-08 |
|
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: 53.51 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1272 AQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQER 1347
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767979166 1348 AREQAQK-GAQERAREQAQKGAQERAReQAQKGAQERAQEQGR 1389
Cdd:pfam05672 97 ERLQKQKeEAEAKAREEAERQRQEREK-IMQQEEQERLERKKR 138
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1434 |
6.29e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKgaqERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQE--RAQEQGREQ 1391
Cdd:PTZ00121 1676 KAEEAKKAEEDE---KKAAEALKKEAEEaKKAEELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEdkKKAEEAKKD 1752
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767979166 1392 THIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1434
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1439 |
6.34e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQ 1315
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1316 AQKGAQERAREQAQKGAQERAREQAQKG-----AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAeelkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767979166 1391 QTHIEAQG--QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:PTZ00121 1607 MKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1324-1435 |
8.19e-08 |
|
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: 53.12 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:pfam05672 23 AREQRER--EEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQ 100
|
90 100 110
....*....|....*....|....*....|....
gi 767979166 1402 KGAQEwARDRARDQGwEQTQIETQRQTQKGAQER 1435
Cdd:pfam05672 101 KQKEE-AEAKAREEA-ERQRQEREKIMQQEEQER 132
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1241-1435 |
1.16e-07 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 56.03 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQA----QWQTQIKAQKWAQEQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1312
Cdd:pfam08017 35 QRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1313 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQG 1388
Cdd:pfam08017 115 QRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767979166 1389 REQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1435
Cdd:pfam08017 195 QRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER 241
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1281-1474 |
2.20e-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: 54.85 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1281 QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAReqaQKGAQERAREQAQKGAQERAREQA--QKGAQE 1358
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR---QKELEQRAAAEKAAKQAEQAAKQAeeKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1359 RAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW-----ARDRARDQGWEQTQIETQRQTQKGAQ 1433
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAkkkaeAEAKAKAEAEAKAKAEEAKAKAEAAK 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767979166 1434 ERAWEQGREQA-LTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1474
Cdd:TIGR02794 203 AKAAAEAAAKAeAEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1301-1475 |
2.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1301 QGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1379
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1380 AQERAQEQGREQTHIEAQGQAQKGAQEWARDRARdQGWEQTQIETQRQTQKgAQERAWEQGREQALTSGMAPRAWEQPIS 1459
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEE-AKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
170
....*....|....*.
gi 767979166 1460 GIAEGVDAAGRSGGSR 1475
Cdd:PTZ00121 1263 AHFARRQAAIKAEEAR 1278
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1257-1530 |
2.82e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 55.05 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1257 QIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1336
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1337 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW--ARDRARD 1414
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAarAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1415 QGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPAPRDGGQSGGSGLGEPS 1494
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 767979166 1495 AGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGG 1530
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVV 281
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1237-1444 |
3.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQ----KGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1312
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1313 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1391 QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1177-1415 |
3.42e-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: 54.08 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1177 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKwaqgqiqgqaqkqvqgEVQKWAQEEAQGQAQWQT 1256
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE----------------QRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1257 QIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQER 1335
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEA----KAKAEAEAERKAKE-----EAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1336 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG---REQTHIEAQGQAQKGAQEWARDRA 1412
Cdd:TIGR02794 185 AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglASGSNAEKQGGARGAAAGSEVDKY 264
|
...
gi 767979166 1413 RDQ 1415
Cdd:TIGR02794 265 AAI 267
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1241-1444 |
4.15e-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: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQER------------------VQGQAQKGAQERAQEQAQEQTQIEAQG 1302
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkelekeeereederiLEYLKEKAEREEEREAEREEIEEEKER 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG---AQERAREQAQKG 1379
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKErrlAEEAEREEEEFE 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979166 1380 AQERAQEQGREQTHIEAQGQAQKgAQEWARDRARdqgweqtQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMK-RLEHRRELEK-------QIEEREEQRAAEREEELEEGERLR 321
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1299-1391 |
4.25e-07 |
|
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: 51.19 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQE-R 1371
Cdd:pfam05672 30 EEQERLEKEEEERLRkeELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaK 109
|
90 100
....*....|....*....|
gi 767979166 1372 AREQAQKGAQERAQEQGREQ 1391
Cdd:pfam05672 110 AREEAERQRQEREKIMQQEE 129
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1434 |
5.56e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQgQAQWQTQIKAQKWAQEqTQKGAQErvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERArEQAQKG-----A 1320
Cdd:PTZ00121 1215 EEAR-KAEDAKKAEAVKKAEE-AKKDAEE-----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKAdelkkA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1321 QE-RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGREQThiEA 1396
Cdd:PTZ00121 1287 EEkKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--EE 1364
|
170 180 190
....*....|....*....|....*....|....*...
gi 767979166 1397 QGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1434
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1444 |
6.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKwAQE----EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1314
Cdd:PTZ00121 1192 ELRK-AEDarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1315 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQErareqAQKGAQE---RAQEQGRE 1390
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEE-----AKKKADAakkKAEEAKKA 1344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767979166 1391 QTHIEAQGQAQKGAQEWARDRAR--DQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
|
| Glutenin_hmw |
pfam03157 |
High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
1123-1547 |
1.06e-06 |
|
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.
Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 53.41 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1123 QAQKQVQEWDRGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQtqieaQG 1202
Cdd:pfam03157 171 QQSGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQ-----QG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1203 QAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQW---QTQIKAQKWAQEQTQKGAQERVQGQ 1279
Cdd:pfam03157 246 QQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYyptSQQQAGQLQQEQQLGQEQQDQQPGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1280 AQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1359
Cdd:pfam03157 326 GRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQ 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1360 AREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWArdrarDQGWEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:pfam03157 406 QPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQP-----GQGQQPGQGQQGQQPGQPEQGQQPGQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1440 GREqaltsGMAPRAWEQPISGIAEGV-DAAGRSGGSRSPAPRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLG 1518
Cdd:pfam03157 481 GQP-----GYYPTSPQQSGQGQQLGQwQQQGQGQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQ 555
|
410 420
....*....|....*....|....*....
gi 767979166 1519 KSPTEPKPEAGGCGTPQAPAQEGSPDHPG 1547
Cdd:pfam03157 556 SGQGQQGQQPGQGQQGQQPGQGQQGQQPG 584
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1128-1376 |
1.20e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1128 VQEWDRGQVQGHAQEQAQWQTQieaqgqaqeqAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEp 1207
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRK----------KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAL- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1208 aqggaqgqvqgqaqkwaqGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqtqiKAQKWAQEQTQKGAQErvqgQAQKGAQEr 1287
Cdd:PRK09510 130 ------------------KQKQAEEAAAKAAAAAKAKAEAEAKRAA-----AAAKKAAAEAKKKAEA----EAAKKAAA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1288 aqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaQKGAQERAREQAQKG 1367
Cdd:PRK09510 182 -----------EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE--AKAAAEKAAAAKAAE 248
|
....*....
gi 767979166 1368 AQERAREQA 1376
Cdd:PRK09510 249 KAAAAKAAA 257
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1442 |
1.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQiEAQGQAQKGAQE--RAREQAQKGAQER 1323
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRK--AEELRKAEDARKAEAARKAEEERKAEEARKAED-AKKAEAVKKAEEakKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGAQER----AREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---------RAQEQGR 1389
Cdd:PTZ00121 1250 NNEEIRKFEEARmahfARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadeakkKAEEAKK 1329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1390 EQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1442
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1244-1444 |
2.57e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIK-AQKWAQ-----EQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1317
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEeAKKKAEdarkaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA------REQAQKGAqerarEQAQKGAQERAQEQGREQ 1391
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkkAEEAKKDA-----EEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1392 THIEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1443 |
3.82e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQErar 1325
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK---------KVEQLKKKEAEEKKKAEELKKAEE--- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1326 EQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAR--EQAQKGAQE--RAQEQGR---EQTHIEAQg 1398
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEEAKkaEELKKKEAEekKKAEELKkaeEENKIKAE- 1733
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767979166 1399 QAQKGAQEWAR--DRARDQGWEQTQIEtqrQTQKGAQERAWEQGREQ 1443
Cdd:PTZ00121 1734 EAKKEAEEDKKkaEEAKKDEEEKKKIA---HLKKEEEKKAEEIRKEK 1777
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1245-1381 |
4.63e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKgaqERVQGQAQKGAQEraqeqaqeqTQIEAQgQAQKGAQERAREQAQKGAQERA 1324
Cdd:COG2268 221 REAEEAELEQEREIETARIAEAEAEL---AKKKAEERREAET---------ARAEAE-AAYEIAEANAEREVQRQLEIAE 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1325 REQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAREQAQKgaqERAREQAQKGAQ 1381
Cdd:COG2268 288 REREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEAEA---EAIRAKGLAEAE 341
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1298-1436 |
4.92e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1298 IEAQGQAQ----KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQkgaQERAR 1373
Cdd:COG2268 186 LDALGRRKiaeiIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETAR 261
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1374 EQAQKGAQERAQEQGReqthiEAQGQAQKGAQEwardrardqgwEQTQIETQRQTQKGAQERA 1436
Cdd:COG2268 262 AEAEAAYEIAEANAER-----EVQRQLEIAERE-----------REIELQEKEAEREEAELEA 308
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1444 |
6.28e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARK--AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQ 1405
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
170 180 190
....*....|....*....|....*....|....*....
gi 767979166 1406 EWARDRARDQGWEQTQIETQRQTQKGAQERAwEQGREQA 1444
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKA-DAAKKKA 1338
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1298-1406 |
6.32e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1298 IEAQGQAQKGAQERAREQAQKgAQER-------AREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1370
Cdd:COG2268 208 AERETEIAIAQANREAEEAEL-EQEReietariAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEI 285
|
90 100 110
....*....|....*....|....*....|....*..
gi 767979166 1371 RAREQAQKGAQ-ERAQEQGREQTHIEAQGQAQKGAQE 1406
Cdd:COG2268 286 AEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE 322
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1240-1456 |
6.80e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1240 VQKWAQEEAQGQAQWQTQIKAQKWAQEQTQK--GAQERVQGQAQKGAQERAQEQaqeqtqieAQGQAQKGAQERAREQAQ 1317
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELE--------ELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1397
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1398 GQAQKGAQEwARDRARDQ----GWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQ 1456
Cdd:TIGR02168 467 REELEEAEQ-ALDAAERElaqlQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1239-1441 |
6.86e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGA-QERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1317
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQKGAQERAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKgaqERAQEQGREQTHIEAQ 1397
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELEELIEELESELEALLN---ERASLEEALALLRSEL 896
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1398 GQAQKGAQEW--ARDRARDQGWEQTQIETQRQTQKGA--------QERAWEQGR 1441
Cdd:TIGR02168 897 EELSEELRELesKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYS 950
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1294-1417 |
1.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1294 EQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAR 1373
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767979166 1374 EQAQkgaQERAQEQGREQTHIEAQ-GQAQKGAQEWARDRARDQGW 1417
Cdd:COG4913 326 DELE---AQIRGNGGDRLEQLEREiERLERELEERERRRARLEAL 367
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1199-1416 |
1.04e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.29 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1199 EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQg 1278
Cdd:PRK12678 57 EARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1279 QAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGaqeRAREQAQ----KGAQERAREQAQKGAQERAREQAQK 1354
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG---DREDRQAeaerGERGRREERGRDGDDRDRRDRREQG 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1355 GAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI--EAQGQAQKGAQEWARDRARDQG 1416
Cdd:PRK12678 213 DRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGddGEGRGGRRGRRFRDRDRRGRRG 276
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1236-1481 |
1.66e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQ 1315
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAR---------EAKAEAEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1316 AQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:COG3064 76 AKKLAEaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1395 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1474
Cdd:COG3064 156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
|
....*..
gi 767979166 1475 RSPAPRD 1481
Cdd:COG3064 236 AVEATEE 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1239-1445 |
1.72e-05 |
|
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: 49.74 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQwqtQIKAQKWAQEQTQKGAQERVQGQAQKG----AQERAQEQAQEQTQIEAQGQAQ--------- 1305
Cdd:pfam17380 349 ELERIRQEERKRELE---RIRQEEIAMEISRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQqqkvemeqi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1306 KGAQERARE-QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1384
Cdd:pfam17380 426 RAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979166 1385 Q---EQGREQTHIEAQGQAQKGA--QEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:pfam17380 506 QamiEEERKRKLLEKEMEERQKAiyEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1236-1391 |
1.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1314
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1315 QAQKGAQERAREQAQKgaqeRAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEK----KKAEELKKAEEENKIkaEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
.
gi 767979166 1391 Q 1391
Cdd:PTZ00121 1776 E 1776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1283-1426 |
2.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1283 GAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERARE 1362
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1363 QAQkgaQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQR 1426
Cdd:COG1196 711 EAE---EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1264-1371 |
3.51e-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: 45.42 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQ 1341
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQ 102
|
90 100 110
....*....|....*....|....*....|.
gi 767979166 1342 K-GAQERAREQAQKGAQERAReQAQKGAQER 1371
Cdd:pfam05672 103 KeEAEAKAREEAERQRQEREK-IMQQEEQER 132
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1171-1448 |
4.16e-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: 48.43 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1171 QAQKQFQNWAQGQAQghAQEQA-QWQTQI-EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE-- 1246
Cdd:TIGR00618 236 QQTQQSHAYLTQKRE--AQEEQlKKQQLLkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRih 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1247 -EAQGQAQWQTQIKAQKWA-QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1324
Cdd:TIGR00618 314 tELQSKMRSRAKLLMKRAAhVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1325 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAQEQGREQTHieaqgqAQKGA 1404
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELCAAAITCTAQCEKLEKIH------LQESA 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767979166 1405 QewaRDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQALTSG 1448
Cdd:TIGR00618 466 Q---SLKEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1259-1441 |
4.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1259 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQkgAQERARE 1338
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLE--------LLEAELEELRAELARLEAELERLEARLDALR--EELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1339 QAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQK-----GAQERAQEQGREQTHIEAQGQAQKGAQEWARDRAR 1413
Cdd:COG4913 330 AQIRGNGGDRLEQLE---REIERLERELEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 767979166 1414 DQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1259-1444 |
5.07e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1259 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR- 1337
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKi 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1338 --EQAQKGAQERAR-EQAQKGAQERAR--EQAQKGAQE---RAREQAQKGAQE--RAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:PTZ00121 1621 kaEELKKAEEEKKKvEQLKKKEAEEKKkaEELKKAEEEnkiKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190
....*....|....*....|....*....|....*....
gi 767979166 1408 ARDRARDQGWEQTQIETQRQTQKGAQERAW--EQGREQA 1444
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaEEAKKEA 1739
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1259-1406 |
5.85e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1259 KAQKWAQEQTQKgaQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQaqKGAQERARE 1338
Cdd:pfam05262 214 RAQQLKEELDKK--QIDAD-KAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ--KREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1339 QAQKGAQE--RAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQEQGREQTHIEAqgQAQKGAQE 1406
Cdd:pfam05262 289 EIKKNDEEalKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEDLQKTKPQVEA--QPTSLNED 354
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1244-1475 |
7.38e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:COG3064 41 EERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:COG3064 121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979166 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSR 1475
Cdd:COG3064 201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAA 272
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1267-1438 |
8.20e-05 |
|
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: 47.25 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1267 QTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaqkgaQE 1346
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE------EE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1347 RAREQAQKGAQERAREQAQ---KGAQERAREQAQKGAqERAQEQGREQTHIEAQ-GQAQKGAQEWArdrardqgwEQTQI 1422
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEefrRKLQELQRKKQQEEA-ERAEAEKQRQKELEMQlAEEQKRLMEMA---------EEERL 477
|
170
....*....|....*.
gi 767979166 1423 ETQRQTQKGAQERAWE 1438
Cdd:pfam15709 478 EYQRQKQEAEEKARLE 493
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1303-1443 |
1.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKG 1379
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSELEQRLRQQQR---AERLLAEFCKR 545
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1380 A----------QERAQEQGREQTHIEAQgQAQKGAQewaRDRARDQGwEQTQIETQRQTQKG-----AQERAwEQGREQ 1443
Cdd:PRK04863 546 LgknlddedelEQLQEELEARLESLSES-VSEARER---RMALRQQL-EQLQARIQRLAARApawlaAQDAL-ARLREQ 618
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1239-1564 |
1.21e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:COG3064 56 EAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:COG3064 136 KAEEERKAAEAEAAAKAEAEAAR--AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPA 1478
Cdd:COG3064 214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1479 PRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPGAERALQDRMEA 1558
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
....*.
gi 767979166 1559 SEPERR 1564
Cdd:COG3064 374 ALLLGK 379
|
|
| DUF5384 |
pfam17358 |
Family of unknown function (DUF5384); This is a family of unknown function found in ... |
1299-1397 |
1.24e-04 |
|
Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.
Pssm-ID: 407453 [Multi-domain] Cd Length: 145 Bit Score: 43.82 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE-QAQ 1377
Cdd:pfam17358 1 EQQGKEDRVAAERQAAYEREWEEEQARAEAAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRALEiEER 80
|
90 100
....*....|....*....|.
gi 767979166 1378 KGAQERAQEQG-REQTHIEAQ 1397
Cdd:pfam17358 81 KLALAAQKARAkRENDFIDQE 101
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1322-1391 |
1.30e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.58 E-value: 1.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1322 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAQ---ERAREQAQKgAQERAQEQGREQ 1391
Cdd:cd06503 43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEAErilEQAKAEIEQ-EKEKALAELRKE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1244-1398 |
1.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQ------ERAREQAQ 1317
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlerEIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQK-----GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaqERAQEQGREQT 1392
Cdd:COG4913 354 LEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR----RELRELEAEIA 429
|
....*.
gi 767979166 1393 HIEAQG 1398
Cdd:COG4913 430 SLERRK 435
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1270-1389 |
1.43e-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: 44.29 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1270 KGAQERVQGQAQKgaQERAQEQAQEQTQIEAQGQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAR 1349
Cdd:pfam11600 1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767979166 1350 EQAQKGAQERAREQAQKGAQE----RAREQAQKGAQERAQEQGR 1389
Cdd:pfam11600 78 DEKEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEK 121
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1239-1409 |
1.44e-04 |
|
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: 46.48 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQ-KGAQERAREQAQ 1317
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFE--EIRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQQQE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 ---KGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQK--GAQERAREQAQKGAQErAREQAQKGAQERAQEQgrEQ 1391
Cdd:pfam15709 427 efrRKLQELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQE-AEEKARLEAEERRQKE--EE 503
|
170
....*....|....*...
gi 767979166 1392 THIEAQGQAQKGAQEWAR 1409
Cdd:pfam15709 504 AARLALEEAMKQAQEQAR 521
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1310-1391 |
1.76e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 43.61 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1310 ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKGAQ---ERAREQAQKGAqERAREQAQKGAQ---ER 1383
Cdd:PRK05759 48 ERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKKRAAqiiEEAKAEAEAEA-ARIKAQAQAEIEqerKR 115
|
....*...
gi 767979166 1384 AQEQGREQ 1391
Cdd:PRK05759 116 AREELRKQ 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1322-1444 |
1.92e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1322 ERAREQAQK----GAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIE- 1395
Cdd:COG1196 206 ERQAEKAERyrelKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEe 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767979166 1396 AQGQAQKGAQEWARDRARDQGWEQTQIE-TQRQTQKGAQERAWEQGREQA 1444
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEEL 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1183-1389 |
2.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1183 QAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQK 1262
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1263 WAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEaqgQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR 1337
Cdd:PTZ00121 1668 KKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAE---ELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1338 --EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGR 1389
Cdd:PTZ00121 1745 kaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1294-1467 |
2.43e-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: 45.76 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1294 EQtqieaqgqaqkgaqERAREQAQKgAQERAREQAQKGaqERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR 1373
Cdd:pfam05262 214 RA--------------QQLKEELDK-KQIDADKAQQKA--DFAQDNADK--QRDEVRQKQQEAKNLPKPADTSSPKEDKQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1374 -EQAQKGAQERAQEQGREQTHiEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQ--ERAWEQGREQALTSGM 1449
Cdd:pfam05262 275 vAENQKREIEKAQIEIKKNDE-EALKAKDHKAFDLKQEsKASEKEAEDKELEAQKKREPVAEdlQKTKPQVEAQPTSLNE 353
|
170
....*....|....*...
gi 767979166 1450 APRAWEQPISGIaEGVDA 1467
Cdd:pfam05262 354 DAIDSSNPVYGL-KVVDP 370
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1241-1442 |
2.64e-04 |
|
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: 44.91 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQAQWQTQ-IKAQKWAQEQTQKGAQERVQGQAQkgaqeraqeqaqeqtqIEAQGQAQKGAQERAREQAQKG 1319
Cdd:pfam13868 36 AEEKEEERRLDEMMEEErERALEEEEEKEEERKEERKRYRQE----------------LEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1320 AQERaREQAQKGAQERAREQAQKGAQERA---------REQAQKGAQERARE----------QAQKGAQERAREQAQKgA 1380
Cdd:pfam13868 100 REQM-DEIVERIQEEDQAEAEEKLEKQRQlreeidefnEEQAEWKELEKEEEreederileyLKEKAEREEEREAERE-E 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979166 1381 QERAQEqgREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1442
Cdd:pfam13868 178 IEEEKE--REIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1252-1469 |
2.79e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1252 AQWQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqERAREQAQKG 1331
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVASAEREIAEL---EAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1332 AQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKgAQERAQEQGREQTHIEAQGQAQKGAQEWAR-- 1409
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEE-ELDELQDRLEAAEDLARLELRALLEERFAAal 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1410 -DRARDQgwEQTQIETQRQTQKGAQERAweqgrEQALTSGMAP--RAWEQPISGIAEGVDAAG 1469
Cdd:COG4913 760 gDAVERE--LRENLEERIDALRARLNRA-----EEELERAMRAfnREWPAETADLDADLESLP 815
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
1236-1390 |
2.84e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.93 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQ--EQTQIEAQGQAQKGAQERAR 1313
Cdd:PTZ00341 979 VEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEydEENVEEIEENAEENVEENIE 1058
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979166 1314 EQAQKGAQERArEQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00341 1059 ENIEEYDEENV-EEIEENIEENIEENVEENVEENV-EEIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNEE 1133
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1244-1452 |
3.17e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQG---QAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGA----QERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR00618 251 AQEEQLKkqqLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1317 QKGAQERAREQAQKG-------AQERAREQAQKGAQERAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQEQgR 1389
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRllqtlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQ-R 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979166 1390 EQTHIEAQGQAQKGAQEwarDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPR 1452
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQG---QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1303-1430 |
3.22e-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: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:pfam11600 8 QSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767979166 1383 RAQEQGRE--QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQK 1430
Cdd:pfam11600 87 RLKEEKRKekQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1256-1458 |
3.56e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1256 TQIKAQKWAQEQTQKGAQERVQGQAQ---KGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER-AREQAQKG 1331
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKReAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1332 AQERAREQAQKG---AQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQA-QKGA 1404
Cdd:TIGR00618 259 QQLLKQLRARIEelrAQEAVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRihtELQSKMRSRAKLLMKRAAhVKQQ 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1405 QEWARDRARDQGWEQTQIETQRQTQkgaQERAWEQGREQALTSGMAPRAWEQPI 1458
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHE---VATSIREISCQQHTLTQHIHTLQQQK 388
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1300-1422 |
4.16e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1300 AQGQAQKGAQERAREQAQKGA---QERAREQAQKGAQERAREQAQKgAQERAREQAQKGA-QERAREQAQKGAQE-RARE 1374
Cdd:COG1566 86 AQAEAQLAAAEAQLARLEAELgaeAEIAAAEAQLAAAQAQLDLAQR-ELERYQALYKKGAvSQQELDEARAALDAaQAQL 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767979166 1375 QAQKGAQERAQEQGREQTHIEAQGQAQKGAQEwARDRARDQgWEQTQI 1422
Cdd:COG1566 165 EAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAELN-LARTTI 210
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1309-1414 |
4.18e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 42.46 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1309 QERAREQAQKGAQ-ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKgaqeRAREQAQKgAQERAQEq 1387
Cdd:PRK05759 34 EERQKKIADGLAAaERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKK----RAAQIIEE-AKAEAEA- 96
|
90 100
....*....|....*....|....*..
gi 767979166 1388 grEQTHIEAQGQAQKGAQewaRDRARD 1414
Cdd:PRK05759 97 --EAARIKAQAQAEIEQE---RKRARE 118
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
748-1142 |
4.28e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 748 GAMAAAGSVASRATPAPAPGSTQSPGDRtAGEPETLGQWGSRALSESHPRGEALPRDPHSHGLLAPGGSLEPKSGAAGRS 827
Cdd:PRK07764 417 PAAAAAPAPAAAPQPAPAPAPAPAPPSP-AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 828 LLRGVALVQHPEDIATLARH-PEDAAALARHPEAarlyisnTSAASRHTAAVGG-RKDVAVegnlLGFSTES---GIPAS 902
Cdd:PRK07764 496 APAAPAAPAGADDAATLRERwPEILAAVPKRSRK-------TWAILLPEATVLGvRGDTLV----LGFSTGGlarRFASP 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 903 DHPRPQARSVAE------SPSYGPGlpPSPPENPQAKGREGVRFPRGAEPDHLLPAVPPAEVDMGWVGGTHQRGPPHLQA 976
Cdd:PRK07764 565 GNAEVLVTALAEelggdwQVEAVVG--PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 977 HLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVAPSGskvvlnPAKEPQTWWAQ 1056
Cdd:PRK07764 643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAGQADD 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1057 DLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEGtrAARNPAVPPGEPEGPGSPAAQGQAQKQVQEWDRGQV 1136
Cdd:PRK07764 717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
|
....*.
gi 767979166 1137 QGHAQE 1142
Cdd:PRK07764 795 DEDRRD 800
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1316-1401 |
5.05e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.91 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1316 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:pfam00430 38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115
|
....*..
gi 767979166 1395 EAQGQAQ 1401
Cdd:pfam00430 116 RQQVVAL 122
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1255-1436 |
5.28e-04 |
|
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: 44.73 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1255 QTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERA-------QEQAQEQTQIEAQGQAQkgaQERAREQAQKGAQERAREQ 1327
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAremervrLEEQERQQQVERLRQQE---EERKRKKLELEKEKRDRKR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1328 aqkgAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:pfam17380 489 ----AEEQRRKILEKELEERKQAMIE---EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561
|
170 180
....*....|....*....|....*....
gi 767979166 1408 ARDRARDQGWEQTQiETQRQTQKGAQERA 1436
Cdd:pfam17380 562 TEERSRLEAMERER-EMMRQIVESEKARA 589
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1253-1472 |
5.30e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 44.99 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1253 QWQTQIkaQKWAQEQTQKGAQERVQ--GQAQKGA---QERAQEQAQEQTQIEAQGQAQKGaQERAREQAQKGAQERAREQ 1327
Cdd:TIGR00927 603 KWNKQI--ELWVKEQLSRRPVAKVMalGDLSKGDvaeAEHTGERTGEEGERPTEAEGENG-EESGGEAEQEGETETKGEN 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1328 AQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKG-AQERAQEQGRE-QTHIEAQGQAQKGA 1404
Cdd:TIGR00927 680 ESEGEIPAERKGEQEGEGEiEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIeTGEEGEEVEDEgEGEAEGKHEVETEG 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1405 QEWARDRARDQGWEQTQIETQRQTQKGAQ-ERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSG 1472
Cdd:TIGR00927 760 DRKETEHEGETEAEGKEDEDEGEIQAGEDgEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEV 828
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1304-1390 |
5.49e-04 |
|
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: 43.72 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1304 AQKGAQERAREQAQKGAQERAREQAQKgaqeraREQAQKGAQERAREQAQKGAQERA--REQAQKGAQERAREQA---QK 1378
Cdd:cd16269 201 EAERAKAEAAEQERKLLEEQQRELEQK------LEDQERSYEEHLRQLKEKMEEEREnlLKEQERALESKLKEQEallEE 274
|
90
....*....|..
gi 767979166 1379 GAQERAQEQGRE 1390
Cdd:cd16269 275 GFKEQAELLQEE 286
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1310-1443 |
6.04e-04 |
|
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: 43.75 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1310 ERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERARE-QAQKGAQERAREQAQKGAQERAQEQG 1388
Cdd:pfam13868 50 EEERERALE--EEEEKEEERKEERKRYRQELEEQIEER-EQKRQEEYEEKLQErEQMDEIVERIQEEDQAEAEEKLEKQR 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767979166 1389 REQTHIEAQGQAQKGAQEWARDRARDqgwEQTQIEtQRQTQKGAQERAWEQGREQ 1443
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEERE---EDERIL-EYLKEKAEREEEREAEREE 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1322-1444 |
6.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1322 ERAREQAQKgAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQ 1399
Cdd:COG4913 238 ERAHEALED-AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767979166 1400 AQKGAQEwardrardqgwEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:COG4913 317 RLDALRE-----------ELDELEAQIRGNGGDRLEQLEREIERL 350
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1324-1462 |
6.54e-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: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQerareQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam13904 62 AAKQRQRQ-KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKAR-----QQTKKREESHKQKAAESASKSLAKPERKV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1404 AQEWARDRArdQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIA 1462
Cdd:pfam13904 136 SQEEAKEVL--QEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQKWMKNVK 192
|
|
| V_ATP_synt_G |
TIGR01147 |
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ... |
1303-1385 |
7.22e-04 |
|
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130217 [Multi-domain] Cd Length: 113 Bit Score: 40.97 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1303 QAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:TIGR01147 13 QAEKRAAEKVSE-ARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAKIREIKKAVQKN 91
|
...
gi 767979166 1383 RAQ 1385
Cdd:TIGR01147 92 KDA 94
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1241-1427 |
7.45e-04 |
|
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: 43.75 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGA--QERAQEqaqeqtqieaqgqaqkgaqERAREQAQK 1318
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-KAERDElrAKLYQE-------------------EQERKERQK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAE---REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI 299
|
170 180
....*....|....*....|....*....
gi 767979166 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQ 1427
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERR 328
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1245-1443 |
7.85e-04 |
|
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: 43.87 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1245 QEEAQGQAQWQTQIKAQKWAQEQTQkgaQERVQGQAQKGAQEraqeqaqeqtqiEAQGQAQKGAQERAR----EQAQKGA 1320
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGREE---RRRADRREKQVIEK------------ESRWREQAEDQENQRqeklERARQEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1321 QERAREQAQkgaqeraREQAQKGAQERAREQAQKGAQERAREQAQK---------------GAQERAREQAQKGA---QE 1382
Cdd:pfam15558 119 EQRKQCQEQ-------RLKEKEEELQALREQNSLQLQERLEEACHKrqlkereeqkkvqenNLSELLNHQARKVLvdcQA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979166 1383 RAQEQGR----EQTHIEAQGQAQKGAQEWARD-RARDQGWEQtqietqrQTQKgAQERAWEQGREQ 1443
Cdd:pfam15558 192 KAEELLRrlslEQSLQRSQENYEQLVEERHRElREKAQKEEE-------QFQR-AKWRAEEKEEER 249
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1308-1444 |
8.60e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1308 AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ------ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1381
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHnsyeedSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1382 ERAQEQGREQTHI------EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:pfam02029 84 ERQKEFDPTIADEkesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA 152
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1304-1385 |
9.79e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 40.76 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1304 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:pfam00430 38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115
|
...
gi 767979166 1383 RAQ 1385
Cdd:pfam00430 116 RQQ 118
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1301-1415 |
9.97e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 42.86 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1301 QGQAQkGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAReqaQKGA 1380
Cdd:PRK06991 149 QAQAD-AARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAA-ALERAR---KKKE 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 767979166 1381 QERAQEQG-REQTHIEAQGQAQKGAQEWARDRARDQ 1415
Cdd:PRK06991 224 ELAAQGAGpKNTEGVSAAVQAQIDAAEARRKRLAEQ 259
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1237-1374 |
1.14e-03 |
|
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: 43.40 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQEraqeqaqeqtqIEAQGQAQKGAQERAREQA 1316
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER-----------AEAEKQRQKELEMQLAEEQ 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1317 QK--GAQERAREQAQKGAQErAREQAQKGAQERarEQAQKGAQERAREQAQKGAQERARE 1374
Cdd:pfam15709 466 KRlmEMAEEERLEYQRQKQE-AEEKARLEAEER--RQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1309-1444 |
1.15e-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: 42.38 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1309 QERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQErAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG 1388
Cdd:pfam13904 70 KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ-QTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWE 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767979166 1389 REQThieAQGQAQKgaQEWARDRARDQgweqtQIETQRQTQKgaqERAWEQGREQA 1444
Cdd:pfam13904 149 RKKL---EQQQRKR--EEEQREQLKKE-----EEEQERKQLA---EKAWQKWMKNV 191
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1299-1381 |
1.20e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQGQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAREQAQKGAqERAREQAQKGAQERA 1372
Cdd:cd06503 44 KAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAEI-EQEKEKALAELRKEV 119
|
....*....
gi 767979166 1373 REQAQKGAQ 1381
Cdd:cd06503 120 ADLAVEAAE 128
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1237-1446 |
1.58e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.45 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR00927 682 EGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDR 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1396
Cdd:TIGR00927 762 KETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767979166 1397 QGQAQKGAQ----EWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALT 1446
Cdd:TIGR00927 842 QGEAKQDEKgvdgGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1299-1382 |
1.60e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQgQAQKGAQER---AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQERAREQ 1375
Cdd:COG0711 49 EAE-AALAEYEEKlaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAEVADL 123
|
....*..
gi 767979166 1376 AQKGAQE 1382
Cdd:COG0711 124 AVAIAEK 130
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1310-1386 |
1.74e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1310 ERAREQAQKGAQER------AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQER 1383
Cdd:COG0711 44 ERAKEEAEAALAEYeeklaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAE 119
|
...
gi 767979166 1384 AQE 1386
Cdd:COG0711 120 VAD 122
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1236-1413 |
1.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1236 VQGEVQKWAQEEAQGQAQwQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIE-AQGQAQKGAQERARE 1314
Cdd:COG4372 43 LQEELEQLREELEQAREE-LEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELEsLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1315 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170
....*....|....*....
gi 767979166 1395 EAQGQAQKGAQEWARDRAR 1413
Cdd:COG4372 200 EELAEAEKLIESLPRELAE 218
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1304-1409 |
1.96e-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: 42.18 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1304 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQaqkgaqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1383
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQ------ERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEER 250
|
90 100 110
....*....|....*....|....*....|..
gi 767979166 1384 AQ---EQGREQTHiEAQGQA---QKGAQEWAR 1409
Cdd:cd16269 251 ENllkEQERALES-KLKEQEallEEGFKEQAE 281
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1244-1424 |
2.15e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:PRK05035 463 EREKAAREARHKKAAEARAAKDKDAVAAALARVK--AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1324 AREQAQKGAQE--RAREQAQKGAQerarEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAq 1401
Cdd:PRK05035 541 AAADPKKAAVAaaIARAKAKKAAQ----QAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA- 615
|
170 180
....*....|....*....|...
gi 767979166 1402 KGAQEWARDRARDQGWEQTQIET 1424
Cdd:PRK05035 616 AVAAAIARAKAKKAEQQANAEPE 638
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1246-1445 |
2.39e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQAQKGAQE 1322
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1323 RAREQAQKgAQERAREQAQKGAQERAREQAQKGAQER-AREQAQKGAQERAREQAQKGAQERAQEQgrEQTHIEAQGQAQ 1401
Cdd:TIGR00618 277 AVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRAAHVKQQSSIE--EQRRLLQTLHSQ 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767979166 1402 KgaqewarDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQAL 1445
Cdd:TIGR00618 354 E-------IHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLT 392
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1188-1390 |
2.60e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1188 AQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQ 1267
Cdd:PRK12678 73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1268 TQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQER 1347
Cdd:PRK12678 153 ATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRD-GDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767979166 1348 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGR 274
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1168-1377 |
2.74e-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: 41.75 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQwQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEE 1247
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQAR-QKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1248 AQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERARE 1326
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767979166 1327 QAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQ 1377
Cdd:TIGR02794 224 EAERKADEAELGDIFGLASGsNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1322-1391 |
2.90e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.77 E-value: 2.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1322 ERAREQAQKgAQERAREQAQKGAQERA--REQAQKGAQ---ERAREQAQKGAqERAREQAQK---GAQERAQEQGREQ 1391
Cdd:COG0711 44 ERAKEEAEA-ALAEYEEKLAEARAEAAeiIAEARKEAEaiaEEAKAEAEAEA-ERIIAQAEAeieQERAKALAELRAE 119
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1309-1439 |
3.65e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.95 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1309 QERaREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQK-GAQERAREQAQKGAQERAREQAQKgaQERAQEQ 1387
Cdd:PRK10811 604 QDR-RKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQqTAETRESQQAEVTEKARTQDEQQQ--APRRERQ 680
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767979166 1388 GREQthiEAQGQAQKGAQEWARDRARDQgwEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:PRK10811 681 RRRN---DEKRQAQQEAKALNVEEQSVQ--ETEQEERVQQVQPRRKQRQLNQ 727
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1334-1415 |
3.89e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.34 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1334 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAQEQGREQthIEAQGQAqkgaqew 1407
Cdd:cd06503 43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAE--IEQEKEK------- 110
|
....*...
gi 767979166 1408 ARDRARDQ 1415
Cdd:cd06503 111 ALAELRKE 118
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1260-1385 |
3.93e-03 |
|
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: 40.06 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1260 AQKWAQEQTQKgaqERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQ 1339
Cdd:pfam11600 3 SQKSVQSQEEK---EKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767979166 1340 AQKGAQERAREQAQKGAQE----RAREQAQKGAQERAREQAQKGAQERAQ 1385
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1241-1452 |
3.96e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAqgqAQKGAQERA---REQAQ 1317
Cdd:PRK10246 226 QVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSL---AQPARQLRPhweRIQEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGA----QERAREQAQKGAQERAQ--EQGREQ 1391
Cdd:PRK10246 303 SAALAHTRQQIE---EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwlaeHDRFRQWNNELAGWRAQfsQQTSDR 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767979166 1392 THIEAQgQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQgREQALTSGMAPR 1452
Cdd:PRK10246 380 EQLRQW-QQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQ 438
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1299-1381 |
4.05e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQ 1377
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQlEQLQEKAAETSQERKQKRKE 220
|
....
gi 767979166 1378 KGAQ 1381
Cdd:PRK11448 221 ITDQ 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1298-1407 |
4.06e-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: 41.29 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1298 IEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQ 1377
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
90 100 110
....*....|....*....|....*....|
gi 767979166 1378 KGAQERAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| AhaH |
TIGR02926 |
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ... |
1323-1403 |
4.19e-03 |
|
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.
Pssm-ID: 131972 [Multi-domain] Cd Length: 85 Bit Score: 37.90 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1323 RAREQAQKGAQErAREQAQKGAQErAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQK 1402
Cdd:TIGR02926 6 KAEEDAEELIEE-AEEERKQRIAE-AREEARE-LLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIEAMKSKAK 82
|
.
gi 767979166 1403 G 1403
Cdd:TIGR02926 83 E 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1264-1435 |
4.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQ-AQKGAQERAREQAQK 1342
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAElERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1343 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQA-QKGAQEWARDRARDQGWEQTQ 1421
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAlRAEAAALLEALEEELEALEEA 406
|
170
....*....|....
gi 767979166 1422 IETQRQTQKGAQER 1435
Cdd:COG4913 407 LAEAEAALRDLRRE 420
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1257-1467 |
4.62e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1257 QIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1335
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEaKARFEARQARLEREKA--------AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1336 AREQAQKG--------AQERAREQAQKGAQERAREQA------QKGAQERAREQAQKGAQERAQEQGREqthiEAQGQAQ 1401
Cdd:PRK05035 505 PIVIKAGArpdnsaviAAREARKAQARARQAEKQAAAaadpkkAAVAAAIARAKAKKAAQQAANAEAEE----EVDPKKA 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767979166 1402 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDA 1467
Cdd:PRK05035 581 AVAAAIARAKAKKA---AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1188-1405 |
4.75e-03 |
|
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: 41.18 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1188 AQEQAQWQTQIEAQ----GQAQEPAQGGAQGQVQGQAQKWAQgqiqgqaqkqvQGEVQKWAQEEAQGQAQWQTQIKaqKW 1263
Cdd:pfam15558 57 QQSQEQWQAEKEQRkarlGREERRRADRREKQVIEKESRWRE-----------QAEDQENQRQEKLERARQEAEQR--KQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1264 AQEQTQKgAQERV----QGQAQKGAQERAQEQAQEQTQIEAQGQAQKGA---QERAREQAQKGA---QERAREQAQKGAQ 1333
Cdd:pfam15558 124 CQEQRLK-EKEEElqalREQNSLQLQERLEEACHKRQLKEREEQKKVQEnnlSELLNHQARKVLvdcQAKAEELLRRLSL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1334 E----RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ------ERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam15558 203 EqslqRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEalaelaDRKIQQARQVAHKTVQDKAQRA 282
|
..
gi 767979166 1404 AQ 1405
Cdd:pfam15558 283 RE 284
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1318-1441 |
4.88e-03 |
|
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: 39.67 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1318 KGAQERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1397
Cdd:pfam11600 1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767979166 1398 GQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:pfam11600 78 DEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEK 121
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1313-1443 |
5.51e-03 |
|
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: 41.09 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1313 REQaQKGAQERAREQAQKGAQ---ERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQ 1387
Cdd:pfam15709 328 REQ-EKASRDRLRAERAEMRRlevERKRreQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE 406
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767979166 1388 GREQthiEAQGQAqkgaqewARDRARDQGWE--QTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:pfam15709 407 ERKQ---RLQLQA-------AQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQRQ 454
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1310-1453 |
5.59e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.12 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1310 ERAREQAQKGAQERAREQAQKG-AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERaqEQG 1388
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQK--REG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979166 1389 REQTHIEAQGQAQKGAQEWARDRARdqgweqtqiETQRQTQKGAQERAWEQGREQALTSGMAPRA 1453
Cdd:PRK07735 82 TEEVTEEEKAKAKAKAAAAAKAKAA---------ALAKQKREGTEEVTEEEKAAAKAKAAAAAKA 137
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1255-1448 |
5.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1255 QTQIKAQKWAQEQTQKGAQ-ERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQ---- 1329
Cdd:COG4372 42 KLQEELEQLREELEQAREElEQLEEELEQ-ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleel 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1330 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWAR 1409
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190
....*....|....*....|....*....|....*....
gi 767979166 1410 DRARDQgWEQTQIETQRQTQKGAQERAWEQGREQALTSG 1448
Cdd:COG4372 201 ELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1265-1394 |
6.28e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.38 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1265 QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqerAREQAqKGAQERAREQAqkga 1344
Cdd:PRK06669 32 IKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLK-----KTDEA-SSIIEKLQMQI---- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767979166 1345 qERAREQAQKgAQERAREQA-QKGAQErAREQAQKGAQERAQEQGREQTHI 1394
Cdd:PRK06669 102 -EREQEEWEE-ELERLIEEAkAEGYEE-GYEKGREEGLEEVRELIEQLNKI 149
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1299-1384 |
7.99e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1299 EAQGQAQ---KGAQERAREQAQKgAQERAREQAqkgaqERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQ 1375
Cdd:COG0711 63 EARAEAAeiiAEARKEAEAIAEE-AKAEAEAEA-----ERIIAQAEA-EIEQERAKALAELRAEVADLAVAIAEKILGKE 135
|
....*....
gi 767979166 1376 AQKGAQERA 1384
Cdd:COG0711 136 LDAAAQAAL 144
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1300-1381 |
8.79e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 38.06 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1300 AQGQAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQ 1377
Cdd:pfam00430 47 KDAAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQvvALAV 124
|
....
gi 767979166 1378 KGAQ 1381
Cdd:pfam00430 125 QIAE 128
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1241-1391 |
8.91e-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: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1241 QKWAQEEAQgQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGA 1320
Cdd:COG4913 262 ERYAAARER-LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1321 QERAREQAQKGAQERAREQAQKGAQERAR---------EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1245-1391 |
9.80e-03 |
|
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: 39.90 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979166 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKgAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgAQERAREQAQKGAQERA 1324
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERK-ERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRK 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979166 1325 REQAQKGAQERAREQAQKGAQERA--REQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:pfam13868 270 QAEDEEIEQEEAEKRRMKRLEHRRelEKQIEEREEQRAAEREEE-LEEGERLREEEAERRERIEEERQK 337
|
|
| |
