|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-371 |
1.63e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEA 180
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 181 EENQRKQRENEEKERLENER-RLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:COG1196 320 ELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 260 AAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELspsATESELEEDAAIAEQSRRLISSRTDLEQKQRMIE 339
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270
....*....|....*....|....*....|..
gi 320545984 340 ENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-371 |
4.16e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 50 AAADAEELPRMRERLDKQIKEAAEREALAGTNVMQdgvlYVNGIRvdPAGDKRQALAAELARQQQIEADTRRQLAEAEAK 129
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIA--RLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 130 LVEERLRVQREKEESEEQQRKLVEAERQRER-EQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAERE 208
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 209 REENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRD 288
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 289 AE----------IVERLLAAERELSPS-----ATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMV 353
Cdd:COG1196 499 AEadyegflegvKAALLLAGLRGLAGAvavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
330
....*....|....*...
gi 320545984 354 MLQQRQLQASHSKEEADE 371
Cdd:COG1196 579 LDKIRARAALAAALARGA 596
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-371 |
1.30e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQQQIEADTRrqlaEAEAKLVE-ERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREaERRQLE 179
Cdd:COG1196 206 ERQAEKAERYRELKEELKEL----EAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-ELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 180 AEENQRKQRENEEKERLENERRLIDaerereenerrlqeaeeqrereeserrivVAERQREQAEAEKERAEQQRilaeae 259
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIA-----------------------------RLEERRRELEERLEELEEEL------ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 260 aAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIE 339
Cdd:COG1196 326 -AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270
....*....|....*....|....*....|..
gi 320545984 340 ENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEE 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-369 |
6.55e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 109 LARQQQIEADTRRQLA--EAEAKLVEERLRVQREKEESEEQQR--KLVEAERQREREQAEkelQEQREAERRQLEAEENQ 184
Cdd:COG1196 188 LERLEDILGELERQLEplERQAEKAERYRELKEELKELEAELLllKLRELEAELEELEAE---LEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 185 RKQRENEEKERLENERRLIDAEREreenerrlQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAE 264
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA--------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 265 RRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARR 344
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260
....*....|....*....|....*
gi 320545984 345 FLEAEEEMVMLQQRQLQASHSKEEA 369
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-359 |
2.71e-12 |
|
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: 72.40 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 54 AEELPRMRERLDKQiKEAAEReALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEE 133
Cdd:TIGR02168 195 LNELERQLKSLERQ-AEKAER-YKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 134 RLRVQREKEESEEQQRKLVEAerqrEREQAEKELQEQREAERRqleaeENQRKQRENEEKERLENERRLIDAEREREENE 213
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYAL----ANEISRLEQQKQILRERL-----ANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 214 RRLQEAEEQREREESErrivVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAeiVE 293
Cdd:TIGR02168 344 EKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR--RE 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320545984 294 RLLAAERELSPSATESELEE--------DAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQ 359
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKElqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
113-381 |
1.17e-10 |
|
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: 67.07 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 113 QQIEADTRRQLAEAEAKLVEERLRVQREKEESE-EQQRKLVEAERQRereQAEKELQEQREAERRQLEAEENQRKQRENE 191
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREvERRRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 192 EKERLENER---RLIDAEREREENERRLQEAEEQREREESERriVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLF 268
Cdd:pfam17380 356 EERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQE--LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 269 DAEIQRERDQADEEGQALRDAEI-----VERLLAAERELSPSATESELEE-DAAIAEQSRRLISSRTDLEQKQRMIEE-N 341
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQerqqqVERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKILEKELEERKQAMIEEeR 513
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 320545984 342 ARRFLEAEEEMvmlQQRQLQASHSKEEADEYAGMEPVVEE 381
Cdd:pfam17380 514 KRKLLEKEMEE---RQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
95-251 |
1.43e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.60 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 95 VDPAgdkrqALAAELARQQQIEADTRRQlAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAE 174
Cdd:PRK09510 55 VDPG-----AVVEQYNRQQQQQKSAKRA-EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 175 RRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQ 251
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-405 |
7.66e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQqRKLVEAERQREREQAE--KELQEQREAER 175
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-KKAEEAKKADEAKKAEeaKKADEAKKAEE 1544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 176 RQlEAEENQRKQ--RENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQ---AEAEKERAE 250
Cdd:PTZ00121 1545 KK-KADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 251 QQRILAEAEAAQAERRLFDAEIQRERDQ--ADEEGQALRDAEIVERllAAERELSPSATESELEEDAAIAEQSRRLISSR 328
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320545984 329 TDLEQKQRMIEENARRF--LEAEEEMVMLQQRQLQashSKEEADEYAGMEPVVEELCVKKVAPPRFQEPPEEPMVHKVK 405
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAeeLKKAEEENKIKAEEAK---KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
100-357 |
1.58e-09 |
|
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: 63.22 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQALAAELARQQQIEADTRRQLAEAEAKLveERLRVQREKEESEE--QQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:pfam17380 320 EAEKARQAEMDRQAAIYAEQERMAMEREREL--ERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERVRQE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 178 LEA--------EENQRK----QRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIV---VAERQREQA 242
Cdd:pfam17380 398 LEAarkvkileEERQRKiqqqKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 243 EAEKERAEQQRIlaeaeaAQAERRLFDAEIQRERdqadeegQALRDAEIVERLLaaERELSPSATESELEEDAAIAEQSR 322
Cdd:pfam17380 478 ELEKEKRDRKRA------EEQRRKILEKELEERK-------QAMIEEERKRKLL--EKEMEERQKAIYEEERRREAEEER 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 320545984 323 RL---ISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQ 357
Cdd:pfam17380 543 RKqqeMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
55-311 |
3.38e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.43 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 55 EELPRMRERLDKQIKEAAER---------EALAGTNVMQDgvlyvNGIrVDPAGDKRQALAAELARQQ--QIEADTRRQL 123
Cdd:COG2268 143 EELNEDREKFAEKVQEVAGTdlaknglelESVAITDLEDE-----NNY-LDALGRRKIAEIIRDARIAeaEAERETEIAI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 124 AEAEaklveerlrvqREKEESEEQQRKLVEAER--QREREQAEKELQEQREAERRQLEAEENQRKQRENEEKErlenerr 201
Cdd:COG2268 217 AQAN-----------REAEEAELEQEREIETARiaEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE------- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 202 lidaerereenerrlqeAEEQREREESERRIVVAERQREQAEAEKERAEQQRilaeaeaaqaerrlfdAEIQRERDQADE 281
Cdd:COG2268 279 -----------------VQRQLEIAEREREIELQEKEAEREEAELEADVRKP----------------AEAEKQAAEAEA 325
|
250 260 270
....*....|....*....|....*....|....*..
gi 320545984 282 EGQA-------LRDAEIVERLLAAERELSPSATESEL 311
Cdd:COG2268 326 EAEAeairakgLAEAEGKRALAEAWNKLGDAAILLML 362
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-394 |
7.42e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 49 DAAADAEELPRMRERlDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEA 128
Cdd:PTZ00121 1326 EAKKKADAAKKKAEE-AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 129 KLVEERLRVQREKEESEEQQRKlveAERQREREQAEKELQEQREAERRQLEAEEnqrKQRENEEKERLENERRLIDAERE 208
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKAEEAKKKAEEAKKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 209 REENERRLQEAEEQREREESerrivvAERQREQAEaEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQA--- 285
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKK------ADEAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdel 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 286 -----LRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEE---------NARRFLEAEEE 351
Cdd:PTZ00121 1552 kkaeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeakiKAEELKKAEEE 1631
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 320545984 352 MVMLQQRQLQASHSKEEADEYAGMEpvvEELCVKKVAPPRFQE 394
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAE---EENKIKAAEEAKKAE 1671
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-370 |
8.78e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 107 AELARQ-QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKlVEAERQREREQAEKELQEQREAErrQLEAEENQR 185
Cdd:PTZ00121 1583 AEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAE--ELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 186 KQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESErrivvAERQREQAEAEKERAEQQRilaeaeAAQAER 265
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELK------KAEEEN 1728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 266 RLFDAEIQRERDQADEEGQALR-DAEIVERLLAAERELSPSATESELEEDAAIAEQ-SRRLISSRTDLEQKQRMIEENAR 343
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFDNFA 1808
|
250 260
....*....|....*....|....*....
gi 320545984 344 RFLEAEEE--MVMLQQRQLQASHSKEEAD 370
Cdd:PTZ00121 1809 NIIEGGKEgnLVINDSKEMEDSAIKEVAD 1837
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-348 |
1.70e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 49 DAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADT--RRQLAEA 126
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTllGRTLVAA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 127 EAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAE 206
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 207 REREEnerrlqeaeeqrereeserrivvAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQAL 286
Cdd:COG1196 711 EAEEE-----------------------RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 287 RDAEIVERL-------LAAERELspsatESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENAR-RFLEA 348
Cdd:COG1196 768 ELERLEREIealgpvnLLAIEEY-----EELEERYDFLSEQREDLEEARETLEEAIEEIDRETReRFLET 832
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-689 |
3.13e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 105 LAAELARQQQIEADTRR---QLAEAEAKLVEERLRVQREKEESEEQQRKlveAERQREREQAEKELQE-QREAERRQLEA 180
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARkadELKKAEEKKKADEAKKAEEKKKADEAKKK---AEEAKKADEAKKKAEEaKKKADAAKKKA 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 181 EENQR--------------------KQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQRE 240
Cdd:PTZ00121 1339 EEAKKaaeaakaeaeaaadeaeaaeEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 241 QAEAEKERAEQQRILAEAEAAQAERRLFD-----AEIQRERDQADEEGQALRDAEIVERllAAERELSPSATESELEEDA 315
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADeakkkAEEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 316 AIAEQSRRLISSRTDLEQKQRmiEENARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPPRFQEP 395
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 396 PEEPMVHKVKtqfgQGSGPEDAYSAKSKTLTFPGVSDEGSSLEPKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQ 475
Cdd:PTZ00121 1575 DKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 476 EVQYTEDYlrslDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKmftslEEEELRHGDREDynpiKYT 555
Cdd:PTZ00121 1651 ELKKAEEE----NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----KAEELKKKEAEE----KKK 1717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 556 SEPTLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEeeiELERPSRGEDV 635
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRM 1794
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 320545984 636 EEEATNEPKSSSFEEATEAQNEqavAALKQQLSKEQLDKEAEkdnpQAVDTSDS 689
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKE---GNLVINDSKEMEDSAIK----EVADSKNM 1841
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-369 |
3.49e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 155 ERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREReeserrivv 234
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 235 AERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpsateselEED 314
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLN 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 320545984 315 AAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEA 369
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-306 |
5.49e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLveAERQREREQAEKELQEQREAERRQLEA 180
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 181 eeNQRKQRENEEKERLENE------RRLI----------DAEREREENERRLQEAEEQREREESERRIVVAERQREQAEA 244
Cdd:COG4942 113 --LYRLGRQPPLALLLSPEdfldavRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320545984 245 EKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALrdaeivERLLAAERELSPSA 306
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL------EAEAAAAAERTPAA 246
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
109-201 |
5.53e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 109 LARQQQIEADTRRQLaEAEAKLveERLRVQREKEESEEQQRKlveAERQREREQAEKELQEQREAERRQLEAEENQRKQR 188
Cdd:pfam02029 230 LSQSQEREEEAEVFL-EAEQKL--EELRRRRQEKESEEFEKL---RQKQQEAELELEELKKKREERRKLLEEEEQRRKQE 303
|
90
....*....|...
gi 320545984 189 ENEEKERLENERR 201
Cdd:pfam02029 304 EAERKLREEEEKR 316
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-721 |
5.92e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQIEADTRRQlaeAEAKLVEERLRVQREKEESEEQQRklVEAERQREREQAEKELQEQREAERRQ 177
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKA---EDAKKAEAVKKAEEAKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 178 LEAEENQRKQRENEEKErlenERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAE 257
Cdd:PTZ00121 1271 AIKAEEARKADELKKAE----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 258 AEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRM 337
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 338 IEE--NARRFLEAEEEMVMLQQRQLQASHSK--EEADEYAGMEPVVEELCVKKVAPPRFQEPPEEPMVHKVKTQFGQGSG 413
Cdd:PTZ00121 1427 AEEkkKADEAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 414 PEDAYSAKSKTLTFPGVSDEGSSLEPKTPFSIQQSSFSTQPSDEGNRIE----------SERPEPEGEDQIQEVQYTEDy 483
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEelkkaeekkkAEEAKKAEEDKNMALRKAEE- 1585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 484 LRSLDGIKNRPLMR---EDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSLEEEELRHGDR----EDYNPIKYTS 556
Cdd:PTZ00121 1586 AKKAEEARIEEVMKlyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaEEENKIKAAE 1665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 557 EP---------TLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPWGEVvpEHYKDTEFWKREKALSIDEEEIELE 627
Cdd:PTZ00121 1666 EAkkaeedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA--EELKKAEEENKIKAEEAKKEAEEDK 1743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 628 RPSRGEDVEEEATNEPKSSSFEEATEAQNeqaVAALKQQLSKEQLDKEAEKDNPQAVDTSDSNKSNLQTSIaaeEQSRGG 707
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII---EGGKEG 1817
|
650
....*....|....
gi 320545984 708 SPGLRRSPRMDEME 721
Cdd:PTZ00121 1818 NLVINDSKEMEDSA 1831
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-336 |
7.59e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 105 LAAELARQQQIEADTRRQLAEAEAKL--VEERLRVQREKEESEEQQRKLVE---AERQREREQAEKELQEQrEAERRQLE 179
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIaeLEKELAALKKEEKALLKQLAALErriAALARRIRALEQELAAL-EAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 180 AEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 260 AAQAerrlfdAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQR 336
Cdd:COG4942 170 EAER------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
103-375 |
8.47e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.31 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 103 QALAAELARQQQIEADTRRQLAEAEAKLveerlrvQREKEESEEQQRKlvEAERQREREQAEKELQEQREAERRQLEAEE 182
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKL-------EQQAEEAEKQRAA--EQARQKELEQRAAAEKAAKQAEQAAKQAEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 183 NQRKQRENEEKERLENerrlidaerereenerrlqeaeeqrereeserrivvaeRQREQAEAEKERAEQQRilaeAEAAQ 262
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEA--------------------------------------KAKAEAEAERKAKEEAA----KQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 263 AERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENA 342
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAEL 234
|
250 260 270
....*....|....*....|....*....|...
gi 320545984 343 RRFLEAEEEMVMLQQRQLQASHSKEEADEYAGM 375
Cdd:TIGR02794 235 GDIFGLASGSNAEKQGGARGAAAGSEVDKYAAI 267
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-705 |
1.28e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 94 RVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVE-ERLRVQREKEESE--EQQRKLVEAER---QREREQAEKEL 167
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARkaEEARKAEDAKRveiARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 168 QEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAE-AEK 246
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 247 ERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEegqaLRDAEIVERllaaERELSPSATESELEEDAAIAEQSRRLIS 326
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE----LKKAEEKKK----ADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 327 SRTDLEQKQRMIE------ENARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPprfQEPPEEPM 400
Cdd:PTZ00121 1320 AKKKAEEAKKKADaakkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEA 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 401 VHKVKTQFGQGSGPEDAYSAKSKTLTFPGVSDEGSSLE--PKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQEVQ 478
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 479 YTEDYLRSLDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSLEEEELRHGDREDYNPIKYTSEP 558
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 559 TLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPwgEVVPEHYKDTEFWKREKALSIDEEEIELERPSRGEdvEEE 638
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE--EEK 1632
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320545984 639 ATNEPKSSSFEEATEAQNEQAVAALKQQLSKEQLDKEAEKDNPQAVDT----SDSNKSNLQTSIAAEEQSR 705
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKEAEEAKK 1703
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
111-202 |
1.79e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.65 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 111 RQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQA-EKELQEQREAERRQLEAEENQRKQRE 189
Cdd:pfam05672 33 ERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAeEREQREQEEQERLQKQKEEAEAKARE 112
|
90
....*....|...
gi 320545984 190 NEEKERLENERRL 202
Cdd:pfam05672 113 EAERQRQEREKIM 125
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-371 |
2.60e-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: 52.75 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 62 ERLDKQIKEAAEREALAGtnvmqdgvlyvngIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREK 141
Cdd:TIGR02168 680 EELEEKIEELEEKIAELE-------------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 142 EESEEQQRKLVEAERQRE-----REQAEKELQEQrEAERRQLEAEENQRKQRENEEKERLE------------------- 197
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEeleerLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREALDelraeltllneeaanlrer 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 198 ---NERRLIDAEREREENERRL-----QEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFD 269
Cdd:TIGR02168 826 lesLERRIAATERRLEDLEEQIeelseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 270 AEiqRERDQADEEGQALRD--AEIVERLLAAEREL----SPSATESELEEDAAIAEQSRRLiSSRTDLEQKQRMIEENAR 343
Cdd:TIGR02168 906 LE--SKRSELRRELEELREklAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKIE-DDEEEARRRLKRLENKIK 982
|
330 340 350
....*....|....*....|....*....|..
gi 320545984 344 RF----LEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:TIGR02168 983 ELgpvnLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-348 |
2.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 109 LARQQQIEADTRRQLAEAEAKLVEerlrVQREKEESEEQQRKLveaerqrerEQAEKELQEQREAERRQLEAEENQRKQR 188
Cdd:COG4913 598 IRSRYVLGFDNRAKLAALEAELAE----LEEELAEAEERLEAL---------EAELDALQERREALQRLAEYSWDEIDVA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 189 ENEEK-ERLENERRLIDAerereenerrlqeaeeqrereeSERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRL 267
Cdd:COG4913 665 SAEREiAELEAELERLDA----------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 268 fdAEIQRERDQA-DEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLissRTDLEQKQRMIEENARRFL 346
Cdd:COG4913 723 --EQAEEELDELqDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELERAMRAFN 797
|
..
gi 320545984 347 EA 348
Cdd:COG4913 798 RE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-308 |
3.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 178 LEAEENQRKQRENEEKERLENERRLIDAerereenERRLQEAEEQREReeserrivVAERQREQAEAEKERAEQQRILAE 257
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEAL-------LAALGLPLPASAE--------EFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 258 AEAAQAERRLFDAeiQRERDQADEEGQALR------DAEIVERLLAAERELSPSATE 308
Cdd:COG4913 405 EALAEAEAALRDL--RRELRELEAEIASLErrksniPARLLALRDALAEALGLDEAE 459
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
48-197 |
3.87e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 48 VDAAADAEELPRMRerldKQIKEAAEREALAGTNVMQDgvlyvngirvdpAGDKRQALAAELARQQQIEadtRRQLAEAE 127
Cdd:TIGR02794 43 VDPGAVAQQANRIQ----QQKKPAAKKEQERQKKLEQQ------------AEEAEKQRAAEQARQKELE---QRAAAEKA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320545984 128 AKLVEERLRVQREKEESEEQQRKLVEAERQ------REREQAEkELQEQREAERRQLEAEENQRKQRENEEKERLE 197
Cdd:TIGR02794 104 AKQAEQAAKQAEEKQKQAEEAKAKQAAEAKakaeaeAERKAKE-EAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-355 |
6.28e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 47 SVDAAADAEELPRMRERLDKQIKEaaerealagtnvmqdgvlyvngirvdpagdkRQALAAELARQQQIEADTRRQLAEA 126
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRE-------------------------------LSSLQSELRRIENRLDELSQELSDA 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 127 EAKLVEERLRVQREKEESEEQQRKLVEAER-----QREREQAEKELQE------QREAERRQLEAEENQRKQRENE---- 191
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsslEQEIENVKSELKElearieELEEDLHKLEEALNDLEARLSHsrip 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 192 ---------EKERLENERRLIDAERE---REENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:TIGR02169 795 eiqaelsklEEEVSRIEARLREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 260 AAQAERRLFDAEIQRERDQADEEGQALRDAE-------IVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLE 332
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIeeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
330 340
....*....|....*....|...
gi 320545984 333 QKQRMIEENARRfLEAEEEMVML 355
Cdd:TIGR02169 955 DVQAELQRVEEE-IRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-276 |
6.79e-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: 51.60 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 62 ERLDKQIKEAAEREALAGTNVMQDGVlyvngiRVDPAGDKRQALAAELARQQQieadtrrQLAEAEAKLVEERLRVQREK 141
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEA------QLEELESKLDELAEELAELEE-------KLEELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 142 EESEEQQRKLVEAERQREREQAE-KELQEQREAERRQLEAEENQrKQRENEEKERLENERR-LIDAEREREENERRLQEA 219
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEeLLKKLEEAELKELQAELE 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 220 EEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRER 276
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-289 |
8.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQ--IEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAER 175
Cdd:COG4913 608 NRAKLAALEAELAELEEelAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 176 RQLEAEENQRKQRENEEKERLEnerRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRIl 255
Cdd:COG4913 688 AALEEQLEELEAELEELEEELD---ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV- 763
|
170 180 190
....*....|....*....|....*....|....
gi 320545984 256 aeaeaAQAERRLFDAEIQRERDQADEEGQALRDA 289
Cdd:COG4913 764 -----ERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-362 |
9.03e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 120 RRQLAEAEAKLVE-----ERLRVQREK-EESEEQQRKLVEAE----------RQREREQAEKELQEQrEAERRQLEAEEN 183
Cdd:TIGR02169 183 EENIERLDLIIDEkrqqlERLRREREKaERYQALLKEKREYEgyellkekeaLERQKEAIERQLASL-EEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 184 QRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQA 263
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 264 ERRLfdAEIQRERDQADEEGQALRDaeiVERLLAAERElspsateselEEDAAIAEQSRRLISSRTDLEQKQRMIEENAR 343
Cdd:TIGR02169 342 EREI--EEERKRRDKLTEEYAELKE---ELEDLRAELE----------EVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250
....*....|....*....
gi 320545984 344 RFLEAEEEMVMLQQRQLQA 362
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADL 425
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
101-372 |
9.94e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQ---QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:pfam13868 70 ERKRYRQELEEQieeREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 178 LEAEENQR----KQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQR 253
Cdd:pfam13868 150 EREEDERIleylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 254 ilaeaeaaqaeRRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSAtesELEEDAAIAEQSRRLISSRTDLEQ 333
Cdd:pfam13868 230 -----------KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA---EDEEIEQEEAEKRRMKRLEHRREL 295
|
250 260 270
....*....|....*....|....*....|....*....
gi 320545984 334 KQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADEY 372
Cdd:pfam13868 296 EKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
60-351 |
1.28e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 60 MRERLDKQIKEAAEREALAGTNVMQDGvlyvNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQR 139
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEE----EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 140 EKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEA 219
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 220 EEQREREESERRIVVAERQREQAEAEKERA---EQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLL 296
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLleeKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 320545984 297 AAERELSPSATESELEEdaAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEE 351
Cdd:pfam02463 962 NKRLLLAKEELGKVNLM--AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
102-362 |
1.28e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 102 RQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESE---EQQRKLVEAERQREREQAEKELQEQREAERRQL 178
Cdd:pfam13868 54 ERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 179 EAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQrEQAEAEKERAEQQRILAEA 258
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ-EKAQDEKAERDELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 259 EAAQAERRLFDAEIQRERDQADEEGQALRDAEIV--ERLLAAEREL------SPSATESELEEDAAIAEQSRRLISSRTD 330
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELQQAREEQIElkERRLAEEAEReeeefeRMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270
....*....|....*....|....*....|..
gi 320545984 331 LEQkQRMIEENARRFLEAEEEMVMLQQRQLQA 362
Cdd:pfam13868 293 REL-EKQIEEREEQRAAEREEELEEGERLREE 323
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-253 |
1.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQALAAELaRQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLE 179
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 180 AEENQRKQREN--EEKERLENE----RRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQR 253
Cdd:COG4717 150 ELEERLEELREleEELEELEAElaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
112-376 |
1.71e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 112 QQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQA------EKELQEQREAERRQLEAEENQR 185
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqieEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 186 KQRENEEKERLENERRLIDAEREREENERRLQEAeeqrereeserrivvaeRQREQAEAEKERAEQQRILAEAEAAQAER 265
Cdd:pfam13868 106 IVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ-----------------AEWKELEKEEEREEDERILEYLKEKAERE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 266 RLFDAEIQRERDQADEEGQALRDAEIVERLLAAERElspsatesELEEDAAIAEQSRrlissrtdlEQKQRMIEENARRf 345
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD--------ELRAKLYQEEQER---------KERQKEREEAEKK- 230
|
250 260 270
....*....|....*....|....*....|.
gi 320545984 346 leAEEEMVMLQQRQLQASHSKEEADEYAGME 376
Cdd:pfam13868 231 --ARQRQELQQAREEQIELKERRLAEEAERE 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-359 |
2.84e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQALAAELA-RQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLV--EAERQREREQAEKELQEQREAERR 176
Cdd:TIGR02169 254 EKLTEEISELEkRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLErsIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 177 QLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESErrivVAERQREQAEAEKERAEQQRILA 256
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE----LKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 257 EAEAaqaerRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELspSATESELEEDAAIAEQ-SRRLISSRTDLEQKQ 335
Cdd:TIGR02169 410 RLQE-----ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKyEQELYDLKEEYDRVE 482
|
250 260
....*....|....*....|....
gi 320545984 336 RMIEENARRFLEAEEEMVMLQQRQ 359
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
100-291 |
2.91e-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: 49.18 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQALAAELARQQQIEADTRRQLAEaeaklveERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLE 179
Cdd:pfam15709 333 ASRDRLRAERAEMRRLEVERKRREQE-------EQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 180 AEENQRKQR--ENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRilae 257
Cdd:pfam15709 406 EERKQRLQLqaAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR---- 481
|
170 180 190
....*....|....*....|....*....|....
gi 320545984 258 AEAAQAERRLFDAEiqrERDQADEEGQALRDAEI 291
Cdd:pfam15709 482 QKQEAEEKARLEAE---ERRQKEEEAARLALEEA 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-371 |
3.26e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 134 RLRVQREKEESEEQQRKLVEAERQREREQAE-KELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIdAEREREEN 212
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAElRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 213 ERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQrILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIV 292
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 293 ERLLAAERELSPSATES--ELEEDAAIAEQSRRliSSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEAD 370
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQieELSEDIESLAAEIE--ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
.
gi 320545984 371 E 371
Cdd:TIGR02168 908 S 908
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
133-201 |
4.13e-05 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 47.95 E-value: 4.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 133 ERLRVQREKEESEEqqRKLVEAERQRER-EQAEKELQEQREAERRQLEAEEnQRKQrenEEKERLENERR 201
Cdd:pfam07946 260 KKAKKTREEEIEKI--KKAAEEERAEEAqEKKEEAKKKEREEKLAKLSPEE-QRKY---EEKERKKEQRK 323
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-205 |
6.30e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 40 FQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADT 119
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 120 RRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEEnQRKQRENEEKERLENE 199
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL-PEPPDLEELERELERL 772
|
....*.
gi 320545984 200 RRLIDA 205
Cdd:COG1196 773 EREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-371 |
7.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 118 DTRRQLAEAEAKLVeerlRVQREKEESEEQQRKLveaERQREREQAEKELQEQREAERRQLEAeenQRKQRENEEKERLE 197
Cdd:TIGR02168 176 ETERKLERTRENLD----RLEDILNELERQLKSL---ERQAEKAERYKELKAELRELELALLV---LRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 198 NErrLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAE-----AEKERAEQQRILAEAEAAQAERRLFDAEI 272
Cdd:TIGR02168 246 EE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 273 QRERDQADEEGQALRDAEIVERL------LAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFL 346
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLeelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260
....*....|....*....|....*
gi 320545984 347 EAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLK 428
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
110-255 |
7.21e-05 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 45.04 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 110 ARQQQIEADTRRQLAEAEAKLVEERLrvQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEA-EENQRKQR 188
Cdd:pfam15346 3 AESKLLEEETARRVEEAVAKRVEEEL--EKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRkEEEERKKR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 189 ENEEKERLENERRLIDAEREREENERRLQEAEEQREReeserrivvAERQREQAEAEKERAEQQRIL 255
Cdd:pfam15346 81 EELERILEENNRKIEEAQRKEAEERLAMLEEQRRMKE---------ERQRREKEEEEREKREQQKIL 138
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
103-201 |
7.45e-05 |
|
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: 46.80 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 103 QALAAELARQQQIEAD-TRRQLAEAEAKLVEERLRVQREK----EESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:cd16269 188 QADQALTEKEKEIEAErAKAEAAEQERKLLEEQQRELEQKledqERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|....
gi 320545984 178 LEAEENQRKQRENEEKERLENERR 201
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-382 |
8.21e-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: 48.04 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 108 ELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRERE--QAEKELQEQREAE---RRQLEA-E 181
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKElkHLREALQQTQQSHaylTQKREAqE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 182 ENQRKQRENEEKERLENERRLIDAEREREENERRLQ-------EAEEQREREESERRIVVAERQREQAEAEKERAEQQRI 254
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 255 LAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELspsateSELEEDAAIAEQSRRLISSRTDL--- 331
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI------HTLQQQKTTLTQKLQSLCKELDIlqr 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 332 EQKQRMIEENARRFLE-----AEEEMVMLQQR-QLQASHSKEEADEYAGMEPVVEEL 382
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQgqlahAKKQQELQQRYaELCAAAITCTAQCEKLEKIHLQES 464
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
45-369 |
9.20e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 45 DSSVDAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLA 124
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 125 EAE-AKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLI 203
Cdd:pfam02463 263 EEEkLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 204 dAEREREENERRLQEAEEQREREESerrivvAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEG 283
Cdd:pfam02463 343 -ELKELEIKREAEEEEEEELEKLQE------KLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 284 QALrdaEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQAS 363
Cdd:pfam02463 416 QLE---DLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
....*.
gi 320545984 364 HSKEEA 369
Cdd:pfam02463 493 QKLEER 498
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
100-181 |
9.51e-05 |
|
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: 44.78 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQAL------AAELARQ--QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQR 171
Cdd:COG0711 30 DERQEKiadglaEAERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQER 109
|
90
....*....|
gi 320545984 172 EAERRQLEAE 181
Cdd:COG0711 110 AKALAELRAE 119
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
133-200 |
1.00e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 47.81 E-value: 1.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320545984 133 ERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENER 200
Cdd:PTZ00266 436 ERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERERLERERLERDRLERDR 503
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
124-204 |
1.41e-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: 46.03 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 124 AEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENE-RRL 202
Cdd:cd16269 181 AEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqERA 260
|
..
gi 320545984 203 ID 204
Cdd:cd16269 261 LE 262
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
110-201 |
1.53e-04 |
|
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: 44.01 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 110 ARQQQIEADtrrqLAEAEaklvEERLRVQREKEESEEQQRKLvEAERQREREQAEKELQEQREAERRQLEAEENQRKQre 189
Cdd:COG0711 31 ERQEKIADG----LAEAE----RAKEEAEAALAEYEEKLAEA-RAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIA-- 99
|
90
....*....|..
gi 320545984 190 nEEKERLENERR 201
Cdd:COG0711 100 -QAEAEIEQERA 110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-371 |
1.72e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 154 AERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLqeaeeqrereeserriv 233
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 234 vAERQREQAEAEKERAEQQRILaeaeaaqaERRLFDAEIQRERD------QADEEGQALRDAEIVERLLAAERELspsat 307
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEEL--------AELLRALYRLGRQPplalllSPEDFLDAVRRLQYLKYLAPARREQ----- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320545984 308 ESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEmvmlQQRQLQASHSKEEADE 371
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAEL 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
98-277 |
1.78e-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: 46.66 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQrerEQAEKELQEQREAERRQ 177
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 178 LEAEENQRKQRENEEKERLENERRLidaEREREENERRLQEAEEQREREESERRIVVAERQREQAEAE----KERAEQQR 253
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKEL---EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErrkqQEMEERRR 553
|
170 180
....*....|....*....|....
gi 320545984 254 ILAEAEAAQAERRLFDAeIQRERD 277
Cdd:pfam17380 554 IQEQMRKATEERSRLEA-MERERE 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-691 |
1.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 94 RVDPAGDKRQALAAELARQQQieaDTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRE---REQAEKELQEQ 170
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAE---DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEearKAEDAKKAEAV 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 171 REAERRQLEAEENQR--KQRENEEKERLENERRL--------IDAEREREENERRLQEAEEQREREESERRIVVAERQRE 240
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKaeEERNNEEIRKFEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 241 QAEaEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQA--DEEGQALRDAEIVERLLAAErELSPSATESELEEDAAIA 318
Cdd:PTZ00121 1310 KAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAakAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKA 1387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 319 EQSRRLISSRTDLEQKQRMIEENARRFLEAE--EEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPPRFQEPP 396
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 397 EEPMVHKVKTQFGQGSGPEDaysAKSKTLTFPGVSDEG-SSLEPKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEdQIQ 475
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADE---AKKKAEEAKKKADEAkKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 476 EVQYTEDyLRSLDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSLEE----EELRHGDREdynp 551
Cdd:PTZ00121 1544 EKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEA---- 1618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 552 iKYTSEptlRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEEEIELERPSR 631
Cdd:PTZ00121 1619 -KIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320545984 632 GEDVEEEATNEPKSSSFEEATEAQNEQAVAALKQQLSKEQLDKEAEKDNPQA----VDTSDSNK 691
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeakKDEEEKKK 1758
|
|
| 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 ... |
99-181 |
2.04e-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: 43.46 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 99 GDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKL-----VEAERQRER--EQAEKELQEQR 171
Cdd:pfam00430 29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLkeeivAAAEAEAERiiEQAAAEIEQEK 108
|
90
....*....|
gi 320545984 172 EAERRQLEAE 181
Cdd:pfam00430 109 DRALAELRQQ 118
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
100-383 |
2.15e-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: 46.50 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAerQREREQAEKELQEQREAERRQLE 179
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--QLKKQQLLKQLRARIEELRAQEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 180 AEENQRKQRENEEKER--LENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQ---------------- 241
Cdd:TIGR00618 278 VLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEeqrrllqtlhsqeihi 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 242 -----------AEAEKERAEQQRILAEAEAAQAERRLFDA------EIQRERDQADEEGQALRDAEIveRLLAAERELSP 304
Cdd:TIGR00618 358 rdahevatsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSlckeldILQREQATIDTRTSAFRDLQG--QLAHAKKQQEL 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320545984 305 SATESELEEdAAIAEQSRRLISSRTDLEQKQRMIEEnaRRFLEAEEEMVMLQQRQLQASHSKeEADEYAGMEPVVEELC 383
Cdd:TIGR00618 436 QQRYAELCA-AAITCTAQCEKLEKIHLQESAQSLKE--REQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSC 510
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
92-201 |
3.25e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 45.88 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 92 GIRVDPAGDKRQALAAELARQQQIEadtrrqLAEAEAKLVEERLRVQREKEESEEQQRklveAERQR-EREQAEKELQEQ 170
Cdd:PTZ00266 427 GGRVDKDHAERARIEKENAHRKALE------MKILEKKRIERLEREERERLERERMER----IERERlERERLERERLER 496
|
90 100 110
....*....|....*....|....*....|.
gi 320545984 171 REAERRQLEAEENQRKQREneEKERLENERR 201
Cdd:PTZ00266 497 DRLERDRLDRLERERVDRL--ERDRLEKARR 525
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
110-201 |
3.47e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 110 ARQQQIEA--DTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEA--ERQREREQAEKELQE--QREAERRQLEAE-E 182
Cdd:PRK11637 167 ARQETIAElkQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQArnERKKTLTGLESSLQKdqQQLSELRANESRlR 246
|
90
....*....|....*....
gi 320545984 183 NQRKQRENEEKERLENERR 201
Cdd:PRK11637 247 DSIARAEREAKARAEREAR 265
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
100-181 |
4.31e-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: 42.42 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 100 DKRQAL------AAELARQ--QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQR 171
Cdd:cd06503 29 DEREEKiaesleEAEKAKEeaEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEK 108
|
90
....*....|
gi 320545984 172 EAERRQLEAE 181
Cdd:cd06503 109 EKALAELRKE 118
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
116-181 |
4.40e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 42.68 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 116 EADTRRQLAEAEA-------KLVEERLRVQREKEESEEQQRKL-------VEAERQREREQAEKELQEQREAERRQLEAE 181
Cdd:PRK07353 45 RAEAKERLAEAEKleaqyeqQLASARKQAQAVIAEAEAEADKLaaealaeAQAEAQASKEKARREIEQQKQAALAQLEQQ 124
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
112-205 |
4.59e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 112 QQQIEADTRRQLAEaeaklvEERLRVQREKEESEEQQRKLvEAERQREREQAEKELQEQREAERRqlEAEENQRKQRENE 191
Cdd:PRK00409 527 ELERELEQKAEEAE------ALLKEAEKLKEELEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKK--EADEIIKELRQLQ 597
|
90
....*....|....*
gi 320545984 192 EKERLE-NERRLIDA 205
Cdd:PRK00409 598 KGGYASvKAHELIEA 612
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-297 |
5.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 97 PAGDKRQALAAELARQQQieadTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREaERR 176
Cdd:COG4717 61 PQGRKPELNLKELKELEE----ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 177 QLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESerriVVAERQREQAEAEKERAEQQRILA 256
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS----LATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 320545984 257 EAEAAQAERRLfdAEIQRERDQADEEGQALRDAEIVERLLA 297
Cdd:COG4717 212 EEELEEAQEEL--EELEEELEQLENELEAAALEERLKEARL 250
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
106-351 |
5.64e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 106 AAELARQQQIEADTRRqlAEAEAKLVEERLRVQREKEESEEQQRKLvEAERQREREQAEKELqEQREAERRQ-LEAEENQ 184
Cdd:NF041483 74 AEQLLRNAQIQADQLR--ADAERELRDARAQTQRILQEHAEHQARL-QAELHTEAVQRRQQL-DQELAERRQtVESHVNE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 185 RKQRENEEKERLENE-RRLIDAEREreenerrlQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILaEAEAAQA 263
Cdd:NF041483 150 NVAWAEQLRARTESQaRRLLDESRA--------EAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAIL-RRARKDA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 264 ERRLFDAEIQ----------------RERDQADEEGQAL-RDAEivERLLAAERELSPSATESELEEDAAIAEQSRRLIS 326
Cdd:NF041483 221 ERLLNAASTQaqeatdhaeqlrsstaAESDQARRQAAELsRAAE--QRMQEAEEALREARAEAEKVVAEAKEAAAKQLAS 298
|
250 260
....*....|....*....|....*.
gi 320545984 327 SRTDLEQKQRMI-EENARRFLEAEEE 351
Cdd:NF041483 299 AESANEQRTRTAkEEIARLVGEATKE 324
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
120-376 |
6.13e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 120 RRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAErrqLEAEENQRKQRENEEKERLENE 199
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA---LEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 200 RRLIdaerereenerrlqeaeeqrereeseRRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQA 279
Cdd:pfam02463 232 LKLN--------------------------EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 280 DEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQ 359
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
250
....*....|....*..
gi 320545984 360 LQASHSKEEADEYAGME 376
Cdd:pfam02463 366 EKLEQLEEELLAKKKLE 382
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
120-199 |
1.05e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 44.26 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 120 RRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQReREQAEKELQEQ------REAERRQLEAEENQ-------RK 186
Cdd:PRK10811 643 RRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQR-RRNDEKRQAQQeakalnVEEQSVQETEQEERvqqvqprRK 721
|
90
....*....|...
gi 320545984 187 QRENEEKERLENE 199
Cdd:PRK10811 722 QRQLNQKVRIEQS 734
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
25-344 |
1.09e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 25 ALEFAFVARHLYHWTFQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALA---GTNVMQDGVLYVNGIRVDPAGDK 101
Cdd:COG3899 767 LLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAerlGDRRLEARALFNLGFILHWLGPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 102 RQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAE 181
Cdd:COG3899 847 REALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAA 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 182 ENQRkQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAA 261
Cdd:COG3899 927 AAAA-LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAA 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 262 QAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEEN 341
Cdd:COG3899 1006 AAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAA 1085
|
...
gi 320545984 342 ARR 344
Cdd:COG3899 1086 AAL 1088
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-678 |
1.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 94 RVDPAGDKRQALA-AELAR--QQQIEADTRRQLAEAEAKLVEERLRVQREKEESE--EQQRKLVEAERQREREQAE--KE 166
Cdd:PTZ00121 1110 KAEEARKAEEAKKkAEDARkaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARkaEEARKAEDAKKAEAARKAEevRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 167 LQEQREAER-RQLEAEENQRKQRENEEKERLENERRLIDAERERE-----------ENERRLQEAEEQREREESERRIVV 234
Cdd:PTZ00121 1190 AEELRKAEDaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdaeeakkaEEERNNEEIRKFEEARMAHFARRQ 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 235 AERQREQAEAEKE--RAEQQRILAEAEAAQAERRLFDAEIQ-RERDQADEEGQALRDAEIVERLLAAERELSPSATESEL 311
Cdd:PTZ00121 1270 AAIKAEEARKADElkKAEEKKKADEAKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 312 EEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADEY--AGMEPVVEELCVKKVAP 389
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 390 PRFQEPPEEPMVHKVKTQFGQGSGPE--DAYSAKSKTLTFPGVSDEGSSLEP--KTPFSIQQSSFSTQPSDEGNRIESER 465
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 466 PEPEGEDQIQEVQYTEDYLRSLDGIKNRPLMREDGSGRRRAFKKRRS-SGSSNSSRESRASRDEELKMFTSLEEEELRHG 544
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 545 DREDYNPIKYTSEPTLRVKSHRRHKrspAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEEEI 624
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 320545984 625 ELERPSRGEDVEEEATNEPKSSSFEEATEAQNEQAVAALKQQLSKEQLDKEAEK 678
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-250 |
1.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 103 QALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQ-REREQAEKELQEQ-------REAE 174
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQlgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320545984 175 RRQLEaEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAE 250
Cdd:COG1579 93 ALQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
101-202 |
1.70e-03 |
|
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: 41.18 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEqrEAERRQLEA 180
Cdd:pfam05672 44 RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKARE--EAERQRQER 121
|
90 100
....*....|....*....|..
gi 320545984 181 EenqrKQRENEEKERLENERRL 202
Cdd:pfam05672 122 E----KIMQQEEQERLERKKRI 139
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
109-359 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 109 LARQQQIEADTRRQLAEAEAKLveERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLeaeenqRKQR 188
Cdd:pfam15709 324 LLEKREQEKASRDRLRAERAEM--RRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL------RKQR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 189 ENEEKERL-ENERrlidaerereenerrlqeaeeqrereeserrivvaeRQREQAEAEKERAEQQRilaeaeaAQAERRL 267
Cdd:pfam15709 396 LEEERQRQeEEER------------------------------------KQRLQLQAAQERARQQQ-------EEFRRKL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 268 FDAEIQRERDQADE-EGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRlisSRTDLEQKQRMIEENARRFL 346
Cdd:pfam15709 433 QELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK---ARLEAEERRQKEEEAARLAL 509
|
250
....*....|...
gi 320545984 347 EAEEEMVMLQQRQ 359
Cdd:pfam15709 510 EEAMKQAQEQARQ 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
108-349 |
1.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 108 ELARQQQIEADTRRQLAEAeAKLV---------EERLRVQREKEESEEQQRKLVEAERQREREQAEKE--LQEQREAERR 176
Cdd:PRK04863 460 SLEQKLSVAQAAHSQFEQA-YQLVrkiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEqrLRQQQRAERL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 177 QLEAEENQRKQRENEEK-ERLENERrlidaerereenerrlqeaeeqrereeserrivvaERQREQAEAEKERAEQQRIl 255
Cdd:PRK04863 539 LAEFCKRLGKNLDDEDElEQLQEEL-----------------------------------EARLESLSESVSEARERRM- 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 256 aeaeAAQAERRLFDAEIQRERDQAdEEGQALRDAeiVERLlaaeRELSPSATESELEEDAAI---AEQSRRLISSRTDLE 332
Cdd:PRK04863 583 ----ALRQQLEQLQARIQRLAARA-PAWLAAQDA--LARL----REQSGEEFEDSQDVTEYMqqlLERERELTVERDELA 651
|
250
....*....|....*..
gi 320545984 333 QKQRMIEENARRFLEAE 349
Cdd:PRK04863 652 ARKQALDEEIERLSQPG 668
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-253 |
1.89e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 50 AAADAEELPRMRERLDKQIKEAaeREALAGTNVMQDGVLyvngirvdpagDKRQALAAELARQQQIEADTRRQLAEAEAK 129
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAEL--EKELAALKKEEKALL-----------KQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 130 LVEERLRVQREKEESEEQQRKLVEAERQ---------------------------------REREQAEKELQEQREAERR 176
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRAlyrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 177 QLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQR 253
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 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 ... |
118-201 |
2.08e-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: 40.37 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 118 DTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENE----EK 193
Cdd:pfam00430 29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAeieqEK 108
|
....*...
gi 320545984 194 ERLENERR 201
Cdd:pfam00430 109 DRALAELR 116
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
120-205 |
2.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 120 RRQLAEAEAKLVEERLR--VQREKEESEEQQR-KLVEA--ERQREREQAEKELQEQR----EAERRQLEAEEN-QRKQRE 189
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKeALLEAkeEIHKLRNEFEKELRERRnelqKLEKRLLQKEENlDRKLEL 104
|
90
....*....|....*..
gi 320545984 190 NEEKER-LENERRLIDA 205
Cdd:PRK12704 105 LEKREEeLEKKEKELEQ 121
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
124-253 |
2.65e-03 |
|
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: 40.41 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 124 AEAEAKLVEERLRVQREKEESEEQQRKLVE-AERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRL 202
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEeEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 320545984 203 IDAEREREENERRLQEAEEQREREEserrivvAERQREQAEAEKERAEQQR 253
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKAREE-------AERQRQEREKIMQQEEQER 132
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
40-178 |
2.77e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 40 FQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALAgtnvmqdgvlyvngirvdpagdkrQALAAELARQQQIEADT 119
Cdd:PRK11448 134 FVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALA------------------------EAQQQELVALEGLAAEL 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 320545984 120 RRQLAEAEAKLveERLRVQREKEESEEQQRklveaeRQREREQAEKELqEQREAERRQL 178
Cdd:PRK11448 190 EEKQQELEAQL--EQLQEKAAETSQERKQK------RKEITDQAAKRL-ELSEEETRIL 239
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
99-204 |
2.97e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 99 GDKRQALAAELARQQQIEAD---------------TRRQLAEA--EAKLVEERLRVQREKEESEEQQRKLVEAER-QRER 160
Cdd:pfam05262 211 DAKRAQQLKEELDKKQIDADkaqqkadfaqdnadkQRDEVRQKqqEAKNLPKPADTSSPKEDKQVAENQKREIEKaQIEI 290
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 320545984 161 EQAEKELQEQREAERRQLEAEENQRKQRenEEKERLENERRLID 204
Cdd:pfam05262 291 KKNDEEALKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREP 332
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
232-380 |
3.52e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 232 IVVAERQREQAEAEkERAEQQRILAEAEAAQAERRLFDAEIQRERDQAdeegQALRDAEIVERLLAAERELSPSATESEL 311
Cdd:COG2268 214 IAIAQANREAEEAE-LEQEREIETARIAEAEAELAKKKAEERREAETA----RAEAEAAYEIAEANAEREVQRQLEIAER 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 312 EEDAAIAEQSRrlissrtdlEQKQRMIEENARRFLEAEEEmVMLQQRQLQASHSKEEAD-EYAGMEPVVE 380
Cdd:COG2268 289 EREIELQEKEA---------EREEAELEADVRKPAEAEKQ-AAEAEAEAEAEAIRAKGLaEAEGKRALAE 348
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
119-371 |
3.70e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 119 TRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQ--REAERRQLEAEENQRKQRENEEKERL 196
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLklNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 197 ENERRLIDAEREREENERRLQEA--------EEQREREESERRIVV---AERQREQAEAEKERAEQQRILAEAEAAQAER 265
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLqeeelkllAKEEEELKSELLKLErrkVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 266 RLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELS-------PSATESELEEDAAIAEQSRRLISSRTDLEQKQRMI 338
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleserLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
|
250 260 270
....*....|....*....|....*....|...
gi 320545984 339 EENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:pfam02463 421 LKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
101-186 |
4.51e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 101 KRQALAAELARQQQIEADTRRQLAEAEaKLVEERLRVQREKEEsEEQQRKLVEAERQREREQAEKE--LQEQREAERRQL 178
Cdd:cd16269 206 KAEAAEQERKLLEEQQRELEQKLEDQE-RSYEEHLRQLKEKME-EERENLLKEQERALESKLKEQEalLEEGFKEQAELL 283
|
....*...
gi 320545984 179 EAEENQRK 186
Cdd:cd16269 284 QEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
103-375 |
4.66e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 103 QALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLveAERQREREQAEKELqEQREAERRQLEAEE 182
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL--ESLQEEAEELQEEL-EELQKERQDLEQQR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 183 NQRKQRENE-EKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAA 261
Cdd:COG4372 132 KQLEAQIAElQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 262 QAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEEN 341
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
250 260 270
....*....|....*....|....*....|....
gi 320545984 342 ARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGM 375
Cdd:COG4372 292 ALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
111-196 |
4.70e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 40.41 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 111 RQQQIEADTRRQLAEAEAKLVEERLRVQ-------REKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEEN 183
Cdd:pfam09756 8 RAKLELKEAKRQQREAEEEEREEREKLEekreeeyKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKSQFVVEEE 87
|
90
....*....|...
gi 320545984 184 QRKQRENEEKERL 196
Cdd:pfam09756 88 GTDKLSAEDESQL 100
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
99-204 |
5.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 99 GDKRQALAAELARQQ----QIEADTRRQLAEAEAKlvEErlrVQREKEESE----EQQRKLVEAERQ-REREQAEKELQE 169
Cdd:PRK12704 29 AEAKIKEAEEEAKRIleeaKKEAEAIKKEALLEAK--EE---IHKLRNEFEkelrERRNELQKLEKRlLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|....*
gi 320545984 170 QREAERRQLEAEENQRKQRENEEKERLENERRLID 204
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
110-201 |
7.65e-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: 38.57 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 110 ARQQQIEADtrrqLAEAEAKLVEerlrVQREKEESEEQQRKlVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRE 189
Cdd:cd06503 30 EREEKIAES----LEEAEKAKEE----AEELLAEYEEKLAE-ARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQA 100
|
90
....*....|..
gi 320545984 190 NEEkerLENERR 201
Cdd:cd06503 101 KAE---IEQEKE 109
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
98-193 |
9.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQRE--------KEESEEQQRKLVEAERQREREQAEKELQE 169
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGGYASVKAHELIE 611
|
90 100
....*....|....*....|....*
gi 320545984 170 QREA-ERRQLEAEENQRKQRENEEK 193
Cdd:PRK00409 612 ARKRlNKANEKKEKKKKKQKEKQEE 636
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
136-365 |
9.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 136 RVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLenerrlidaerereenerr 215
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE------------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545984 216 lqeaeeqrereeserrivvAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDA------EIQRERDQADEE-GQALRD 288
Cdd:COG4913 300 -------------------LRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleQLEREIERLERElEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320545984 289 AEIVERLLAAeRELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHS 365
Cdd:COG4913 361 RARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| |
