|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-371 |
1.90e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEA 180
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 181 EENQRKQRENEEKERLENER-RLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:COG1196 320 ELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 260 AAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELspsATESELEEDAAIAEQSRRLISSRTDLEQKQRMIE 339
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270
....*....|....*....|....*....|..
gi 21355931 340 ENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-371 |
4.10e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 101 KRQALAAELARQQQIEADTRR--------QLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRER---EQAEKELQE 169
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRlelEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 170 QREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRivVAERQREQAEAEKERA 249
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE--EAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 250 EQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpSATESELEEDAAIAEQSRRLISSRT 329
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-RLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 21355931 330 DLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-371 |
1.37e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 50 AAADAEELPRMRERLDKQIKEAAEREALAGTNVMQdgvlyvNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAK 129
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELAR------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 130 LVEERLRVQREKEESEEQQRKLVEAERQRER-EQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAERE 208
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 209 REENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRD 288
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 289 AE----------IVERLLAAERELSPS-----ATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMV 353
Cdd:COG1196 499 AEadyegflegvKAALLLAGLRGLAGAvavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
330
....*....|....*...
gi 21355931 354 MLQQRQLQASHSKEEADE 371
Cdd:COG1196 579 LDKIRARAALAAALARGA 596
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-369 |
5.84e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 109 LARQQQIEADTRRQLA--EAEAKLVEERLRVQREKEESEEQQR--KLVEAERQREREQAEkelQEQREAERRQLEAEENQ 184
Cdd:COG1196 188 LERLEDILGELERQLEplERQAEKAERYRELKEELKELEAELLllKLRELEAELEELEAE---LEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 185 RKQRENEEKERLENERRLIDAEREreenerrlQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAE 264
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA--------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 265 RRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARR 344
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260
....*....|....*....|....*
gi 21355931 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 |
2.44e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 54 AEELPRMRERLDKQiKEAAEReALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEE 133
Cdd:TIGR02168 195 LNELERQLKSLERQ-AEKAER-YKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 134 RLRVQREKEESEEQQRKLVE-AERQREREQAEKELQEQREAERRQLEA--EENQRKQRENEEKERLENERRLIDAERERE 210
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYAlANEISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 211 ENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLfdAEIQRERDQADEEGQALRDAE 290
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL--ERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355931 291 IVERLLAAERELSpsateselEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQ 359
Cdd:TIGR02168 431 EEAELKELQAELE--------ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
104-251 |
2.12e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 104 ALAAELARQQQIEADTRRQlAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEEN 183
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRA-EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355931 184 QRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQ 251
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-405 |
5.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQR--KLVEAERQREREQAEKELQEQREAER 175
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 176 RQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQ---AEAEKERAEQQ 252
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkAEEAKIKAEEL 1625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 253 RILAEAEAAQAERRLFDAEIQRERDQ--ADEEGQALRDAEIVERllAAERELSPSATESELEEDAAIAEQSRRLISSRTD 330
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355931 331 LEQKQRMIEENARRF--LEAEEEMVMLQQRQLQashSKEEADEYAGMEPVVEELCVKKVAPPRFQEPPEEPMVHKVK 405
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAeeLKKAEEENKIKAEEAK---KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
113-381 |
7.51e-08 |
|
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: 55.90 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 113 QQIEADTRRQLAEAEAKLVEERLRVQREKEESE-EQQRKLVEAERQRereQAEKELQEQREAERRQLEAEENQRKQRENE 191
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREvERRRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 192 EKERLENERRLIDAEREREENERRLQE-AEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDA 270
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 271 EIQRERDQADEEGQALRDAEI-----VERLLAAERELSPSATESELEE-DAAIAEQSRRLISSRTDLEQKQRMIEE-NAR 343
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQerqqqVERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKILEKELEERKQAMIEEeRKR 515
|
250 260 270
....*....|....*....|....*....|....*...
gi 21355931 344 RFLEAEEEMvmlQQRQLQASHSKEEADEYAGMEPVVEE 381
Cdd:pfam17380 516 KLLEKEMEE---RQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-394 |
6.59e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 49 DAAADAEELPRMRERlDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADTRRQLAEAEA 128
Cdd:PTZ00121 1326 EAKKKADAAKKKAEE-AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 129 KLVEERLRVQREKEESEEQQRKlveAERQREREQAEKELQEQREAERRQLEAEEnqrKQRENEEKERLENERRLIDAERE 208
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKAEEAKKKAEEAKKADEAKKK 1478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 209 REENERRLQEAEEQREREESerrivvAERQREQAEaEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQA--- 285
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKK------ADEAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdel 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 286 -----LRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEE---------NARRFLEAEEE 351
Cdd:PTZ00121 1552 kkaeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeeakiKAEELKKAEEE 1631
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21355931 352 MVMLQQRQLQASHSKEEADEYAGMEpvvEELCVKKVAPPRFQE 394
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAE---EENKIKAAEEAKKAE 1671
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
115-311 |
9.84e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 115 IEADTRRQLAEAeaklveerlrVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLeAEENQRKQRENEEKE 194
Cdd:COG2268 186 LDALGRRKIAEI----------IRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARI-AEAEAELAKKKAEER 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 195 RLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRilaeaeaaqaerrlfdAEIQR 274
Cdd:COG2268 255 REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKP----------------AEAEK 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21355931 275 ERDQADEEGQA-------LRDAEIVERLLAAERELSPSATESEL 311
Cdd:COG2268 319 QAAEAEAEAEAeairakgLAEAEGKRALAEAWNKLGDAAILLML 362
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
103-357 |
2.70e-06 |
|
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: 50.89 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 103 QALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEA-- 180
Cdd:pfam17380 323 KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAar 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 181 ------EENQRK----QRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIV---VAERQREQAEAEKE 247
Cdd:pfam17380 403 kvkileEERQRKiqqqKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 248 RAEQQRIlaeaeaAQAERRLFDAEIQRERdqadeegQALRDAEIVERLLaaERELSPSATESELEEDAAIAEQSRRL--- 324
Cdd:pfam17380 483 KRDRKRA------EEQRRKILEKELEERK-------QAMIEEERKRKLL--EKEMEERQKAIYEEERRREAEEERRKqqe 547
|
250 260 270
....*....|....*....|....*....|...
gi 21355931 325 ISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQ 357
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-369 |
5.94e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 155 ERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREReeserrivv 234
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ--------- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 235 AERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSpsateselEED 314
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLN 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21355931 315 AAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEA 369
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-370 |
6.26e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 107 AELARQ-QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKlVEAERQREREQAEKELQEQREAErrQLEAEENQR 185
Cdd:PTZ00121 1583 AEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAE--ELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 186 KQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESErrivvAERQREQAEAEKERAEQQRilaeaeAAQAER 265
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELK------KAEEEN 1728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 266 RLFDAEIQRERDQADEEGQALR-DAEIVERLLAAERELSPSATESELEEDAAIAEQ-SRRLISSRTDLEQKQRMIEENAR 343
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFDNFA 1808
|
250 260
....*....|....*....|....*....
gi 21355931 344 RFLEAEEE--MVMLQQRQLQASHSKEEAD 370
Cdd:PTZ00121 1809 NIIEGGKEgnLVINDSKEMEDSAIKEVAD 1837
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-308 |
1.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 178 LEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAeeqrereeserrivvAERQREQAEAEKERAEQQRILAE 257
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---------------FAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21355931 258 AEAAQAERRLFDAeiQRERDQADEEGQALR------DAEIVERLLAAERELSPSATE 308
Cdd:COG4913 405 EALAEAEAALRDL--RRELRELEAEIASLErrksniPARLLALRDALAEALGLDEAE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-289 |
2.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQ--IEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAER 175
Cdd:COG4913 608 NRAKLAALEAELAELEEelAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 176 RQLEAEENQRKQRENEEKERLEnerRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRIl 255
Cdd:COG4913 688 AALEEQLEELEAELEELEEELD---ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV- 763
|
170 180 190
....*....|....*....|....*....|....
gi 21355931 256 aeaeaAQAERRLFDAEIQRERDQADEEGQALRDA 289
Cdd:COG4913 764 -----ERELRENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-306 |
2.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLveAERQREREQAEKELQEQREAERRQLEA 180
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 181 eeNQRKQRENEEKERLENE----------------RRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEA 244
Cdd:COG4942 113 --LYRLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355931 245 EKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALrdaeivERLLAAERELSPSA 306
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL------EAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-336 |
3.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 105 LAAELARQQQIEADTRRQLAEAEAKL--VEERLRVQREKEESEEQQRKLVE---AERQREREQAEKELQEQrEAERRQLE 179
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIaeLEKELAALKKEEKALLKQLAALErriAALARRIRALEQELAAL-EAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 180 AEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355931 260 AAQAerrlfdAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQR 336
Cdd:COG4942 170 EAER------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-348 |
3.48e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 49 DAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADT--RRQLAEA 126
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTllGRTLVAA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 127 EAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAE 206
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 207 REREEnerrlqeaeeqrereeserrivvAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQAL 286
Cdd:COG1196 711 EAEEE-----------------------RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 287 RDAEIVERL-------LAAERELspsatESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENAR-RFLEA 348
Cdd:COG1196 768 ELERLEREIealgpvnLLAIEEY-----EELEERYDFLSEQREDLEEARETLEEAIEEIDRETReRFLET 832
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
101-200 |
3.78e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 101 KRQALAAELARQQQI------EADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRE--REQAEKELQEQRe 172
Cdd:COG2268 220 NREAEEAELEQEREIetariaEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEiaEREREIELQEKE- 298
|
90 100
....*....|....*....|....*...
gi 21355931 173 AERRQLEAEENQRKQRENEEKERLENER 200
Cdd:COG2268 299 AEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
133-200 |
5.78e-05 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 46.65 E-value: 5.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355931 133 ERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENER 200
Cdd:PTZ00266 436 ERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERERLERERLERDRLERDR 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
105-657 |
5.84e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 105 LAAELARQQQIEADTRR---QLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAE 181
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARkadELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 182 ------------------ENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAE 243
Cdd:PTZ00121 1342 kkaaeaakaeaeaaadeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 244 AEKERAEQQRILAEAEAAQAERRLFD-----AEIQRERDQADEEGQALRDAEIVERllAAERELSPSATESELEEDAAIA 318
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADeakkkAEEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 319 EQSRRLISSRTDLEQKQRmiEENARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPPRFQEPPEE 398
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 399 PMVHKVKtqfgQGSGPEDAYSAKSKTLTFPGVSDEGSSLEPKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQEVQ 478
Cdd:PTZ00121 1578 MALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 479 YTEDYlrslDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKmftslEEEELRHGDREDynpiKYTSEP 558
Cdd:PTZ00121 1654 KAEEE----NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----KAEELKKKEAEE----KKKAEE 1720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 559 TLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEeeiELERPSRGEDVEEE 638
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRMEVD 1797
|
570
....*....|....*....
gi 21355931 639 ATNEPKSSSFEEATEAQNE 657
Cdd:PTZ00121 1798 KKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-348 |
7.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 109 LARQQQIEADTRRQLAEAEAKLVEerlrVQREKEESEEQQRKLveaerqrerEQAEKELQEQREAERRQLEAEENQRKQR 188
Cdd:COG4913 598 IRSRYVLGFDNRAKLAALEAELAE----LEEELAEAEERLEAL---------EAELDALQERREALQRLAEYSWDEIDVA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 189 ENEEK-ERLENERRLIDAerereenerrlqeaeeqrereeSERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRL 267
Cdd:COG4913 665 SAEREiAELEAELERLDA----------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 268 fdAEIQRERDQA-DEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLissRTDLEQKQRMIEENARRFL 346
Cdd:COG4913 723 --EQAEEELDELqDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELERAMRAFN 797
|
..
gi 21355931 347 EA 348
Cdd:COG4913 798 RE 799
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
133-201 |
7.95e-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: 45.25 E-value: 7.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 133 ERLRVQREKEESEEqqRKLVEAERQRER-EQAEKELQEQREAERRQLEAEEnQRKQrenEEKERLENERR 201
Cdd:pfam07946 260 KKAKKTREEEIEKI--KKAAEEERAEEAqEKKEEAKKKEREEKLAKLSPEE-QRKY---EEKERKKEQRK 323
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-693 |
9.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQIEADTRRQlaeAEAKLVEERLRVQREKEESEEQQRklVEAERQREREQAEKELQEQREAERRQ 177
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKA---EDAKKAEAVKKAEEAKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 178 LEAEENQRKQRENEEKErlenERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAE 257
Cdd:PTZ00121 1271 AIKAEEARKADELKKAE----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 258 AEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRM 337
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 338 IEE--NARRFLEAEEEMVMLQQRQLQASHSK--EEADEYAGMEPVVEELCVKKVAPPRFQEPPEEPMVHKVKTQFGQGSG 413
Cdd:PTZ00121 1427 AEEkkKADEAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 414 PEDAYSAKSKTLTFPGVSDEGSSLEPKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQEVQYTED---------YL 484
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmalrkaeEA 1586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 485 RSLDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSL---EEEELRHGDR----EDYNPIKYTSE 557
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLkkkEAEEKKKAEElkkaEEENKIKAAEE 1666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 558 PTLRVKSHRRHK--RSPAKDVRPTAESTTSLEMLGEESTNPWGEVVPEHYKDTEFWKREKALSIDEEEIELERPSRGEDV 635
Cdd:PTZ00121 1667 AKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 636 EEEATNEPKSSSFEEATEAQNEQAVAALKQQLS--KEQLDKEAEKDNPQAVDTSDSNKSN 693
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
107-201 |
9.20e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 107 AELARQQQIEADTRRQLaEAEAKLveERLRVQREKEESEEQQRKlveAERQREREQAEKELQEQREAERRQLEAEENQRK 186
Cdd:pfam02029 228 GGLSQSQEREEEAEVFL-EAEQKL--EELRRRRQEKESEEFEKL---RQKQQEAELELEELKKKREERRKLLEEEEQRRK 301
|
90
....*....|....*
gi 21355931 187 QRENEEKERLENERR 201
Cdd:pfam02029 302 QEEAERKLREEEEKR 316
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
94-683 |
1.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 94 RVDPAGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESE---EQQRKLVEAER---QREREQAEKEL 167
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRveiARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 168 QEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQA-EAEK 246
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAkKAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 247 ERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEegqaLRDAEIVERllaaERELSPSATESELEEDAAIAEQSRRLIS 326
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE----LKKAEEKKK----ADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 327 SRTDLEQKQRMIE------ENARRFLEAEEEMVMLQQRQLQASHSKEEADEYAGMEPVVEELCVKKVAPprfQEPPEEPM 400
Cdd:PTZ00121 1320 AKKKAEEAKKKADaakkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEA 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 401 VHKVKTQFGQGSGPEDAYSAKSKTLTFPGVSDEGSSLE--PKTPFSIQQSSFSTQPSDEGNRIESERPEPEGEDQIQEVQ 478
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 479 YTEDYLRSLDGIKNRPLMREDGSGRRRAFKKRRSSGSSNSSRESRASRDEELKMFTSLEEEELRHGDREDYNPIKYTSEP 558
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 559 TLRVKSHRRHKRSPAKDVRPTAESTTSLEMLGEESTNPwgEVVPEHYKDTEFWKREKALSIDEEEIELERPSRGEdvEEE 638
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE--EEK 1632
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 21355931 639 ATNEPKSSSFEEATEAQNEQAVAALKQQLSKEQLDKEAEKDNPQA 683
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-276 |
2.04e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 62 ERLDKQIKEAAEREALAGTNVMQDGVlyvngiRVDPAGDKRQALAAELARQQQieadtrrQLAEAEAKLVEERLRVQREK 141
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEA------QLEELESKLDELAEELAELEE-------KLEELKEELESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 142 EESEEQQRKLVEAERQREREQAE-KELQEQREAERRQLEAEENQrKQRENEEKERLENERR-LIDAEREREENERRLQEA 219
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEeLLKKLEEAELKELQAELE 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21355931 220 EEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRER 276
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
92-201 |
2.80e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 44.34 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 92 GIRVDPAGDKRQALAAELARQQQIEadtrrqLAEAEAKLVEERLRVQREKEESEEQQRklveAERQR-EREQAEKELQEQ 170
Cdd:PTZ00266 427 GGRVDKDHAERARIEKENAHRKALE------MKILEKKRIERLEREERERLERERMER----IERERlERERLERERLER 496
|
90 100 110
....*....|....*....|....*....|.
gi 21355931 171 REAERRQLEAEENQRKQREneEKERLENERR 201
Cdd:PTZ00266 497 DRLERDRLDRLERERVDRL--ERDRLEKARR 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-371 |
3.79e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 134 RLRVQREKEESEEQQRKLVEAERQREREQAE-KELQEQREAERRQLEAEENQRKQRENEEKERLENERRLIdAEREREEN 212
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAElRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 213 ERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQrILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIV 292
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355931 293 ERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-371 |
6.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 100 DKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRE-----REQAEKELQEQrEAE 174
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerLEEAEEELAEA-EAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 175 RRQLEAEENQRKQRENEEKERLE----------------------NERRLIDAEREREENERRL-----QEAEEQREREE 227
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDelraeltllneeaanlrerlesLERRIAATERRLEDLEEQIeelseDIESLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 228 SERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEiqRERDQADEEGQALRD--AEIVERLLAAEREL--- 302
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE--SKRSELRRELEELREklAQLELRLEGLEVRIdnl 941
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355931 303 -SPSATESELEEDAAIAEQSRRLISS---RTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSKEEADE 371
Cdd:TIGR02168 942 qERLSEEYSLTLEEAEALENKIEDDEeeaRRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
111-202 |
7.57e-04 |
|
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: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 111 RQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQA-EKELQEQREAERRQLEAEENQRKQRE 189
Cdd:pfam05672 33 ERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAeEREQREQEEQERLQKQKEEAEAKARE 112
|
90
....*....|...
gi 21355931 190 NEEKERLENERRL 202
Cdd:pfam05672 113 EAERQRQEREKIM 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-205 |
8.02e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 40 FQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALAGTNVMQDGVLYVNGIRVDPAGDKRQALAAELARQQQIEADT 119
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 120 RRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEEnQRKQRENEEKERLENE 199
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL-PEPPDLEELERELERL 772
|
....*.
gi 21355931 200 RRLIDA 205
Cdd:COG1196 773 EREIEA 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-279 |
8.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 100 DKRQALAAELaRQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLE 179
Cdd:COG4717 71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 180 AEENQRKQRENEEKERLENERRLIDAEREREENERRLQeAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAE 259
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLS-LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|
gi 21355931 260 AAQAERRLFDAEIQRERDQA 279
Cdd:COG4717 229 LEQLENELEAAALEERLKEA 248
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
112-205 |
8.51e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 112 QQQIEADTRRQLAEaeaklvEERLRVQREKEESEEQQRKLvEAERQREREQAEKELQEQREAERRqlEAEENQRKQRENE 191
Cdd:PRK00409 527 ELERELEQKAEEAE------ALLKEAEKLKEELEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKK--EADEIIKELRQLQ 597
|
90
....*....|....*
gi 21355931 192 EKERLE-NERRLIDA 205
Cdd:PRK00409 598 KGGYASvKAHELIEA 612
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
137-366 |
9.21e-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: 42.42 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 137 VQREKEESEEQQRKLVEAERQrEREQAEKElQEQREAERRQLEAEENQRKQRENEEKERLENERRLIDAEREREENERRL 216
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKE-EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 217 QEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLL 296
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355931 297 AAERELSPSATESE--LEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEEMVMLQQRQLQASHSK 366
Cdd:pfam17380 436 EVRRLEEERAREMErvRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-371 |
9.35e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 118 DTRRQLAEAEAKLVeerlRVQREKEESEEQQRKLveaERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLE 197
Cdd:TIGR02168 176 ETERKLERTRENLD----RLEDILNELERQLKSL---ERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 198 NERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERD 277
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 278 QADEEGQALRDAEIVERL------LAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRFLEAEEE 351
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLeelkeeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260
....*....|....*....|
gi 21355931 352 MVMLQQRQLQASHSKEEADE 371
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLK 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-355 |
9.91e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 47 SVDAAADAEELPRMRERLDKQikeAAEREALAGTNVMQDGvlyvngiRVDPAGDKRQALAAEL----ARQQQIEADTRRQ 122
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGL---KRELSSLQSELRRIEN-------RLDELSQELSDASRKIgeieKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 123 LAEAEAklVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAE-ENQRKQRENEEKERLENERR 201
Cdd:TIGR02169 736 KERLEE--LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 202 LIDAERE---REENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQAERRLFDAEIQRERDQ 278
Cdd:TIGR02169 814 LREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 279 ADEEGQALRDAE-------IVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRMIEENARRfLEAEEE 351
Cdd:TIGR02169 894 LEAQLRELERKIeeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE-IRALEP 972
|
....
gi 21355931 352 MVML 355
Cdd:TIGR02169 973 VNML 976
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
100-351 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 100 DKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLE 179
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 180 AEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERA---EQQRILA 256
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleeKENEIEE 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 257 EAEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEdaAIAEQSRRLISSRTDLEQKQR 336
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLM--AIEEFEEKEERYNKDELEKER 999
|
250
....*....|....*
gi 21355931 337 MIEENARRFLEAEEE 351
Cdd:pfam02463 1000 LEEEKKKLIRAIIEE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-359 |
1.07e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 100 DKRQALAAELA-RQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLV--EAERQREREQAEKELQEQREAERR 176
Cdd:TIGR02169 254 EKLTEEISELEkRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLErsIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 177 QLEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESErrivVAERQREQAEAEKERAEQQRILA 256
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE----LKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 257 EAEAaqaerRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELspSATESELEEDAAIAEQ-SRRLISSRTDLEQKQ 335
Cdd:TIGR02169 410 RLQE-----ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI--KKQEWKLEQLAADLSKyEQELYDLKEEYDRVE 482
|
250 260
....*....|....*....|....
gi 21355931 336 RMIEENARRFLEAEEEMVMLQQRQ 359
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-362 |
1.08e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 120 RRQLAEAEAKLVE-----ERLRVQREK-EESEEQQRKLVEAE----------RQREREQAEKELQEQrEAERRQLEAEEN 183
Cdd:TIGR02169 183 EENIERLDLIIDEkrqqlERLRREREKaERYQALLKEKREYEgyellkekeaLERQKEAIERQLASL-EEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 184 QRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAEAEAAQA 263
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 264 ERRLfdAEIQRERDQADEEGQALRDaeiVERLLAAERElspsateselEEDAAIAEQSRRLISSRTDLEQKQRMIEENAR 343
Cdd:TIGR02169 342 EREI--EEERKRRDKLTEEYAELKE---ELEDLRAELE----------EVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250
....*....|....*....
gi 21355931 344 RFLEAEEEMVMLQQRQLQA 362
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADL 425
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
124-199 |
1.89e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355931 124 AEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAEENQRKQRENEEKERLENE 199
Cdd:cd16269 181 AEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKE 256
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
120-199 |
1.97e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.56 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 120 RRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQRERE-------QAEKELQEQREAERRQLEAEENQ-----RKQ 187
Cdd:PRK10811 643 RRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNdekrqaqQEAKALNVEEQSVQETEQEERVQqvqprRKQ 722
|
90
....*....|..
gi 21355931 188 RENEEKERLENE 199
Cdd:PRK10811 723 RQLNQKVRIEQS 734
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
110-201 |
2.52e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 110 ARQQQIEA--DTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEA--ERQREREQAEKELQE--QREAERRQLEAE-E 182
Cdd:PRK11637 167 ARQETIAElkQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQArnERKKTLTGLESSLQKdqQQLSELRANESRlR 246
|
90
....*....|....*....
gi 21355931 183 NQRKQRENEEKERLENERR 201
Cdd:PRK11637 247 DSIARAEREAKARAEREAR 265
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
101-249 |
2.63e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 101 KRQALAAELARQQQIEADTRRQLAEAEAKLVEE---RLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE 260
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355931 178 LEAEENQRKQRENEEKERLENERRlidAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERA 249
Cdd:pfam13868 261 EEFERMLRKQAEDEEIEQEEAEKR---RMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
103-201 |
2.91e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 103 QALAAELARQQQIEAD-TRRQLAEAEAKLVEERLRVQREK----EESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:cd16269 188 QADQALTEKEKEIEAErAKAEAAEQERKLLEEQQRELEQKledqERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|....
gi 21355931 178 LEAEENQRKQRENEEKERLENERR 201
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
40-178 |
3.09e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 40 FQHPGDSSVDAAADAEELPRMRERLDKQIKEAAEREALAgtnvmqdgvlyvngirvdpagdkrQALAAELARQQQIEADT 119
Cdd:PRK11448 134 FVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALA------------------------EAQQQELVALEGLAAEL 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 21355931 120 RRQLAEAEAKLveERLRVQREKEESEEQQRklveaeRQREREQAEKELqEQREAERRQL 178
Cdd:PRK11448 190 EEKQQELEAQL--EQLQEKAAETSQERKQK------RKEITDQAAKRL-ELSEEETRIL 239
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
100-279 |
4.64e-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: 39.93 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 100 DKRQALAAELARQQQIEADTRRQLAEaeaklveERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLE 179
Cdd:pfam15709 333 ASRDRLRAERAEMRRLEVERKRREQE-------EQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 180 AEENQRKQR--ENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRilae 257
Cdd:pfam15709 406 EERKQRLQLqaAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR---- 481
|
170 180
....*....|....*....|..
gi 21355931 258 AEAAQAERRLFDAEIQRERDQA 279
Cdd:pfam15709 482 QKQEAEEKARLEAEERRQKEEE 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
98-277 |
5.46e-03 |
|
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: 40.11 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQrerEQAEKELQEQREAERRQ 177
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 178 LEAEENQRKQRENEEKERLENERRLidaEREREENERRLQEAEEQREREESERRIVVAERQREQAEAE----KERAEQQR 253
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKEL---EERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErrkqQEMEERRR 553
|
170 180
....*....|....*....|....
gi 21355931 254 ILAEAEAAQAERRLFDAeIQRERD 277
Cdd:pfam17380 554 IQEQMRKATEERSRLEA-MERERE 576
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
106-181 |
5.90e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 37.84 E-value: 5.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355931 106 AAELARQ--QQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQLEAE 181
Cdd:COG0711 42 EAERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAE 119
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
102-362 |
6.14e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 102 RQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESE---EQQRKLVEAERQREREQAEKELQEQREAERRQL 178
Cdd:pfam13868 54 ERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 179 EAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQrEQAEAEKERAEQQRILAEA 258
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ-EKAQDEKAERDELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 259 EAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAEREL--------SPSATESELEEDAAIAEQSRRLISSRTD 330
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAereeeefeRMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270
....*....|....*....|....*....|..
gi 21355931 331 LEQkQRMIEENARRFLEAEEEMVMLQQRQLQA 362
Cdd:pfam13868 293 REL-EKQIEEREEQRAAEREEELEEGERLREE 323
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
98-370 |
7.81e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 39.25 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 98 AGDKRQALAAELARQQQIEADTRRQLAEAEAKLVEERLRVQREKEESEEQQRKLVEAERQREREQAEKELQEQREAERRQ 177
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 178 LEAEENQRKQRENEEKERLENERRLIDAEREREENERRLQEAEEQREREESERRIVVAERQREQAEAEKERAEQQRILAE 257
Cdd:COG3064 119 KEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355931 258 AEAAQAERRLFDAEIQRERDQADEEGQALRDAEIVERLLAAERELSPSATESELEEDAAIAEQSRRLISSRTDLEQKQRM 337
Cdd:COG3064 199 AAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGL 278
|
250 260 270
....*....|....*....|....*....|...
gi 21355931 338 IEENARRFLEAEEEMVMLQQRQLQASHSKEEAD 370
Cdd:COG3064 279 VVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
|
| |
