|
Name |
Accession |
Description |
Interval |
E-value |
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-696 |
1.06e-43 |
|
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: 169.92 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 39 EEFIFSTKRPKRPRPKTKAASStltaaptsaasssthpstttptpTVAFPTPALLPTPEPTTVRPYRPVFTTPNRKIVSS 118
Cdd:pfam17380 101 EEFVFSTIRPKSRKPKARTRGK-----------------------KRKTTTTMIQTTTPMMVTTSSSALEMTTTPKIVIF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 119 AATKSPKPPPTRTTATTLTTPPLKNRKV------------TEPIPVSEA---------------QMTGMQPSTRGYT--- 168
Cdd:pfam17380 158 ASKKNASGGNRSGEQRKQIQLIRRRRGNhsaftrpgrprtTTPMPVTHAtrfvpgiqmstvapkEVQGMPHTLAPYEkme 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 169 RGPQMHTTGVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEaHQVAINKIEEQvgeerrrggvEDHEHPAGSFRKQGPS 248
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQ-HQKAVSERQQQ----------EKFEKMEQERLRQEKE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 249 GNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMqraqkemew 328
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRM--------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 qREIARQKAEMDEKEkqrqveiarqmaERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:pfam17380 378 -RELERLQMERQQKN------------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 409 KKsemeKKERERQQEIARQHaERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:pfam17380 445 AR----EMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 489 ERLRKEEEQRIEAQ--RKAEEERRIEEQLAARE---------VENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDA 557
Cdd:pfam17380 520 KEMEERQKAIYEEErrREAEEERRKQQEMEERRriqeqmrkaTEERSRLEAMEREREMMRQIVESEKARAEYEATTPITT 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 558 TKTVlaglmsMSSRLTSTEPPQLE--IIHFTAPPPtpsspanEWVT-SPHSWRPPPDMQTNVLEWSRTPIpstgtselps 634
Cdd:pfam17380 600 IKPI------YRPRISEYQPPDVEshMIRFTTQSP-------EWATpSPATWNPEWNTVTAEEETPGIPI---------- 656
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 635 tVTSECDSNVECAFSYEDDLLCPHPNDATRYLQCTPMIGRRGRWTERMCPPNLVFIPSYGRC 696
Cdd:pfam17380 657 -IHSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIFIVSIGRC 717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
252-521 |
4.45e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.38 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQRE 331
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEK-EKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQK---EIARQVVERKKQEEVRRIEKA 407
Cdd:PTZ00121 1442 EAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadEAKKAAEAKKKADEAKKAEEA 1521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 408 RKKSEMEKKERERQQEIARQHAERQR----KEEEARRQEEARLFAERQKKERE------RQEEIARQMEEEEKRQREEAE 477
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEARIEEVMKLY 1601
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 597837628 478 KEEmRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1602 EEE-KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
252-523 |
5.68e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAE--MEQLERQRQQEIARQVAERQQKEREELEWQQEiARQEAERQRKEEEMR------RQQEYAQQMAEMQRAQ 323
Cdd:PTZ00121 1394 DEAKKKAEedKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAKKADEAKkkaeeaKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 324 KEMEWQREIARQKAEMDEK--EKQRQVEIARQMAERQRQEEELlRQQEVALQEAERQKKERERQKEIARQVVERKKQEEV 401
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEA-KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 402 RRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEM 481
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 597837628 482 RKRKIEEERLRKEEEQRIEAQRKAEEERRIE-EQLAAREVENQ 523
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDK 1674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-526 |
9.84e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 198 EDEFLKQLVRIVEAhqvAINKIEEQVGEERRRGGVED---HEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQ 274
Cdd:PTZ00121 1221 EDAKKAEAVKKAEE---AKKDAEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 275 VAERQQ-----KEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQR-EIARQKAEMDEK---EKQ 345
Cdd:PTZ00121 1298 AEEKKKadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEaEAAEEKAEAAEKkkeEAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 346 RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERErqqeiA 425
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA---KKKAEEKKKADEAKKKAEEAKKADE-----A 1449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 426 RQHAERQRKEEEARRQEEARLFAERQKK---ERERQEEIARQMEEEEKRQREEAEKEEMRKR----KIEEERLRKEEEQR 498
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKK 1529
|
330 340
....*....|....*....|....*...
gi 597837628 499 IEAQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
220-523 |
1.23e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 220 EEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAERQQ----KEREELEWQQEIARQ 295
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKKadeaKKKAEEAKKAEEAKK 1464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAemdekEKQRQVEIARQMAERQRQEEelLRQQEVALQEA 375
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA-----EAKKKADEAKKAEEAKKADE--AKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 376 ERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEmEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER 455
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 456 E---RQEEIAR-QMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:PTZ00121 1617 EakiKAEELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-522 |
1.52e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqRE 331
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:COG1196 367 LLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEearlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERL 491
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLE-----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
250 260 270
....*....|....*....|....*....|.
gi 597837628 492 RKEEEQRIEAQRKAEEERRIEEQLAAREVEN 522
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
264-521 |
3.98e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwQREIARQKAEMDEKE 343
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK-KAEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQmAERQRQEEELLRQQEValQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQ- 422
Cdd:PTZ00121 1532 EAKKADEAKK-AEEKKKADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMk 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 423 -EIARQHAERQRKEEEARRQEEARLFAERQKK----ERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE-ERLRKEEE 496
Cdd:PTZ00121 1609 aEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEK 1688
|
250 260
....*....|....*....|....*
gi 597837628 497 QRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAE 1713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
265-521 |
6.23e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEMEwqrEIARQKAEMDEKE 343
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElELELEEAQAEEYELLAELA---RLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 424 IARQHAERQRKEEEARRQEEARLfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQR 503
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALL-ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250
....*....|....*...
gi 597837628 504 KAEEERRIEEQLAAREVE 521
Cdd:COG1196 470 EEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-524 |
3.20e-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: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQvaERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:COG1196 245 EAELEELEAELEELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:COG1196 323 EELAELEEELE-ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260
....*....|....*....|....*...
gi 597837628 497 QRIEAQRKAEEERRIEEQLAAREVENQS 524
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-523 |
5.77e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 260 MEQLERQRQQ--------------EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMR-RQQEYAQQMAEMQRAQK 324
Cdd:COG1196 202 LEPLERQAEKaeryrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 325 EMEW-QREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRR 403
Cdd:COG1196 282 ELEEaQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQkkERERQEEIARQMEEEEKRQREEAEKEEMRK 483
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA--EEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 597837628 484 RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-521 |
7.78e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM-RRQQEYAQQMAEMQRAQKEMEWQREIA 333
Cdd:COG1196 232 LKLRELEAELeelEAELEELEAELEELEAELAELEAELEELRLELEELELELeEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKksem 413
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 414 EKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRK 493
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260
....*....|....*....|....*...
gi 597837628 494 EEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
210-513 |
1.63e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 210 EAHQVAINKIEEQVGEERRRGGVEDhehpagsFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQV--AERQQKEREELE 287
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAED-------ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAedARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 288 WQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAqkEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ 367
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAED-ARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE-RQRKEEEARRQEEARL 446
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAE--EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKK 1329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 447 FAERQKKERERQEEIARQMEEEEKRQREEAEKEEmRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
206-514 |
1.98e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 206 VRIVEAHQVAIN--KIEE--QVGEERRRGGVEDHEHPAgsfRKQGPSGNFEEGSSNAEMEQLERQRQQEIAR-QVAERQQ 280
Cdd:PTZ00121 1199 ARKAEAARKAEEerKAEEarKAEDAKKAEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEEARMAHFARrQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 281 KEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEmdekEKQRQVEIARQMAERQRQ 360
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 361 EEELLRQQevaLQEAERQKKERERQKEIARQVVE--RKKQEEVRRIEKARKKSEMEKKERE--RQQEIARQHAER-QRKE 435
Cdd:PTZ00121 1351 EAEAAADE---AEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEaKKKA 1427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 436 EEARRQEEARLFAERQKK--ERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
.
gi 597837628 514 Q 514
Cdd:PTZ00121 1508 A 1508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
218-514 |
4.97e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 218 KIEEQVGEERRRGGVEDHEHPAGSFRKQGpsgnfEEGSSNAEMEQLERQRQQEIARQVAERqqKEREELEWQQEIarQEA 297
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAA-----EAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEK--KKA 1548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 298 ERQRKEEEMRRqqeyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAER 377
Cdd:PTZ00121 1549 DELKKAEELKK----AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 378 QKKERERQKEIARqvVERKKQEEVRRIEKARKKSE---MEKKERERQQEIARQHAERQRKEEEARRQEEARLfaERQKKE 454
Cdd:PTZ00121 1625 LKKAEEEKKKVEQ--LKKKEAEEKKKAEELKKAEEenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL--KKEAEE 1700
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 455 RERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEErlRKEEEqriEAQRKAEEERRIEEQ 514
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--KKEAE---EDKKKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
218-521 |
6.92e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 218 KIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAErQQKEREELEWQQEIARQE- 296
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE----EAKKKADEAKKAAE-AKKKADEAKKAEEAKKADe 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 297 ---AERQRKEEEMRRQQEY--AQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVA 371
Cdd:PTZ00121 1527 akkAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEK 1605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 372 LQEAERQKKERErqkeiarqvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQ-----HAERQRKEEEARRQEEARL 446
Cdd:PTZ00121 1606 KMKAEEAKKAEE----------AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeEENKIKAAEEAKKAEEDKK 1675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 447 FAERQKKERERQEEIARQMEEEEKRQR-----EEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
216-454 |
9.47e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 216 INKIEEQVGEERRRGGVEDHEHPAgsfrKQGPSGNFEEGSSNAEMEQL---ERQRQQEIARQVAERQQKEREELEWQQEI 292
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 293 ARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVeiaRQMAERQRQEEELLRQQEVAL 372
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL---KKEAEEAKKAEELKKKEAEEK 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 373 QEAERQKKERERQKEIARQVV-----ERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLF 447
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKkeaeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
....*..
gi 597837628 448 AERQKKE 454
Cdd:PTZ00121 1796 VDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-513 |
1.13e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 240 GSFRKQGPSgnfeegSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEM 319
Cdd:PTZ00121 1067 GQDEGLKPS------YKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE-ARKAEDA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 QRAQKemewqreiARQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERERQKEIARQVVERKKQE 399
Cdd:PTZ00121 1140 RKAEE--------ARKAEDAKRVEIARKAEDARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 400 EVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeEARRQEEARLFAERQKKERERQEEIARQmeEEEKRQREEAEKE 479
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAE------EAKKAEEERNNEEIRKFEEARMAHFARR--QAAIKAEEARKAD 1281
|
250 260 270
....*....|....*....|....*....|....*...
gi 597837628 480 EMRK----RKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1282 ELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
274-419 |
2.01e-16 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 82.61 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 274 QVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAqqMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQ 353
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIE--TARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEA 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 354 MAER--QRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRriEKARKKSEMEKKERE 419
Cdd:COG2268 274 NAERevQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE--AEAEAEAIRAKGLAE 339
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
252-523 |
2.62e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERqqKEREELEWQQEIARQE----AERQRKEEEMR----RQQEYAQQmAEMQRAQ 323
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEekkkAEEAKKAEEDKnmalRKAEEAKK-AEEARIE 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 324 KEMEWQREIARQKAEMDEKEKQRQV--EIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKeIARQVVERKKQEEV 401
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK-IKAAEEAKKAEEDK 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 402 RRIEKARKKSEMEKKERE---RQQEIARQHAERQRKEEEARRQeearlfAERQKKERERQE---EIARQMEEEEKRQREE 475
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKK------AEELKKAEEENKikaEEAKKEAEEDKKKAEE 1748
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 597837628 476 AEKEEMRKRKIEEERLrkeeeqriEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKK--------EEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
261-519 |
3.64e-14 |
|
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: 74.57 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEA-ERQRKEEEMRRQQEYAQQMAEMQRAQKEMewQREIARQKAEM 339
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEkEEERKEERKRYRQELEEQIEEREQKRQEE--YEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 340 DEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQK-KERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKER 418
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 419 ERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQR 498
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF 263
|
250 260
....*....|....*....|.
gi 597837628 499 IEAQRKAEEERRIEEQLAARE 519
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKR 284
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
261-523 |
7.81e-14 |
|
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: 73.80 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQ----EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:pfam13868 47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQieerEQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEKQRQVEIARQMAERQRQEEELLRqqevaLQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDER-----ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 417 ERER------QQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKrqreeaEKEEMRKRKieeer 490
Cdd:pfam13868 202 ERDElraklyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE------EFERMLRKQ----- 270
|
250 260 270
....*....|....*....|....*....|...
gi 597837628 491 lrkeeEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:pfam13868 271 -----AEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
258-513 |
2.05e-13 |
|
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: 72.64 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE---MQRAQKEMEWQREIAR 334
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEderILEYLKEKAEREEERE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIArqvveRKKQEEVRRIEKARKKsEME 414
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA-----EKKARQRQELQQAREE-QIE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 415 KKERERQQEIARQHAERQR--KEEEARRQEEARLFAERQKKERERQEEIARQMeeeekrqreeAEKEEMRKRKIEEERLR 492
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI----------EEREEQRAAEREEELEE 316
|
250 260
....*....|....*....|.
gi 597837628 493 KEEeqriEAQRKAEEERRIEE 513
Cdd:pfam13868 317 GER----LREEEAERRERIEE 333
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
256-430 |
1.23e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 70.61 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 256 SNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQR-KEEEMRRQQEyaqqmaemQRAQKEMEWQREIAR 334
Cdd:PRK09510 57 PGAVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAA--------QEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQevalQEAERQKKERERQKeiARQVVERKKQEEVRRIEK----ARKK 410
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK----AAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKaaaeAKKK 202
|
170 180
....*....|....*....|
gi 597837628 411 SEMEKKERERQQEIARQHAE 430
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAE 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-464 |
8.20e-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: 69.32 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 202 LKQLVRIVEAHQVAINKIEEQVgEERRRGGVEDHEhpagsfRKQGPSGNFEEgsSNAEMEQLErqrqQEIARQVAERQQK 281
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKL-EELRLEVSELEE------EIEELQKELYA--LANEISRLE----QQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 282 EREELEWQQEIARQEAERQRKEEEM-RRQQEYAQQMAEMQRAQKEMEwqrEIARQKAEMDEKEKQRQVEI---ARQMAER 357
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELaELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLetlRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 358 QRQEEELLRQQEVALQEAERQKKERERQKeiarqvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEE 437
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQ-------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260
....*....|....*....|....*..
gi 597837628 438 ARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARL 491
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
258-465 |
1.34e-11 |
|
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: 66.87 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQ-QKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMaemQRAQKEMEWQREIARQK 336
Cdd:pfam13868 140 AEWKELEKEEEREEDERILEYLkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE---KAERDELRAKLYQEEQE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEKQrqveiarQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:pfam13868 217 RKERQKERE-------EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 597837628 417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQM 465
Cdd:pfam13868 290 EHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-464 |
2.70e-11 |
|
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: 67.77 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 250 NFEEGSSNAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEM 326
Cdd:TIGR02168 245 QEELKEAEEELEELTAElqeLEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE---RLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 EWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ-VVERKKQEEV--RR 403
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASlnNE 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
263-432 |
4.31e-11 |
|
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: 66.51 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 263 LERQRQQEIARQV--AERQQKEREELEW----QQEIARQEAERQRKEEEMRRQQEYAQQ-MAEMQRAQKEmewQREIARQ 335
Cdd:pfam15709 325 LEKREQEKASRDRlrAERAEMRRLEVERkrreQEEQRRLQQEQLERAEKMREELELEQQrRFEEIRLRKQ---RLEEERQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAERQRQE---EELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ----EEVRRIEKAR 408
Cdd:pfam15709 402 RQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmemAEEERLEYQR 481
|
170 180
....*....|....*....|....
gi 597837628 409 KKSEMEKKERERQQEiARQHAERQ 432
Cdd:pfam15709 482 QKQEAEEKARLEAEE-RRQKEEEA 504
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
304-432 |
8.79e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQeyaQQMAEMQRAQKEMEWQRE-IARQKAEMDEKEKQRQVEIARQMAERQRQEEellrQQEVALQEAERQKKER 382
Cdd:PRK09510 62 EQYNRQQ---QQQKSAKRAEEQRKKKEQqQAEELQQKQAAEQERLKQLEKERLAAQEQKK----QAEEAAKQAALKQKQA 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 597837628 383 ERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-523 |
8.79e-11 |
|
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: 65.85 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEME-QLER-QRQQEIARQVAErQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR- 334
Cdd:TIGR02168 196 NELErQLKSlERQAEKAERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKQRQ-------VEIAR--QMAERQRQEEELLRQQEVALQEA-ERQKKERERQKEIARQVVERKK--QEEVR 402
Cdd:TIGR02168 275 EVSELEEEIEELQkelyalaNEISRleQQKQILRERLANLERQLEELEAQlEELESKLDELAEELAELEEKLEelKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 403 RIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQ---------KKERERQEEIARQMEEEEKRQR 473
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerlEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 597837628 474 EEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQ--LAAREVENQ 523
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQalDAAERELAQ 486
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
329-456 |
9.73e-11 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 64.89 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQE-----EVRR 403
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEaeaayEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 597837628 404 IEkARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERE 456
Cdd:COG2268 273 AN-AEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
307-432 |
1.10e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 64.89 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 307 RRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA-RQMAERQRqeeELLRQQEVALQEAERQKKERERQ 385
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIEtARIAEAEA---ELAKKKAEERREAETARAEAEAA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 597837628 386 KEIARQVVER--KKQEEVRRIEKARKKSEMEKKERERQQE---IARQHAERQ 432
Cdd:COG2268 268 YEIAEANAERevQRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQ 319
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-516 |
1.30e-10 |
|
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: 65.38 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQ---QEIARQEAERQRKEEEM---RRQQEYAQQMAEMQRAQK 324
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqeLKLKEQAKKALEYYQLKeklELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 325 EMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEV-----ALQEAERQKKERERQKEIARQVVERKK-- 397
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqeeelKLLAKEEEELKSELLKLERRKVDDEEKlk 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 398 --QEEVRRIEKARKKS-------EMEKKERERQQEiARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:pfam02463 318 esEKEKKKAEKELKKEkeeieelEKELKELEIKRE-AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 597837628 469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLA 516
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
260-432 |
2.18e-10 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 63.38 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 260 MEQLERQRQQEIA-RQVAERQQKEREELEWQQEIARQE--AERQRKEEEMRRQ-----QEYAQQMAEMQRAQKEMEWQRE 331
Cdd:pfam05914 150 QEQMREWLEQQIEeKKQAEEEEKHAELLYDQKRLERDRraLELAKLEEECRRAvnaatKNFNQALAAEQAERRRLEKRQE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 iarQKAEMDEKEKQ---------RQVEIARQMAER----------QRQEEELLRQQEVALQEAERQKK-ERERQKEIARQ 391
Cdd:pfam05914 230 ---QEDNLAEIYNHltsdlltenPEVAQSSLGPHRvipdrwkgmsPEQLKEIRKEQEQQREEKERRREeEKQRDAEWDRQ 306
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 597837628 392 VVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam05914 307 RLELARAALLLEREQQRLRRELRRQLDEENLQLAQEQKARQ 347
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
258-432 |
3.85e-10 |
|
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: 63.43 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLE----RQRQQEIARQVAERQQKE---REELEWQQEIARQEAE--RQRKEEEMRRQQEY-AQQMAEMQRAQKEME 327
Cdd:pfam15709 343 AEMRRLEverkRREQEEQRRLQQEQLERAekmREELELEQQRRFEEIRlrKQRLEEERQRQEEEeRKQRLQLQAAQERAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 328 WQREIARQKAEmdekEKQRQveiaRQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiARQVVERKKQEEVrriEKA 407
Cdd:pfam15709 423 QQQEEFRRKLQ----ELQRK----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-ERLEYQRQKQEAE---EKA 490
|
170 180
....*....|....*....|....*
gi 597837628 408 RKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15709 491 RLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-401 |
4.04e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 198 EDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAE 277
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE----EAKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 278 RQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKAEMDEKEKQRQVEIARQMAER 357
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED------KKKAEEAKKDEEEKKKIAHLKKEE 1766
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 597837628 358 QRQEEELLRQQEVALQEaERQKKERERQKEIARQVVERKKQEEV 401
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
261-426 |
8.37e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRK--EEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE 338
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKqaEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 339 MDEKE--KQRQVEIARQM---------AERQRQEEELLRQQEVALQ--EAERQKKERERQKEIARQVVERKKQE-EVRRI 404
Cdd:TIGR02794 158 AKAAAeaKKKAEEAKKKAeaeakakaeAEAKAKAEEAKAKAEAAKAkaAAEAAAKAEAEAAAAAAAEAERKADEaELGDI 237
|
170 180
....*....|....*....|..
gi 597837628 405 EKARKKSEMEKKERERQQEIAR 426
Cdd:TIGR02794 238 FGLASGSNAEKQGGARGAAAGS 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-539 |
9.98e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 240 GSFRKQGPSGNF-----EEGSSNAEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQE 311
Cdd:TIGR02169 658 GSRAPRGGILFSrsepaELQRLRERLEGLKRELsslQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 312 yaqQMAEMQRAQKEMEwqREIARQKAEMDEKEKqrqvEIARQmaerqrqeEELLRQQEVALQEAERqKKERERQKEIARQ 391
Cdd:TIGR02169 738 ---RLEELEEDLSSLE--QEIENVKSELKELEA----RIEEL--------EEDLHKLEEALNDLEA-RLSHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 392 VveRKKQEEVRRIEKARKKSEMEKKERERQQEIA---RQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:TIGR02169 800 L--SKLEEEVSRIEARLREIEQKLNRLTLEKEYLekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER--RIEEQLAAREVENQSTVVNPAFGMHIPGET 539
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-518 |
1.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQ-RQQEIARQVAERQQKEREEL------EWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:TIGR02168 684 EKIEELEEKiAELEKALAELRKELEELEEEleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQK-AEMDEKEKQRQVEIARQMAERQRQEEEL--LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA 407
Cdd:TIGR02168 764 EELEERlEEAEEELAEAEAEIEELEAQIEQLKEELkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 408 RKKSEmekKERERQQEIARQHAERQRKEEEARRQeearlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIE 487
Cdd:TIGR02168 844 EEQIE---ELSEDIESLAAEIEELEELIEELESE------LEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270
....*....|....*....|....*....|....
gi 597837628 488 EERLRKEEEQRIEAQRKAE---EERRIEEQLAAR 518
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGlevRIDNLQERLSEE 948
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
261-378 |
1.35e-09 |
|
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: 57.74 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:pfam05672 25 EQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKE 104
|
90 100 110
....*....|....*....|....*....|....*...
gi 597837628 341 EKEKQrqveiARQMAERQRQEEELLRQQEvalqEAERQ 378
Cdd:pfam05672 105 EAEAK-----AREEAERQRQEREKIMQQE----EQERL 133
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-430 |
2.42e-09 |
|
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: 60.16 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQM------------ 316
Cdd:COG4942 49 EEKALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 317 AEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA--RQMAERQRQE-EELLRQQEVALQEAERQKKERErqkEIARQVV 393
Cdd:COG4942 129 EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalRAELEAERAElEALLAELEEERAALEALKAERQ---KLLARLE 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 597837628 394 ERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
304-520 |
3.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE-MDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERqKKER 382
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEaKKKAEDARKAEEARK-AEDARKAEEARKAEDAKRVEIAR-KAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 383 ERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeearrqeearlfaERQKKERERQEEIA 462
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE------------------ERKAEEARKAEDAK 1224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 463 RqmeeeekrqreeaeKEEMRKrkieeerlrkeeeqrIEAQRKAEEE-RRIEEQLAAREV 520
Cdd:PTZ00121 1225 K--------------AEAVKK---------------AEEAKKDAEEaKKAEEERNNEEI 1254
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
268-525 |
3.31e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.47 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 268 QQEIARQVAERQQKEreelewqQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRaqkemewQREIARQKAemDEKEKQRQ 347
Cdd:TIGR02794 45 PGAVAQQANRIQQQK-------KPAAKKEQERQKKLEQQAEEAE-KQRAAEQAR-------QKELEQRAA--AEKAAKQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 VEIARQMAERQRQEEELLRQQEvalqeAERQKKererqkeiARQVVERKKQEEvrriekARKKSEMEKKERErqQEIARQ 427
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQA-----AEAKAK--------AEAEAERKAKEE------AAKQAEEEAKAKA--AAEAKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 428 HAERQRKeeearrqeearlfaeRQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEE 507
Cdd:TIGR02794 167 KAEEAKK---------------KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
250
....*....|....*...
gi 597837628 508 ERRIEEQLAAREVENQST 525
Cdd:TIGR02794 232 AELGDIFGLASGSNAEKQ 249
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
289-426 |
4.82e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.79 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 289 QQEIARQEAERQRKEEEMRrqqeyaqqmAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL---- 364
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKE---------AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 365 --LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR-------KKSEMEKKERERQQEIAR 426
Cdd:PRK12704 103 elLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeaKEILLEKVEEEARHEAAV 173
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
270-400 |
5.36e-09 |
|
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: 55.82 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 270 EIARQVAERQQKERE--ELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQ 347
Cdd:pfam05672 11 EAARILAEKRRQAREqrEREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 597837628 348 VEIARQMAERQRQEEELLRQQEvalqEAERQKKERERQKEIARQV-VERKKQEE 400
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKARE----EAERQRQEREKIMQQEEQErLERKKRIE 140
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-426 |
7.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEMEWQ--REIARQKA 337
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERlEARLDALREELDELEAQIRGNggDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 338 EMDEKEKQRQveiaRQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:COG4913 346 EIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
....*....
gi 597837628 418 RERQQEIAR 426
Cdd:COG4913 422 RELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
258-432 |
7.43e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQqEIARQVAERQQKEREELEWQQEIARQEAERQRKEEE---MRRQQEYAQQMAEMQRAQKEMEwqrEIAR 334
Cdd:COG4717 71 KELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREElekLEKLLQLLPLYQELEALEAELA---ELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKqrqvEIARQMAERQRQEEELLR-QQEVALQEAERQKKERERQKEIARQVveRKKQEEVRRIEKARKKSEM 413
Cdd:COG4717 147 RLEELEERLE----ELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELEEAQE 220
|
170
....*....|....*....
gi 597837628 414 EKKERERQQEIARQHAERQ 432
Cdd:COG4717 221 ELEELEEELEQLENELEAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
338-519 |
8.96e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEiarqMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:PTZ00121 1080 DFDAKEDNRADE----ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 418 RERQQEIARQhaerqrkeeearrqeearlFAERQKKERERQEEIARQmeeeekrQREEAEKEEMRKrkieeerlrkEEE- 496
Cdd:PTZ00121 1156 IARKAEDARK-------------------AEEARKAEDAKKAEAARK-------AEEVRKAEELRK----------AEDa 1199
|
170 180
....*....|....*....|...
gi 597837628 497 QRIEAQRKAEEERRIEEQLAARE 519
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAED 1222
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
264-521 |
1.04e-08 |
|
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: 59.21 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERER---QKEIARQVVERKKQEEVRRIEKARKKSEMEKKERER 420
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelsLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 421 QQE----IARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:pfam02463 807 EEElkeeAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
250 260
....*....|....*....|....*
gi 597837628 497 QRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNL 911
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
252-541 |
1.04e-08 |
|
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: 59.21 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-----EMQRAQKEM 326
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKvddeeKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 EW-QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:pfam02463 324 KKaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 406 KARKKSEMEkkERERQQEIARqhAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRK 485
Cdd:pfam02463 404 EKEAQLLLE--LARQLEDLLK--EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 486 IEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQA 541
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
250-523 |
1.47e-08 |
|
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: 58.83 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 250 NFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQ 329
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 330 REIARQKAEMDEKEKQRQVEIARQMAERQRQ--EEELLRQQEVALQEAERQKKERERQKEiarqvverKKQEEVRRIEKA 407
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEQKLEKlaEEELERLEEEITKEELLQELLLKEEEL--------EEQKLKDELESK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 408 RKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER--------ERQEEIARQMEEEEKRQREEAEKE 479
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEllleeadeKEKEENNKEEEEERNKRLLLAKEE 971
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 597837628 480 EMRK--RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:pfam02463 972 LGKVnlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-517 |
1.53e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 202 LKQLVRIVEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQvaERQQK 281
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 282 EREELEWQQEIARQEAERQRkEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKaemdEKEKQRQVEIARQMAERQRQE 361
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAE-EELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 362 EELLRQQEVALQEAERQKKERERQKEIARQVVErkkqEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQ 441
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 442 EEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER--RIEEQLAA 517
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkRLENKIKE 983
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
275-532 |
1.93e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 57.74 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 275 VAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQmAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQM 354
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRK 434
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 435 EEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQ 514
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250
....*....|....*...
gi 597837628 515 LAAREVENQSTVVNPAFG 532
Cdd:COG3064 240 TEEAALGGAEEAADLAAV 257
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-457 |
2.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEkqrqveiaRQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQ-------EEVRRIEKARK 409
Cdd:COG4717 132 QELEALE--------AELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEqlslateEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 597837628 410 KSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERER 457
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
259-530 |
2.40e-08 |
|
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: 58.06 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELEwQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE 338
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLL-KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 339 MDEKEKQRQVEIARQMAERQRQEEELLRqqevaLQEAERQ--KKERERQKEIARQVVERKKQEEvRRIEKARKKSEMEKK 416
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEE-----EQLLIEQeeKIKEEELEELALELKEEQKLEK-LAEEELERLEEEITK 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
250 260 270
....*....|....*....|....*....|....
gi 597837628 497 QRIEAQRKAEEERRIEEQLAAREVENQSTVVNPA 530
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
272-463 |
2.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 272 ARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA 351
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 352 RQ-MAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG1196 659 GGsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
170 180 190
....*....|....*....|....*....|...
gi 597837628 431 RQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
252-410 |
2.77e-08 |
|
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: 56.78 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREElewqQEIARQEAERQRKEEEMRRQQEY-AQQMAEMQRAQKemewQR 330
Cdd:TIGR02794 74 EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA----EQAAKQAEEKQKQAEEAKAKQAAeAKAKAEAEAERK----AK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQ--EAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:TIGR02794 146 EEAAKQAE-EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAkaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
..
gi 597837628 409 KK 410
Cdd:TIGR02794 225 AE 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
327-526 |
4.64e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 EWQReIARQKAEMDEKEKQRQVEIARQMAE-RQRQEEELLRQQEVAlQEAERQKKERERQKEIARQVVERKKQEE---VR 402
Cdd:PRK09510 63 QYNR-QQQQQKSAKRAEEQRKKKEQQQAEElQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEeaaAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 403 RIEKARKKSEMEKKereRQQEIARQHAERQRKEEEARRQEEARlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMR 482
Cdd:PRK09510 141 AAAAAKAKAEAEAK---RAAAAAKKAAAEAKKKAEAEAAKKAA--AEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 597837628 483 KRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
252-427 |
5.08e-08 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 56.92 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLE---RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKEM 326
Cdd:pfam13779 503 ERGASDEEIAKLMqelREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARSgrRAEAQQMLSQL 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 ewQREIAR-QKAEMDekekQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE--------RQKEIARQVVERKK 397
Cdd:pfam13779 583 --QQMLENlQAGQPQ----QQQQQGQSEMQQAMDELGDLLREQQQLLDETFRQLQQQGgqqqgqpgQQGQQGQGQQPGQG 656
|
170 180 190
....*....|....*....|....*....|
gi 597837628 398 QEEVRRIEKARKKSEMEKKERERQQEIARQ 427
Cdd:pfam13779 657 GQQPGAQMPPQGGAEALGDLAERQQALRRR 686
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-420 |
7.70e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 341 EKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIAR-------------QVVERKK--QEEVRRIE 405
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeELEERYDflSEQREDLE 808
|
170 180
....*....|....*....|
gi 597837628 406 KARKK-----SEMEKKERER 420
Cdd:COG1196 809 EARETleeaiEEIDRETRER 828
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
203-392 |
1.04e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.85 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 203 KQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKE 282
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 283 REELEWQQEI---ARQEAERQRKEEEMRRQQEY---AQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAE 356
Cdd:TIGR02794 145 KEEAAKQAEEeakAKAAAEAKKKAEEAKKKAEAeakAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 597837628 357 RQRQEEEL-LRQQEVALQEAERQKKERERQKEIARQV 392
Cdd:TIGR02794 225 AERKADEAeLGDIFGLASGSNAEKQGGARGAAAGSEV 261
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-518 |
1.04e-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: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 279 QQKEREELEwqQEIARQE---AERQRKEEEMRRQQEYAQQMAEMQRAQKEmewqrEIARQKAEMDEKEKQRQVEIARQMA 355
Cdd:TIGR02168 675 RRREIEELE--EKIEELEekiAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA---RKKSEMEKKERERQQEIARQHAERQ 432
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 433 RKEEEARRQEEARLFAERQKKE-RERQEEIARQMEEEEKRQREEAEK-----EEMRKRKIEEERLRKEEEQRIEAQRKAE 506
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEElSEDIESLAAEIEELEELIEELESEleallNERASLEEALALLRSELEELSEELRELE 907
|
250
....*....|..
gi 597837628 507 EERRIEEQLAAR 518
Cdd:TIGR02168 908 SKRSELRRELEE 919
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
252-422 |
1.76e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQlERQRQQEIARQVAERQQKEREELEWQ-QEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKemewQR 330
Cdd:PRK09510 90 EELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEAAKQaALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK----AA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKK 410
Cdd:PRK09510 165 AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA 244
|
170
....*....|..
gi 597837628 411 SEMEKKERERQQ 422
Cdd:PRK09510 245 KAAEKAAAAKAA 256
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
261-559 |
1.81e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyAQQMAEMQRA---QKEMEWQREIARQKA 337
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ--AEEEAREAKAeaeQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKeiARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEK-AAAAAEKEKAEEAKRK--AEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 418 RERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQ 497
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 498 RIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDATK 559
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDD 299
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
269-426 |
2.21e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQQEI-ARQEAERQRKEEEmrrqQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQrq 347
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE----KELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 vEIARQMAERQRQEEELLRQQEVALQEAERQKKERER----QKEIARQVVERKKQEEVRRiEKARKKSEMEKKERERQQE 423
Cdd:PRK12704 111 -ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEILLEKVEEEARH-EAAVLIKEIEEEAKEEADK 188
|
...
gi 597837628 424 IAR 426
Cdd:PRK12704 189 KAK 191
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
199-402 |
2.33e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 199 DEFLKQLVRI-VEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSS---------NAEMEQLERQRQ 268
Cdd:COG3206 159 EAYLEQNLELrREEARKALEFLEEQLPELRKE--LEEAEAALEEFRQKNGLVDLSEEAKlllqqlselESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQ--------QEIARQEAERQRKEEEMRRQqeYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPellqspviQQLRAQLAELEAELAELSAR--YTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 341 EKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVER--KKQEEVR 402
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllQRLEEAR 378
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
258-388 |
2.53e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMrrQQEYAQQMAEmqrAQKemewqrEIARQKA 337
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA--EKEAQQAIKE---AKK------EADEIIK 591
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 597837628 338 EMDEKEKQRQVEIARQmaerqrQEEELLRQQEVALQEAE-RQKKERERQKEI 388
Cdd:PRK00409 592 ELRQLQKGGYASVKAH------ELIEARKRLNKANEKKEkKKKKQKEKQEEL 637
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
277-519 |
3.04e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.19 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQ-EIARQEAERQRKE-EEMRRQQEYAQQMAEMQRAQKEMEWQReiarqKAEMDEKEKQRQVEiarqm 354
Cdd:pfam15709 329 EQEKASRDRLRAERaEMRRLEVERKRREqEEQRRLQQEQLERAEKMREELELEQQR-----RFEEIRLRKQRLEE----- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 aERQRQEEELLRQqevALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKArkksemeKKERERQQEIARQHAERQRK 434
Cdd:pfam15709 399 -ERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERA-------EAEKQRQKELEMQLAEEQKR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 435 EEEARRQeearlfaERQKKERERQEEiarqmeeeekrqreeaekEEMRKRKIEEERLRKEeeqriEAQRKAEEERRIEEQ 514
Cdd:pfam15709 468 LMEMAEE-------ERLEYQRQKQEA------------------EEKARLEAEERRQKEE-----EAARLALEEAMKQAQ 517
|
....*
gi 597837628 515 LAARE 519
Cdd:pfam15709 518 EQARQ 522
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
313-432 |
3.24e-07 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 50.56 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 313 AQQMAE-MQRAQKEMEWQREIarqKAEMDEKEKQRQVEIARQMAERQRQEEELLRQqevalQEAERQKKERERQKEIARQ 391
Cdd:pfam15236 41 PAQLEErERKRQKALEHQNAI---KKQLEEKERQKKLEEERRRQEEQEEEERLRRE-----REEEQKQFEEERRKQKEKE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 597837628 392 VVERKKQEEVRR-IEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15236 113 EAMTRKTQALLQaMQKAQELAQRLKQEQRIRELAEKGHDTSQ 154
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
280-424 |
3.45e-07 |
|
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: 52.96 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 280 QKEREELEwqqEIARQEAERQRKEEE-----MRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRqveiarqM 354
Cdd:cd16269 148 LEDREKLV---EKYRQVPRKGVKAEEvlqefLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKL-------L 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQ---KKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEI 424
Cdd:cd16269 218 EEQQRELEQKLEDQERSYEEHLRQlkeKMEEERENLLKEQ---ERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
258-535 |
3.60e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQeiARQVAERQQKEREELEwqQEIARQEAERQRKEEEMRR--------QQEYAQQMAEMQRAQKEME-W 328
Cdd:COG4372 38 FELDKLQEELEQ--LREELEQAREELEQLE--EELEQARSELEQLEEELEElneqlqaaQAELAQAQEELESLQEEAEeL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDEKEKQRQV------EIARQMAERQRQEEELLRQQEVALQEAERQKKERERQ-KEIARQVVERKKQEEV 401
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQleaqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 402 RRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLF-AERQKKERERQEEIARQMEEEEKRQREEAEKEE 480
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLdALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 481 MRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHI 535
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
309-419 |
3.92e-07 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 53.07 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 309 QQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRqveiarqMAERQRQEEELLRQQEVALQEAERQKKER---ERQ 385
Cdd:pfam07767 202 QKAVEAEKKRLKEEEKLERVLEKIAESAATAEAREEKR-------KTKAQRNKEKRRKEEEREAKEEKALKKKLaqlERL 274
|
90 100 110
....*....|....*....|....*....|....
gi 597837628 386 KEIARQVVERKKQEEVRRIEKARKKSEMEKKERE 419
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
264-398 |
4.19e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 53.89 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKEREELEWQQEIARQeaeRQRKEEEMRRQQEYAQQMAEMQRaqkemewqreiaRQKAEMDEKE 343
Cdd:PRK10811 601 ERQQDRRKPRQNNRRDRNERRDTRDNRTRREG---RENREENRRNRRQAQQQTAETRE------------SQQAEVTEKA 665
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 344 KQRQVEIARQMAERQ--RQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ 398
Cdd:PRK10811 666 RTQDEQQQAPRRERQrrRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQ 722
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
296-425 |
4.70e-07 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 51.04 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEA 375
Cdd:pfam12072 26 EAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQRQ-ERRLLQKEETLDRKDESLEKK 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 376 ERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE--------------MEKKERERQQEIA 425
Cdd:pfam12072 105 EESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELErisgltseeakeilLDEVEEELRHEAA 168
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
264-423 |
4.96e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 52.73 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKEREELEWQQEiarqEAERQRKEEEMRRQQEYAQQMaEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQE----TLERERRLLLQQSQEQWQAEK-EQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARqvvERKKQEEVRRIEKA-RKKSEMEKKERERQQ 422
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAcHKRQLKEREEQKKVQ 170
|
.
gi 597837628 423 E 423
Cdd:pfam15558 171 E 171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
197-513 |
5.52e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 197 SEDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDhehpaGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEiarQVA 276
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE-----KSRLKKEEKEEEKSELSLKEKELAEEREKTE---KLK 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEM-DEKEKQRQVEIARQMA 355
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKlAEEELERLEEEITKEE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEvrrIEKARKKSEMEKKERERQQEIARQHAERQRKE 435
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL---EEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 436 EEARRQEEARLFAERQKKER-ERQEEIARQMEEEEKRQREEAEKEEMR----------KRKIEEERLRKEEEQRIEAQRK 504
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKdelekerleeEKKKLIRAIIEETCQRLKEFLE 1024
|
....*....
gi 597837628 505 AEEERRIEE 513
Cdd:pfam02463 1025 LFVSINKGW 1033
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
355-517 |
5.84e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAER----QKKERERQKEIARqvVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAEReteiAIAQANREAEEAE--LEQEREIETARIAEAEAELAKKKAEERREAETARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 431 RQRKEEearrqeearlfAERQKKERERQEEIARQmeeeekrQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER- 509
Cdd:COG2268 266 AAYEIA-----------EANAEREVQRQLEIAER-------EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170
....*....|.
gi 597837628 510 ---RIEEQLAA 517
Cdd:COG2268 328 eaeAIRAKGLA 338
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
261-381 |
6.09e-07 |
|
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: 52.19 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLER--QRQQEIARQV--AERQQKEREELEWQQEIARQEAERQRK-EEEMRRQQEyaQQMAEMQRAQKEMewqreIARQ 335
Cdd:cd16269 170 EVLQEflQSKEAEAEAIlqADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELE--QKLEDQERSYEEH-----LRQL 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 597837628 336 KAEMdEKEKQRQVEIARQMAERQRQEEELLrQQEVALQEAERQKKE 381
Cdd:cd16269 243 KEKM-EEERENLLKEQERALESKLKEQEAL-LEEGFKEQAELLQEE 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
266-523 |
7.58e-07 |
|
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: 53.05 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM----RRQQEYAQQMAEMQRAQKEMEWQR------EIARQ 335
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqlrARIEELRAQEAVLEETQERINRARkaaplaAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAER---------------------------QRQEEELLRQQEVAL---QEAERQKKERER- 384
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRakllmkraahvkqqssieeqrrllqtlHSQEIHIRDAHEVATsirEISCQQHTLTQHi 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 385 -----QKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQrkeeearrQEEARLFAERQKKERERQE 459
Cdd:TIGR00618 382 htlqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--------LQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 460 EIARQMEEEEKRQREEAEKEEMR-KRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
299-431 |
7.76e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 52.35 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELL--RQQEVALQE-- 374
Cdd:pfam15558 16 RHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKEsr 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 375 ----AERQKKERERQKEIARQVVERKKQEEVRRIekaRKKSEMEKKERERQQEIARQHAER 431
Cdd:pfam15558 96 wreqAEDQENQRQEKLERARQEAEQRKQCQEQRL---KEKEEELQALREQNSLQLQERLEE 153
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-530 |
8.49e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 253 EGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-EMQRAQKEMEWQRE 331
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 ----IARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA 407
Cdd:COG4372 102 elesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 408 RKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIE 487
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 597837628 488 EERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPA 530
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-427 |
8.54e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 237 HPAGSFRKQGPSGNFEE---GSSNaemeqleRQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYA 313
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRyvlGFDN-------RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 314 QQMAEMQRAQKEM-EWQREIARQKAEMDE-KEKQRQVEIARQMAERQRQEEELLRQQEVALQEA-ERQKKERERQKEIAR 390
Cdd:COG4913 658 WDEIDVASAEREIaELEAELERLDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKElEQAEEELDELQDRLE 737
|
170 180 190
....*....|....*....|....*....|....*..
gi 597837628 391 QVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQ 427
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
332-461 |
1.14e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.52 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEM-DEKEKQRQVeIARQMAERQRQEEELlRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARK- 409
Cdd:PRK00409 504 IEEAKKLIgEDKEKLNEL-IASLEELERELEQKA-EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKe 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 410 -KSEME---KKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEI 461
Cdd:PRK00409 582 aKKEADeiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
243-430 |
1.17e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 51.93 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 243 RKQGPSGNFeegsSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAER---QRKEEEMRRQQEYAQQMAEM 319
Cdd:pfam05262 161 KKNILSGNV----SDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKraqQLKEELDKKQIDADKAQQKA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 QRAQKEMEWQREIARQKaemdEKEKQRQVEIARQMAERQRQeeellrqqevalQEAERQKKERER-QKEIARQVVERKKQ 398
Cdd:pfam05262 237 DFAQDNADKQRDEVRQK----QQEAKNLPKPADTSSPKEDK------------QVAENQKREIEKaQIEIKKNDEEALKA 300
|
170 180 190
....*....|....*....|....*....|..
gi 597837628 399 EEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:pfam05262 301 KDHKAFDLKQESKASEKEAEDKELEAQKKREP 332
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
268-430 |
1.21e-06 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 52.35 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 268 QQEIARQVAERQQKEREELEWQQEIARQEAERQRKeeeMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQ 347
Cdd:pfam10168 530 PQECLQLLSRATQVFREEYLKKHDLAREEIQKRVK---LLKLQK-EQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 VEIARQMAERQRqeeeLLRQQEVALQEAERQ-KKERERQKEIARQVVER-----KKQEEVRR-IEK---ARKKSEMEKKE 417
Cdd:pfam10168 606 EKLMRRCKKVLQ----RLNSQLPVLSDAEREmKKELETINEQLKHLANAikqakKKMNYQRYqIAKsqsIRKKSSLSLSE 681
|
170
....*....|....*
gi 597837628 418 RERQ--QEIARQHAE 430
Cdd:pfam10168 682 KQRKtiKEILKQLGS 696
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-463 |
1.50e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 254 GSSNAEMEQLERQrqqeIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ-EYAQQMAEMQRAQKEMEWQR-- 330
Cdd:TIGR02169 297 GELEAEIASLERS----IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkRRDKLTEEYAELKEELEDLRae 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 --EIARQKAEMDEKEKQRQVEIarqmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAr 408
Cdd:TIGR02169 373 leEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA- 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 409 kkSEMEKKERERQQEIARQHAERQRKEEEARRqeearlFAERQKKERERQEEIAR 463
Cdd:TIGR02169 448 --LEIKKQEWKLEQLAADLSKYEQELYDLKEE------YDRVEKELSKLQRELAE 494
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
280-410 |
1.61e-06 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 50.09 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 280 QKEREELE-WQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEM---EWQREIARQKAEMDEKEKQRQVEIARQMA 355
Cdd:pfam13904 48 KLERQPLEaYENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEkyqEWLQRKARQQTKKREESHKQKAAESASKS 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERE-RQKEIARQVVERKKQEEVRRIEKARKK 410
Cdd:pfam13904 128 LAKPERKVSQEEAKEVLQEWERKKLEQQqRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-463 |
1.65e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAER-QKKERERQKEIARQVVERKKQEEVRRIEKARKKsemEKKERER 420
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELeLEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLEAER 734
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 597837628 421 QQEIARQHAERQRKEEEARRQEEARLFAERQKKERER-QEEIAR 463
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERlEREIEA 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-427 |
1.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQE---AERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR 334
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEM-------DEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiarqvverkkqEEVRRIEka 407
Cdd:COG4913 366 ALLAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-----------AEIASLE-- 432
|
170 180
....*....|....*....|
gi 597837628 408 RKKSEMEKKERERQQEIARQ 427
Cdd:COG4913 433 RRKSNIPARLLALRDALAEA 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-523 |
1.97e-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: 51.99 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQ-----QEIARQVAERQQKE--REELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-EMQRAQKEMEwqr 330
Cdd:TIGR02169 199 QLERLRREREkaeryQALLKEKREYEGYEllKEKEALERQKEAIERQLASLEEELEKLTEEISELEkRLEEIEQLLE--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQKAEMDEKEkqrQVEIARQMAERQRQEEELLRQQEVALQE----AERQKKERERQKEIARQVVERKKQEEVRRIEK 406
Cdd:TIGR02169 276 ELNKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKEREledaEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 407 ARKKSEMEKKERERQ------QEIARQHAERQrkeeearrqeearlfaERQKKERERQEEIARQMeeeEKRQREEAEKEE 480
Cdd:TIGR02169 353 DKLTEEYAELKEELEdlraelEEVDKEFAETR----------------DELKDYREKLEKLKREI---NELKRELDRLQE 413
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 597837628 481 MRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
295-464 |
2.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 QEAERQRKEEEmRRQQEYAQQMAEMQRAQKEME-WQREIARQKAEMDEKEKQRQveiARQMAERQRQEEELLRQQEVALQ 373
Cdd:COG4717 74 KELEEELKEAE-EKEEEYAELQEELEELEEELEeLEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 374 EAERQKKE-RERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQK 452
Cdd:COG4717 150 ELEERLEElRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 597837628 453 KERERQEEIARQ 464
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
259-383 |
2.27e-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: 50.69 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQkae 338
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMKRLEHRRELEKQ--- 298
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 597837628 339 mdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE 383
Cdd:pfam13868 299 --IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
265-527 |
3.64e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELE-WQQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDkLQEELEQLREELEQAREELEQLEE------ELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELlrqqevaLQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:COG4372 93 QAELAQAQEELESLQEEAEEL-------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 424 IARQHAERQRKEEEARRQEEARLFAE-RQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQ 502
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260
....*....|....*....|....*
gi 597837628 503 RKAEEERRIEEQLAAREVENQSTVV 527
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVE 270
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-484 |
3.95e-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: 50.84 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 196 MSEDefLKQLVRIVEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQ------ 269
Cdd:TIGR02169 679 LRER--LEGLKRELSSLQSELRRIENRLDELSQE--LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSleqeie 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 270 ----EIARQVAERQQKEREELEWQQEIARQEAER-----QRKEEEMRRQQEYAQ----QMAEMQRAQKEMEWQREIARQK 336
Cdd:TIGR02169 755 nvksELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEmdeKEKQRQVEIARQMAERQRQEEEL-LRQQEVALQEAERQKKERE---RQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:TIGR02169 835 IQ---ELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 413 MEKKE-RERQQEIARQHAE----------RQRKEEEARRQEEARLFAERQKKERERQ--------------EEIARQMEE 467
Cdd:TIGR02169 912 IEKKRkRLSELKAKLEALEeelseiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeyeEVLKRLDEL 991
|
330
....*....|....*..
gi 597837628 468 EEKRQREEAEKEEMRKR 484
Cdd:TIGR02169 992 KEKRAKLEEERKAILER 1008
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
274-405 |
4.15e-06 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 47.17 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 274 QVAERQQKEREELEWQQEIARQEAERqrkeEEMRRQQEyaQQMAEMQRAQkEMEWQREIARQKAEMDEKEKQRQVEIARQ 353
Cdd:pfam12474 2 QLQKEQQKDRFEQERQQLKKRYEKEL----EQLERQQK--QQIEKLEQRQ-TQELRRLPKRIRAEQKKRLKMFRESLKQE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 597837628 354 MAERqRQEEELLRQQEvaLQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:pfam12474 75 KKEL-KQEVEKLPKFQ--RKEAKRQRKEELELEQKHEELEFLQAQSEALERE 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-512 |
4.45e-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: 50.84 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQ---EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR--QQEYAQQMAEMQRAQKEMEW---- 328
Cdd:TIGR02169 230 KEKEALERQKEAierQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASlers 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQ--EVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEK 406
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 407 ARKKSEMEKKERE-------RQQEIARQHAERQRKEEEARRQEEARL--FAERQKKERERQEEIARQMEEEEKRQREEAE 477
Cdd:TIGR02169 390 YREKLEKLKREINelkreldRLQEELQRLSEELADLNAAIAGIEAKIneLEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270
....*....|....*....|....*....|....*....
gi 597837628 478 KEEMRKRKIEE----ERLRKEEEQRIEAQRKAEEERRIE 512
Cdd:TIGR02169 470 ELYDLKEEYDRvekeLSKLQRELAEAEAQARASEERVRG 508
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
314-409 |
5.27e-06 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 46.80 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 314 QQMAEMQRAQKEME-----WQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEI 388
Cdd:pfam03938 12 EESPEGKAAQAQLEkkfkkRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
|
90 100
....*....|....*....|.
gi 597837628 389 ARQVVERKKQEEVRRIEKARK 409
Cdd:pfam03938 92 LLQPIQDKINKAIKEVAKEKG 112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-432 |
5.32e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQRQQeiARQVAERQQKEREELewQQEIARQEAERQRKEEEMrrqqeyAQQMAEMQRAQKEMEW------ 328
Cdd:COG3883 41 ALQAELEELNEEYNE--LQAELEALQAEIDKL--QAEIAEAEAEIEERREEL------GERARALYRSGGSVSYldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 --------------QREIARQKAEMDE-KEKQRQVEIARQMAERQRQE-EELLRQQEVALQEAERQKKERERQ-KEIARQ 391
Cdd:COG3883 111 sesfsdfldrlsalSKIADADADLLEElKADKAELEAKKAELEAKLAElEALKAELEAAKAELEAQQAEQEALlAQLSAE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 597837628 392 VVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-464 |
5.52e-06 |
|
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: 49.76 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEeemRRQQEYAQQMAEMQRAQKEMewQRE 331
Cdd:COG4942 17 AQADAAAEAEAELeqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAEL--EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQ-RQVEIARQMAERQRQEEELLRQQEVAlqeaerqkkERERQKEIARQVVERKKQeevrRIEKARKK 410
Cdd:COG4942 92 IAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFL---------DAVRRLQYLKYLAPARRE----QAEELRAD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 597837628 411 SEmEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:COG4942 159 LA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
318-423 |
6.11e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 318 EMQRAQKEMEWQR-EIARQKAEmdeKEKQrqvEIARQMAERQRQEEELLRQQEVALQEAERQKKE---------RERQKE 387
Cdd:PRK00409 526 EELERELEQKAEEaEALLKEAE---KLKE---ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 597837628 388 IARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-521 |
6.24e-06 |
|
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: 49.38 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 288 WQQEIARQEAERQRKEeemrRQQEYAQQMAEMQRAQKEmewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELlrq 367
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAEL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKERERQKEIARQVVERKKQEEVRRI----------EKARKKSEMEKKERERQQEIARQHAERQRKEEE 437
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 438 ARRqeearLFAERQKKERERQEEIARQmeeeekrQREEAEKEEmrKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAA 517
Cdd:COG4942 166 RAE-----LEAERAELEALLAELEEER-------AALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....
gi 597837628 518 REVE 521
Cdd:COG4942 232 LEAE 235
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
259-416 |
6.85e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQE--AERQRK-EEEMRRQQEYAQQMAEMQRA-QKEMEWQREIAR 334
Cdd:PRK10929 193 ELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQlnSQRQREaERALESTELLAEQSGDLPKSiVAQFKINRELSQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 ----QKAEMDE-KEKQRQveiARQMAERQRQEEELLRQQ------EVALQEAERQKKER--ERQK------EIARQVVER 395
Cdd:PRK10929 273 alnqQAQRMDLiASQQRQ---AASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARlpEMPKpqqldtEMAQLRVQR 349
|
170 180
....*....|....*....|.
gi 597837628 396 KKQEEVrrIEKARKKSEMEKK 416
Cdd:PRK10929 350 LRYEDL--LNKQPQLRQIRQA 368
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
208-432 |
7.09e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 208 IVEAHQVAINKIEEQVGEERR----RGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEM--EQLERQRQQ------EIARQV 275
Cdd:PRK10929 46 IVEALQSALNWLEERKGSLERakqyQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstDALEQEILQvssqllEKSRQA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 276 AERQQKERE------ELEWQQEiarqEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKemewQREIARQKAEMDEKE---- 343
Cdd:PRK10929 126 QQEQDRAREisdslsQLPQQQT----EARRQLNEIERRLQTLGTPNtpLAQAQLTAL----QAESAALKALVDELElaql 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 --KQRQvEIARQMAE-RQRQEEEL-LRQQEVALQEAERQKKERERQKEIARQVVERKKQ---EEVRRIEKARKKSEMEKK 416
Cdd:PRK10929 198 saNNRQ-ELARLRSElAKKRSQQLdAYLQALRNQLNSQRQREAERALESTELLAEQSGDlpkSIVAQFKINRELSQALNQ 276
|
250
....*....|....*.
gi 597837628 417 ERERQQEIARQhaERQ 432
Cdd:PRK10929 277 QAQRMDLIASQ--QRQ 290
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
258-464 |
7.69e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMR-RQQEYA-QQMAEMQRAQKEMEWQR----- 330
Cdd:pfam15558 72 ARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRkQCQEQRlKEKEEELQALREQNSLQlqerl 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQKAEMDEKEKQRQV------EIARQMA-----ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVER--KK 397
Cdd:pfam15558 152 EEACHKRQLKEREEQKKVqennlsELLNHQArkvlvDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKaqKE 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 398 QEEVRRIEKARKKSEMEKKER--------ERQQEIARQHAERQRKEEEARrqeearlfAERQKKERERQEEIARQ 464
Cdd:pfam15558 232 EEQFQRAKWRAEEKEEERQEHkealaelaDRKIQQARQVAHKTVQDKAQR--------ARELNLEREKNHHILKL 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-462 |
7.88e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKE-MEWQREIARQKAEMDE-- 341
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------EIDKLQAEiAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQ----------------------VEIARQMAERQRqeeELLRQQEVALQEAERQKKERERQKEIARQVV----ER 395
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsdfldrLSALSKIADADA---DLLEELKADKAELEAKKAELEAKLAELEALKaeleAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 396 KKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIA 462
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-426 |
7.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM-----RRQQEYAQQMAEMQRAQKEMEWQREI 332
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGeggsaGGSLTGGSRRELLAALLEAEAELEEL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
170
....*....|....
gi 597837628 413 MEKKERERQQEIAR 426
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
343-464 |
7.98e-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: 46.57 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 EKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQ 422
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQE 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 597837628 423 EIARQHAERQRKEEEArrqeearlfAERQKKERER---QEEIARQ 464
Cdd:pfam05672 98 RLQKQKEEAEAKAREE---------AERQRQEREKimqQEEQERL 133
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
314-424 |
8.21e-06 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 47.14 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 314 QQMAEMQRAQKEMEwqreiarqkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVaLQEAERQKKERErqkeIarqvv 393
Cdd:COG2825 36 QESPEGKAAQKKLE-------------KEFKKRQAELQKLEKELQALQEKLQKEAAT-LSEEERQKKERE----L----- 92
|
90 100 110
....*....|....*....|....*....|.
gi 597837628 394 eRKKQEEVRRIEKARKKsEMEKKERERQQEI 424
Cdd:COG2825 93 -QKKQQELQRKQQEAQQ-DLQKRQQELLQPI 121
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
258-564 |
8.50e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREE--LEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQ 335
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREAKAEAEQraAELAAEAAKKLAEAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEK 415
Cdd:COG3064 118 EKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 416 KERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEE 495
Cdd:COG3064 198 AAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSG 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 496 EQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDATKTVLAG 564
Cdd:COG3064 278 LVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAA 346
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
304-464 |
8.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE 383
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEiARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER-RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
.
gi 597837628 464 Q 464
Cdd:COG4913 399 E 399
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
259-416 |
9.47e-06 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 47.37 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIA-RQEAERQRKEEEMRRQQEYAQQMAEMQRaqKEMEWQREIARqka 337
Cdd:pfam01991 1 FIRQEAEEKAEEIRAKAEEEFAIEKAELVQEAEEKiDEIYEKKEKQAEMQKKIIISNAKNEARL--KVLEAREEILD--- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEevrrIEKARKKSEMEKK 416
Cdd:pfam01991 76 EVFNEAEKKLAELEEDTDEYKDLLRKLIVQALVKLGEPEVIVRCRKRDEELVESALDKAAEE----YKAKTKKVTVEKA 150
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-410 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKER--EELEW---QQEIARQEAERQRKE------EEMRRQQEYAQqmAEMQRAQKE 325
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYswDEIDVasaEREIAELEAELERLDassddlAALEEQLEELE--AELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 326 mewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEvRRIE 405
Cdd:COG4913 708 ---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR-ARLN 783
|
....*
gi 597837628 406 KARKK 410
Cdd:COG4913 784 RAEEE 788
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
266-357 |
1.16e-05 |
|
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: 45.51 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQV--AERQQKEREEL--EWQQEI--ARQEAERQRKEEEMRRQQEYAQQMAEMQR-AQKEME-WQREIARQKA 337
Cdd:cd06503 30 EREEKIAESLeeAEKAKEEAEELlaEYEEKLaeARAEAQEIIEEARKEAEKIKEEILAEAKEeAERILEqAKAEIEQEKE 109
|
90 100
....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAER 357
Cdd:cd06503 110 KALAELRKEVADLAVEAAEK 129
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
290-432 |
1.39e-05 |
|
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: 47.23 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 290 QEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEmEWQREIARQKAEMDEKEKQRQVEIARQMAER-QRQEEELlrQQ 368
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEAL--QK 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 369 EVALQEAERQKKErERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:COG1579 97 EIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
261-369 |
1.58e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 44.91 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIAR--QVAERQQKEREELEWQQEIARQ-EAERQRKEEEMRRQQEYAQQMAEMQR-----AQKEMEWQREI 332
Cdd:pfam20492 2 EEAEREKQELEERlkQYEEETKKAQEELEESEETAEElEEERRQAEEEAERLEQKRQEAEEEKErleesAEMEAEEKEQL 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 597837628 333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQE 369
Cdd:pfam20492 82 EAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
265-430 |
1.62e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQE---AERQRKEEEMRRQQEyaqqmaEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKElllRERNQQRQEARRERE------ELQREEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKErERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQ 421
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPE-QARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
170
....*....|..
gi 597837628 422 ---QEIARQHAE 430
Cdd:PRK12705 181 ilaQAMQRIASE 192
|
|
| CCDC50_N |
pfam15295 |
Coiled-coil domain-containing protein 50 N-terminus; |
329-403 |
1.63e-05 |
|
Coiled-coil domain-containing protein 50 N-terminus;
Pssm-ID: 464621 [Multi-domain] Cd Length: 126 Bit Score: 45.10 E-value: 1.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ-QEVALQEAERQKKERERQKEIARQVVERKKQEEVRR 403
Cdd:pfam15295 50 QNDIRVAKQLQEEEELQAQTLFQRRLAQLEEQDEEIAKEiQEELQREAEERRRREEEDEEIARQLQERERERERRR 125
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
261-367 |
1.68e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEeemrrqqeyaQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALE----------GLAAELEEKQQELEAQLEQLQEKAAET 210
|
90 100
....*....|....*....|....*...
gi 597837628 341 EKE-KQRQVEIARQMAERQRQEEELLRQ 367
Cdd:PRK11448 211 SQErKQKRKEITDQAAKRLELSEEETRI 238
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
276-394 |
1.74e-05 |
|
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: 45.12 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 276 AERQQKEREELEwQQEIARQEAERQrkeeemrrQQEYAQQMAEmqrAQKEMEWQREIARQKAemdEKEKQRQVEIARQMA 355
Cdd:cd06503 29 DEREEKIAESLE-EAEKAKEEAEEL--------LAEYEEKLAE---ARAEAQEIIEEARKEA---EKIKEEILAEAKEEA 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 597837628 356 ERQRQEEellrQQEValqEAERQKKERERQKEIARQVVE 394
Cdd:cd06503 94 ERILEQA----KAEI---EQEKEKALAELRKEVADLAVE 125
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
266-463 |
2.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQVAERQQKEREELEWQQEIAR----QEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KeKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERErqkEIARQVVERKKQEEVRRIEKARKksEMEKKERERQ 421
Cdd:COG4717 379 A-GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE---ELLEALDEEELEEELEELEEELE--ELEEELEELR 452
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 597837628 422 QEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
259-411 |
2.36e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQE------------------YAQQMAEMQ 320
Cdd:pfam05262 205 ERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknlpkpadtsspkedkqvAENQKREIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 321 RAQKEmewqreiARQKAEMDEKEKQRQVEIARQMAERQRQEEEllrqqevalQEAERQKKERERQKEIARQVVERKKQEE 400
Cdd:pfam05262 285 KAQIE-------IKKNDEEALKAKDHKAFDLKQESKASEKEAE---------DKELEAQKKREPVAEDLQKTKPQVEAQP 348
|
170
....*....|.
gi 597837628 401 VRRIEKARKKS 411
Cdd:pfam05262 349 TSLNEDAIDSS 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-518 |
2.40e-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: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQRE 331
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERL 491
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
250 260
....*....|....*....|....*..
gi 597837628 492 RKEEEQRIEAQRKAEEERRIEEQLAAR 518
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERE 768
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
298-524 |
2.52e-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: 48.04 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 298 ERQRKEEEMRRQQEYaqqMAEMQRAQKEME----------WQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL--- 364
Cdd:pfam02463 154 RRLEIEEEAAGSRLK---RKKKEALKKLIEetenlaeliiDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyld 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 365 ---LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRI--EKARKKSEMEKK-----ERERQQEIARQHAERQRK 434
Cdd:pfam02463 231 ylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkEEEKEKKLQEEElkllaKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 435 EEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRK------RKIEEERLRKEEEQRIEAQRKAEEE 508
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEeleklqEKLEQLEEELLAKKKLESERLSSAA 390
|
250
....*....|....*.
gi 597837628 509 RRIEEQLAAREVENQS 524
Cdd:pfam02463 391 KLKEEELELKSEEEKE 406
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
220-521 |
2.57e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 220 EEQVGEERRRGGVEDhehpagsFRKQGPSGnfEEGSSNAEMEQLERQRQQEIARQVAERQQKEREE----LEWQQEiaRQ 295
Cdd:pfam02029 4 EEEAARERRRRAREE-------RRRQKEEE--EPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAK--RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqREIARQKAEMDEKEKQRQVEIARQMAE----RQRQEEELLRQQEVA 371
Cdd:pfam02029 73 ERRQKRLQEALERQKEFDPTIADEKESVAERK--ENNEEEENSSWEKEEKRDSRLGRYKEEeteiREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 372 lQEAERQKKERERQKEIARQVVERKKQEEVR--RIEKARKKSEMEKKERERQQEIARQHAE------------------- 430
Cdd:pfam02029 151 -QAEEEGEEEEDKSEEAEEVPTENFAKEEVKdeKIKKEKKVKYESKVFLDQKRGHPEVKSQngeeevtklkvttkrrqgg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 431 ---RQRKEEEARRQEEARLFAERQKK---ERERQE-EIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQR 503
Cdd:pfam02029 230 lsqSQEREEEAEVFLEAEQKLEELRRrrqEKESEEfEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKL 309
|
330
....*....|....*....
gi 597837628 504 KAEEE-RRIEEQLAAREVE 521
Cdd:pfam02029 310 REEEEkRRMKEEIERRRAE 328
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
266-357 |
2.59e-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: 45.16 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQV--AERQQKEREEL--EWQQEI--ARQEAERQRKE--EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA 337
Cdd:COG0711 31 ERQEKIADGLaeAERAKEEAEAAlaEYEEKLaeARAEAAEIIAEarKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERA 110
|
90 100
....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAER 357
Cdd:COG0711 111 KALAELRAEVADLAVAIAEK 130
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
252-389 |
2.61e-05 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 46.93 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE-----MQRAQKEM 326
Cdd:PRK06669 56 EAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEgyeegYEKGREEG 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 327 EwqreiarqkAEMDEKEKQRQVEIARQMAERQRQ----EEELLrqqEVALQEAERQKKER-ERQKEIA 389
Cdd:PRK06669 136 L---------EEVRELIEQLNKIIEKLIKKREEIlessEEEIV---ELALDIAKKVIKEIsENSKEIA 191
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
251-431 |
2.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKEREEL--------EWQQ---EIARQEAERQRKEEEMRRQQEYAQQMAEM 319
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrieELQEllrEAEELEEELQLEELEQEIAALLAEAGVED 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 --------QRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ 391
Cdd:COG4717 384 eeelraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 597837628 392 VVERKKQEEVRRIEKARKKSEMEKKERERQ-QEIARQHAER 431
Cdd:COG4717 464 QLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEE 504
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
266-432 |
2.77e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.09 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQVAERQ-QKEREELEWQQEIARQEAERQRKEeemrrqqeYAQQMAEMQRAQKEMEwQREIARQKAEMDEKEK 344
Cdd:PTZ00491 662 KSQEAAARHQAELLeQEARGRLERQKMHDKAKAEEQRTK--------LLELQAESAAVESSGQ-SRAEALAEAEARLIEA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 QRQVEIARQMAERQRQEEEllrqqevALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEI 424
Cdd:PTZ00491 733 EAEVEQAELRAKALRIEAE-------AELEKLRKRQELELEYEQAQNELEIAKAKELADIEATKFERIVEALGRETLIAI 805
|
....*...
gi 597837628 425 ARQHAERQ 432
Cdd:PTZ00491 806 ARAGPELQ 813
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
258-365 |
3.10e-05 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 47.20 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQ-----EI-----------ARQVAERQ---------------QKEREELEWQQEIARQEAERQRkEEEM 306
Cdd:pfam05914 219 AERRRLEKRQEQednlaEIynhltsdllteNPEVAQSSlgphrvipdrwkgmsPEQLKEIRKEQEQQREEKERRR-EEEK 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 307 RRQQEYAQQMAEMQRAQkeMEWQREIARQKAEMdekeKQRQVEIARQMAERQRQEEELL 365
Cdd:pfam05914 298 QRDAEWDRQRLELARAA--LLLEREQQRLRREL----RRQLDEENLQLAQEQKARQEYL 350
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
259-401 |
3.24e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.82 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQKEREELE---WQQEIARQEAERQRKE-----EEMRRQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:pfam07111 513 EQGEAERQQLSEVAQQLEQELQRAQESLAsvgQQLEVARQGQQESTEEaaslrQELTQQQEIYGQALQEKVAEVETRLRE 592
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 331 EIARQKAEMDE--KEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERERqkeIARQVVERKKQEEV 401
Cdd:pfam07111 593 QLSDTKRRLNEarREQAKAVVSLRQIQHRATQEKE--RNQELRRLQDEARKEEGQR---LARRVQELERDKNL 660
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
264-547 |
4.06e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.51 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKErEELEWqqeiARQEAERQRKE-----EEMRRQQEYA----QQMAEMQRAQKEMEWQREIAR 334
Cdd:NF041483 505 ERVRTEAIERATTLRRQAE-ETLER----TRAEAERLRAEaeeqaEEVRAAAERAarelREETERAIAARQAEAAEELTR 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEK--EKQRQVEIARQMAERQRQE--EELLRQQEVA------LQEAERQKKERERQKEIARQVVERKKQEEVRRI 404
Cdd:NF041483 580 LHTEAEERltAAEEALADARAEAERIRREaaEETERLRTEAaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAVR 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 405 EKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERqeeiaRQMEEEEKRQREEAEKEEMRKR 484
Cdd:NF041483 660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRR-----REAEETLGSARAEADQERERAR 734
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 485 KIEEERLRKEEEQRIEAQRKA-----EEERRIEEQLAAREVENQStVVNPAFGMH------IPGETQAGEHSTD 547
Cdd:NF041483 735 EQSEELLASARKRVEEAQAEAqrlveEADRRATELVSAAEQTAQQ-VRDSVAGLQeqaeeeIAGLRSAAEHAAE 807
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
258-405 |
4.14e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQ----------QEIARQVAERQQKEREELEwqqeiarQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEME 327
Cdd:COG3096 522 AELEQRLRQQQnaerlleefcQRIGQQLDAAEELEELLAE-------LEAQLEELEEQAAEAVE---QRSELRQQLEQLR 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 328 WQREIARQKAEMDEKekqrqveiARQMAERQRQE--EELLRQQEValQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:COG3096 592 ARIKELAARAPAWLA--------AQDALERLREQsgEALADSQEV--TAAMQQLLEREREATVERDELAARKQALESQIE 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-522 |
4.32e-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: 47.37 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 247 PSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQK-EREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQK 324
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDaSRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 325 EMEWQREIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIarqvveRKKQEEVRRI 404
Cdd:TIGR02169 731 EEEKLKERLEELEE-DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 405 EKARkkSEMEKKERERQQEIARQHAERQrkeeearrqeearlFAERQKKERERQeeiarqmeeeekrqREE-AEKEEMRK 483
Cdd:TIGR02169 804 EEEV--SRIEARLREIEQKLNRLTLEKE--------------YLEKEIQELQEQ--------------RIDlKEQIKSIE 853
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 597837628 484 RKIEEERLRKEEEQRiEAQRKAEEERRIEEQLA--AREVEN 522
Cdd:TIGR02169 854 KEIENLNGKKEELEE-ELEELEAALRDLESRLGdlKKERDE 893
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
271-416 |
4.40e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 271 IARQVAERQQKEREELEwqQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKE-MEWQREIARQKAEMDEKEKqrqvE 349
Cdd:COG2433 382 LEELIEKELPEEEPEAE--REKEHEERELTEEEEEIRRLEE------QVERLEAEvEELEAELEEKDERIERLER----E 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 350 IARqmaERQRQEEELLRQQEValqeaerqkkeRERQKEIARqvVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:COG2433 450 LSE---ARSEERREIRKDREI-----------SRLDREIER--LERELEEERERIEELKRKLERLKE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
294-523 |
4.42e-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: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 294 RQEAERQRK--EEEMRR----QQEYAQQMAEMQRaqkemewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ 367
Cdd:COG1196 174 KEEAERKLEatEENLERlediLGELERQLEPLER-------QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKsemekkERERQQEIARQHAERQRKeeearrqeearlf 447
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARL------------- 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 448 AERQKKERERQEEIARQmeeeekrqreeaekeemrkrkieEERLRkEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196 308 EERRRELEERLEELEEE-----------------------LAELE-EELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
273-455 |
4.68e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.05 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 273 RQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ--EYAQQM-AEMQRAQKEM-----------EWQREIARQKAE 338
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQlsEVAQQLeQELQRAQESLasvgqqlevarQGQQESTEEAAS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 339 MDEKEKQRQVEIARQMAERQRQEEELLRQQevaLQEAERQKKERERQKEIA----RQVvERKKQEEVRRIEKARKKSEME 414
Cdd:pfam07111 564 LRQELTQQQEIYGQALQEKVAEVETRLREQ---LSDTKRRLNEARREQAKAvvslRQI-QHRATQEKERNQELRRLQDEA 639
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 597837628 415 KKerERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER 455
Cdd:pfam07111 640 RK--EEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQR 678
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-521 |
4.91e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 291 EIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL---LRQ 367
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKE-RERQKEIARQVVE----RKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERqrkeeearrqe 442
Cdd:PRK03918 257 LEEKIRELEERIEElKKEIEELEEKVKElkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----------- 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 443 earlfAERQKKERERQEEIARQMeeeekrqreEAEKEEMRKRKIEEERLRKEEEqriEAQRKAEEERRIEEQLAAREVE 521
Cdd:PRK03918 326 -----IEERIKELEEKEERLEEL---------KKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE 387
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
265-423 |
5.46e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.64 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAE-RQQKEREELEWQQEIARQEAERQRKEEEMRRQQ--------EYAQQMAEMQRAQKEMEWQREIA-- 333
Cdd:pfam03528 7 QQRVAELEKENAEfYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNavlqeaqvELDALQNQLALARAEMENIKAVAtv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 ----RQKAeMDEKEKQRQVEIArqmaERQRQEEELLRQQEValQEAERQKKERERQKEIaRQVVERKKQEEVRRIEKARK 409
Cdd:pfam03528 87 sentKQEA-IDEVKSQWQEEVA----SLQAIMKETVREYEV--QFHRRLEQERAQWNQY-RESAEREIADLRRRLSEGQE 158
|
170
....*....|....
gi 597837628 410 KSEMEKKERERQQE 423
Cdd:pfam03528 159 EENLEDEMKKAQED 172
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
314-407 |
5.50e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 43.73 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 314 QQMAEMQRAQKEMEwqREIARQKAEMDEKEKQrqveiARQMAERQRQEEELLRQQEVALQEAERQKKERE--RQKEIARQ 391
Cdd:smart00935 11 QESPAGKAAQKQLE--KEFKKRQAELEKLEKE-----LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEfqRKQQKLQQ 83
|
90
....*....|....*.
gi 597837628 392 VVERKKQEEVRRIEKA 407
Cdd:smart00935 84 DLQKRQQEELQKILDK 99
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
258-379 |
8.21e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQ-EIARQVAERQQKE--REELEwqqEIARQEAERQRKEEEMRRQQEyaqqmAEMQRAQKEMEWQREIAR 334
Cdd:COG0542 411 EELDELERRLEQlEIEKEALKKEQDEasFERLA---ELRDELAELEEELEALKARWE-----AEKELIEEIQELKEELEQ 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 335 QKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVA-------------LQEAERQK 379
Cdd:COG0542 483 RYGKIPELEKELA-ELEEELAELAPLLREEVTEEDIAevvsrwtgipvgkLLEGEREK 539
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
293-397 |
8.59e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 43.33 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 293 ARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVAL 372
Cdd:pfam03938 16 EGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQ------KDGALLEEEREEKEQELQKKEQELQQLQQK--AQQELQK 87
|
90 100
....*....|....*....|....*
gi 597837628 373 QEAERQKKERERQKEIARQVVERKK 397
Cdd:pfam03938 88 KQQELLQPIQDKINKAIKEVAKEKG 112
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
265-486 |
8.86e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.09 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEReelewqqeiARQ--EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEK 342
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEE---------AKArfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 EKQRQVEIARQ------MAERQ-RQEEELLRQQEVALQEAERQKKErERQKEIARqvVERKKQEevRRIEKARKKSEMEK 415
Cdd:PRK05035 503 TQPIVIKAGARpdnsavIAAREaRKAQARARQAEKQAAAAADPKKA-AVAAAIAR--AKAKKAA--QQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 416 KERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKI 486
Cdd:PRK05035 578 KKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
269-527 |
9.74e-05 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 46.34 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVA---ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQ 345
Cdd:COG2203 334 EALADQAAiaiERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 346 RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:COG2203 414 GLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLL 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 426 RQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKA 505
Cdd:COG2203 494 LLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLS 573
|
250 260
....*....|....*....|..
gi 597837628 506 EEERRIEEQLAAREVENQSTVV 527
Cdd:COG2203 574 VLLIELALALILALALLELLLV 595
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
310-523 |
1.12e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 310 QEYAQQMAEMQRAQKEMEWQREIArQKAEMDEKEKQRQVEIARQM-AERQRQEEELLRQQEVALQEAERQKKERERQKEI 388
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIA-EKKRIKAEEKEEERRLDEMMeEERERALEEEEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 389 ARQvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:pfam13868 85 REQ--KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERriEEQLAAREVENQ 523
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER--DELRAKLYQEEQ 215
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
292-411 |
1.31e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 45.88 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 292 IARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKemewqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEELLrqqeva 371
Cdd:PTZ00266 430 VDKDHAERARIEKENAHRKALEMKILEKKRIER---------LEREERERLERERMERIERERLERERLERERL------ 494
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 597837628 372 lqeaERQKKERERQKEIARQVVERKKQEevrRIEKARKKS 411
Cdd:PTZ00266 495 ----ERDRLERDRLDRLERERVDRLERD---RLEKARRNS 527
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
340-518 |
1.53e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 340 DEKEKQRQV-EIARQMA-ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVverKKQEEVRRIEKARKKSEMEKKE 417
Cdd:TIGR02794 44 DPGAVAQQAnRIQQQKKpAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA---AAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 418 ----RERQQEIARQHAE---RQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEK--EEMRKRKIEE 488
Cdd:TIGR02794 121 aeeaKAKQAAEAKAKAEaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKakAEEAKAKAEA 200
|
170 180 190
....*....|....*....|....*....|
gi 597837628 489 ERLRKEEeqriEAQRKAEEERRIEEQLAAR 518
Cdd:TIGR02794 201 AKAKAAA----EAAAKAEAEAAAAAAAEAE 226
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
257-334 |
1.54e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 42.56 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKEREeleWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR 334
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAKQKELQKLYEE---LQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQP 95
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
355-431 |
1.67e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 45.50 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQ--EVALQEAER-QKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAER 431
Cdd:PTZ00266 435 AERARIEKENAHRKalEMKILEKKRiERLEREERERLERERMERIERERLERERLERERLERDRLERDRLDRLERERVDR 514
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
343-535 |
1.73e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 EKQRQVEIARQMAE-RQRQEEELLRQQEVALQEAERQKKERERQK----------EIARQVVERKKQEEVRRIEKARKKS 411
Cdd:pfam05262 189 DNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQIDADKAQqkadfaqdnaDKQRDEVRQKQQEAKNLPKPADTSS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEkEEMRKRKieeerl 491
Cdd:pfam05262 269 PKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVA-EDLQKTK------ 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 597837628 492 rkeeeQRIEAQRKAEEERRIEEqlaarevenqstvVNPAFGMHI 535
Cdd:pfam05262 342 -----PQVEAQPTSLNEDAIDS-------------SNPVYGLKV 367
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
278-395 |
1.74e-04 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 42.69 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 278 RQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEK---------EKQRQV 348
Cdd:TIGR02473 12 EKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqqqelaLLQQEV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 597837628 349 EIARQMAERQRQEE---ELLRQQEVALQEAERQKKERERQKEIARQVVER 395
Cdd:TIGR02473 92 EAKRERLLEARRELkalEKLKEKKQKEYRAEEAKREQKEMDELATQRFRR 141
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
344-425 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQM--AERQRQE-EELLRQQEVALQEAERQKKE-----RERQKEIARQVVERKKQEEVRRIEKARKKSEMEK 415
Cdd:cd06503 29 DEREEKIAESLeeAEKAKEEaEELLAEYEEKLAEARAEAQEiieeaRKEAEKIKEEILAEAKEEAERILEQAKAEIEQEK 108
|
90
....*....|..
gi 597837628 416 KE--RERQQEIA 425
Cdd:cd06503 109 EKalAELRKEVA 120
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-523 |
1.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVErKKQEEVRRIEKARKKSEM 413
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 414 EKKERERQQEIAR-----QHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:COG4717 131 YQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|....*
gi 597837628 489 ERLRKEEEQRiEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG4717 211 LEEELEEAQE-ELEELEEELEQLENELEAAALEER 244
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
241-425 |
1.84e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.02 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 241 SFRKQGPSG-NFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEiARQEAERQRKEEEMRRQQEYAQQMAEM 319
Cdd:pfam05667 283 SFSGSSTTDtGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQRE-EELEELQEQLEDLESSIQELEKEIKKL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 QRAQKEMEwqREIARQKAEMDEKEKqrQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIAR----QVVER 395
Cdd:pfam05667 362 ESSIKQVE--EELEELKEQNEELEK--QYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRA 437
|
170 180 190
....*....|....*....|....*....|
gi 597837628 396 KKQEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:pfam05667 438 LKEAKSNKEDESQRKLEEIKELREKIKEVA 467
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
274-481 |
1.87e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 274 QVAERQQKEREELEWQQeiaRQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEM---DEKEKQRQVEI 350
Cdd:pfam10174 450 RIIERLKEQREREDRER---LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkDSKLKSLEIAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 351 ARQMAERQRQEEELLRQQEVALQE---AERQKKERERQKEIARQVVE-RKKQEEVRRIEKARKKSEMEKKERERQQEIAR 426
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVrtnPEINDRIRLLEQEVARYKEEsGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 427 QHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEM 481
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM 661
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
255-486 |
2.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEE------EMRRQQEYAQQ-MAEMQRAQKEME 327
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieELEKELESLEGsKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 328 WQREIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAE-RQKKERERQKEIARQVVER-KKQEEVRRIE 405
Cdd:PRK03918 266 ERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELeEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 406 KARKKSE---MEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMR 482
Cdd:PRK03918 345 KKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
....
gi 597837628 483 KRKI 486
Cdd:PRK03918 425 KKAI 428
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
336-395 |
2.23e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 45.25 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 336 KAEMDE--------KEKQRQVE-IARQMAERQRQ-EEELLRQQEVALQEAERQ--KKERERQKEIARQVVER 395
Cdd:PLN02316 238 EGGMDEhsfedfllEEKRRELEkLAKEEAERERQaEEQRRREEEKAAMEADRAqaKAEVEKRREKLQNLLKK 309
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
96-341 |
2.29e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 96 PEPTTVRPYRPVFTTPNrKIVSSAATKSPKPPPTRTTATTLTTPPLKNRKVTEPIPVSEAQMTGMQPSTRGYTRGPQMHT 175
Cdd:NF033875 50 PGTTTVQPDNPDPQSGS-ETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 176 tgVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEAHQVAINKieeQVGEERRRGGVEDHEHPAGSFrkqGPSGNFEEGS 255
Cdd:NF033875 129 --VVSPETTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDK---AVDEAKKDPNITVVEKPAEDL---GNVSSKDLAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 256 SNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEI-ARQEAERQRKEEEMRRQQEYAQQMAEMQRA-QKEMEWQREIA 333
Cdd:NF033875 201 KEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIaAKNKAEKERYEKEVAEYNKHKNENGYVNEAiSKNLVFDQSVV 280
|
....*...
gi 597837628 334 RQKAEMDE 341
Cdd:NF033875 281 TKDTKISS 288
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
257-370 |
2.31e-04 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 43.38 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQvAERQQKEREELEWQQEIARQEAERQRKEEemrrqqeyaQQMAEMQRAQKEMEwQREI--AR 334
Cdd:pfam06391 67 EKKIEQYEKENKDLILKN-KMKLSQEEEELEELLELEKREKEERRKEE---------KQEEEEEKEKKEKA-KQELidEL 135
|
90 100 110
....*....|....*....|....*....|....*...
gi 597837628 335 QKAEMDEKE--KQRQVEIARQMAERQRQEEELLRQQEV 370
Cdd:pfam06391 136 MTSNKDAEEiiAQHKKTAKKRKSERRRKLEELNRVLEQ 173
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
657-696 |
2.65e-04 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 39.35 E-value: 2.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 597837628 657 PHPNDATRYLQCTPmigrrGRWTERMCPPNLVFIPSYGRC 696
Cdd:smart00494 12 PHPTDCSKYYQCSN-----GRPIVGSCPAGLVFNPATQTC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-464 |
2.66e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIA 333
Cdd:COG4372 107 QEEAEELQEEleeLQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEM 413
Cdd:COG4372 187 EL-----LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 597837628 414 EKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
357-422 |
2.68e-04 |
|
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: 44.10 E-value: 2.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 357 RQRQEEELLRQQEVALQEAERQKKErerqkeiarqvvERKKQEEVRRIEK----ARKKseMEKKERERQQ 422
Cdd:pfam07946 266 REEEIEKIKKAAEEERAEEAQEKKE------------EAKKKEREEKLAKlspeEQRK--YEEKERKKEQ 321
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-366 |
2.74e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLE--RQRQQEIARQVAERQQKEREELEWQQEIARQEAE-RQRKEEEMRR-QQEYAQQMAEMQRAQKEME-WQRE 331
Cdd:COG4717 142 AELPERLEelEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDlAEELEELQQRLAELEEELEeAQEE 221
|
90 100 110
....*....|....*....|....*....|....*
gi 597837628 332 IARQKAEMDEKEKQRQVEiarQMAERQRQEEELLR 366
Cdd:COG4717 222 LEELEEELEQLENELEAA---ALEERLKEARLLLL 253
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
333-417 |
2.94e-04 |
|
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: 42.72 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 333 ARQKAEMDEKEKQRQ----VEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIekar 408
Cdd:pfam09756 5 AKKRAKLELKEAKRQqreaEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQ--ERKEQEEYEKL---- 78
|
....*....
gi 597837628 409 kKSEMEKKE 417
Cdd:pfam09756 79 -KSQFVVEE 86
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
245-521 |
3.16e-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: 44.57 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 245 QGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAE------RQRKEEEMRRQQEYAQQMAE 318
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlctPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 319 MQRAQKEMEWQREIARQKAEMDEKEKQRQveiarQMAERQRQEEELLRQQEVALqeaERQKKERERQKEIARQVVERKKQ 398
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQ-----QLLKQLRARIEELRAQEAVL---EETQERINRARKAAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 399 EEVRriekarkksemekkererqQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEK 478
Cdd:TIGR00618 303 TQIE-------------------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 597837628 479 EEMRKRKIEEERLRKEEEQRIEAQRKAEEERrieEQLAAREVE 521
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQK---LQSLCKELD 403
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
262-419 |
3.53e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.47 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAeMQRAQKEMEWQREIARQKAEmde 341
Cdd:PRK06669 13 NKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDA-FEIVEAAEEEAKEELLKKTD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 kEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE--MEKKERE 419
Cdd:PRK06669 89 -EASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKKREeiLESSEEE 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-515 |
3.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 292 IARQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEMEWQREIARQKAEMDEKE---KQRQVEIARQMAERQRqeeelLRQQ 368
Cdd:COG4913 612 LAALEAELAELEEELAEAEE---RLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELER-----LDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 369 EVALQEAERQKKERERQKEIARQvverkkqeevrRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFA 448
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEE-----------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 449 ERqkKERERQEEIARQMEEEekrqreeaekeemrkrkieeerlrkeeeqrIEAQRKAEEER--RIEEQL 515
Cdd:COG4913 753 ER--FAAALGDAVERELREN------------------------------LEERIDALRARlnRAEEEL 789
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
266-418 |
3.99e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQvAERQQKEREELEWQQEIARQEAERQRKE------------EEMRRQQEYAQQMAEMQRAQKEMEWQR--- 330
Cdd:PRK07735 9 DLKKEAARR-AKEEARKRLVAKHGAEISKLEEENREKEkalpknddmtieEAKRRAAAAAKAKAAALAKQKREGTEEvte 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 -EIARQKAEMDEKEKQRQVEIARQ--MAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIEKA 407
Cdd:PRK07735 88 eEKAKAKAKAAAAAKAKAAALAKQkrEGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTE--EVTEEEEETDKEKA 165
|
170
....*....|.
gi 597837628 408 RKKSEMEKKER 418
Cdd:PRK07735 166 KAKAAAAAKAK 176
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
255-330 |
4.36e-04 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 41.12 E-value: 4.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 255 SSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEemrrQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKREEREELFEERRAE----QIELRALEEKLELKELMETWHE 93
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
263-382 |
4.45e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.86 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 263 LERqRQQEIA---RQVAERQQKEREELEWQQE---IARQEAERQRKEeemrrqqeyAQQMAEMQRAQKEMEWQREIAR-- 334
Cdd:PRK07352 48 LEE-RREAILqalKEAEERLRQAAQALAEAQQklaQAQQEAERIRAD---------AKARAEAIRAEIEKQAIEDMARlk 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 597837628 335 QKAEMDEKekqrqveiarqmAERQRQEEELLRQ-QEVALQEAERQKKER 382
Cdd:PRK07352 118 QTAAADLS------------AEQERVIAQLRREaAELAIAKAESQLPGR 154
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
290-420 |
4.46e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.98 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 290 QEIARQEAERQRKEEEmrRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQE 369
Cdd:pfam11600 4 QKSVQSQEEKEKQRLE--KDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 597837628 370 VALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERER 420
Cdd:pfam11600 82 KAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
257-461 |
4.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLeRQRQQEIARQVAERQQKEREELEWQQEIARQEAERQ----RKEEEMRRQQEYAQQMAEMQRAQKEMEWQREI 332
Cdd:COG1340 84 NEKLNEL-REELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELVEKIKELEKELEKAKKALEKNEKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 333 ARQKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERErqkEIARQVVErkKQEEVRRIEKarKKSE 412
Cdd:COG1340 163 KELRAELKELRKEAE-EIHKKIKELAEEAQELHEEMIELYKEADELRKEAD---ELHKEIVE--AQEKADELHE--EIIE 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 597837628 413 MEKKERERQQEIARQHAERQRKEEearrqeearlfAERQKKERERQEEI 461
Cdd:COG1340 235 LQKELRELRKELKKLRKKQRALKR-----------EKEKEELEEKAEEI 272
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
263-460 |
4.74e-04 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 43.35 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 263 LERQRQQEIARQ----------------VAERQQKEREElewqqeiaRQEAERQRKE---EEMRRQQEYAQQM-AEMQRA 322
Cdd:pfam05914 9 IERRRQREEERKsrifnarnrtigvdveALDKQVEEKKR--------QEAAEKAREEafaEEMVQNDKIALMLeKREEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEME------WQREiarQKAEM---------DEKEKQRQVEIARQ------------MAERQRQEEELLRQQEVALQEA 375
Cdd:pfam05914 81 RRRLNkelnefRQQH---QRPETrrefdlndpDALKKDLPARVSDDdprcgpssmqkfEGEDLNREERKKLQQEQMREWL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 376 ERQKKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEIAR--------QHAERqrkeeearrqeearlf 447
Cdd:pfam05914 158 EQQIEEKKQAEEEEKH---AELLYDQKRLERDRRALELAKLEEECRRAVNAatknfnqaLAAEQ---------------- 218
|
250
....*....|...
gi 597837628 448 AERQKKERERQEE 460
Cdd:pfam05914 219 AERRRLEKRQEQE 231
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
258-432 |
4.81e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEI--ARQVAERQQKEREELEwQQEIARQEAERQRK---------EEEMRRQQ----EYAQQMAEMQRA 322
Cdd:pfam19220 118 AQAEALERQLAAETeqNRALEEENKALREEAQ-AAEKALQRAEGELAtarerlallEQENRRLQalseEQAAELAELTRR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEMEWQREIARQKAEMDEkekqrqVEIARQMAERQRQEEELLrqQEVALQEAERQKKERERQKEIAR---------QVV 393
Cdd:pfam19220 197 LAELETQLDATRARLRALE------GQLAAEQAERERAEAQLE--EAVEAHRAERASLRMKLEALTARaaateqllaEAR 268
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 597837628 394 E--RKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam19220 269 NqlRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERR 309
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
308-404 |
5.29e-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: 41.31 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 308 RQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEeellrqqevALQEAErqkKERERQKE 387
Cdd:COG0711 32 RQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEE---------AKAEAE---AEAERIIA 99
|
90 100
....*....|....*....|
gi 597837628 388 IARQVVERKKQ---EEVRRI 404
Cdd:COG0711 100 QAEAEIEQERAkalAELRAE 119
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
257-332 |
5.35e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 41.75 E-value: 5.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKErEELEwQQEIARQEAERQRKEEE-MRRQQEYAQQMAEMQR--AQKEMEWQREI 332
Cdd:COG2825 45 QKKLEKEFKKRQAELQKLEKELQALQ-EKLQ-KEAATLSEEERQKKERElQKKQQELQRKQQEAQQdlQKRQQELLQPI 121
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
253-414 |
5.45e-04 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 42.09 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 253 EGSSNAEMEQLERQRQQEIARQVAERQQKE-REELEWQQEIARQEAERQRKEEEMRRQQEYAQQmaemQRAQKEMEWQRE 331
Cdd:pfam14662 35 EETNAKLLEENLNLRKQAKSQQQAVQKEKLlEEELEDLKLIVNSLEEARRSLLAQNKQLEKENQ----SLLQEIESLQEE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQvEIARQMAERQRQEEELlrqQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:pfam14662 111 NKKNQAERDKLQKKKK-ELLKSKACLKEQLHSC---EDLACNRETILIEKTTQIEELKSTVEEYSSIEEELRAEKSRLES 186
|
...
gi 597837628 412 EME 414
Cdd:pfam14662 187 QLP 189
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
261-421 |
5.96e-04 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 463525 [Multi-domain] Cd Length: 428 Bit Score: 43.15 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEiaRQEAERQRKEEEMRR--QQEYAQ--QMAEMQRAQKEMEWQREIARQK 336
Cdd:pfam12297 209 GRLQEEYERKMAALAAECNLETREKMEAQHQ--REMAEKEEAEELLKHadEQEALEcsSLLDKLHKLEQEHLQRSLLLRQ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKekqrqveIARQMAERQRQEeeLLRQQEVALQEAERQKkerERQKEIARQVVERKKQ-----EEVRRIEKARKKS 411
Cdd:pfam12297 287 EEDFAK-------AQRQLAVFQRVE--LHKIFFTQLKEATRKG---ELKPEAAKRLLQDYSKiqeqiEELMDFFQANQRY 354
|
170
....*....|
gi 597837628 412 EMEKKERERQ 421
Cdd:pfam12297 355 HLSERFAQRE 364
|
|
| PRK14474 |
PRK14474 |
F0F1 ATP synthase subunit B; Provisional |
262-393 |
6.08e-04 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184696 [Multi-domain] Cd Length: 250 Bit Score: 42.50 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQkereelewQQEIARQEAERQRKEeemrrQQEYAQQMAEMqraqkemewqreIARQKAEMDE 341
Cdd:PRK14474 32 QVMKKRQQRIANRWQDAEQ--------RQQEAGQEAERYRQK-----QQSLEQQRASF------------MAQAQEAADE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 597837628 342 kEKQRQVEIARQMAERQRQE--EELLRQQEVALQEAerQKKERERQKEIARQVV 393
Cdd:PRK14474 87 -QRQHLLNEAREDVATARDEwlEQLEREKQEFFKAL--QQQTGQQMVKIIRAAL 137
|
|
| 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 ... |
308-395 |
6.24e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 40.76 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 308 RQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQE------EELLRQQEVALQEAERQKKE 381
Cdd:pfam00430 31 RRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEivaaaeAEAERIIEQAAAEIEQEKDR 110
|
90
....*....|....*....
gi 597837628 382 -----RERQKEIARQVVER 395
Cdd:pfam00430 111 alaelRQQVVALAVQIAEK 129
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-521 |
6.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 198 EDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKqgpsgnfEEGSSNAEMEQLErqrqqEIARQVAE 277
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK-------ELESLEGSKRKLE-----EKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 278 RQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEME-WQREIARQKAEMDEKE-KQRQVEIARQM 354
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKlSEFYEEYLDELREIEKRLSrLEEEINGIEERIKELEeKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE-RERQQEIARQHAERQR 433
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 434 KEEEARRQEEARLFAERQKKERERQEEIARQMEE----EEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER 509
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
330
....*....|..
gi 597837628 510 RIEEQLAAREVE 521
Cdd:PRK03918 507 ELEEKLKKYNLE 518
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
277-360 |
6.95e-04 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 40.22 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQEIARQEAERQRK-EEEMRRQQEYAQQMAEMQR--AQKEMEWQREIARQKAE-MDEKEKQRQVEIAR 352
Cdd:COG3599 37 ERLIRENKELKEKLEELEEELEEYRElEETLQKTLVVAQETAEEVKenAEKEAELIIKEAELEAEkIIEEAQEKARKIVR 116
|
....*...
gi 597837628 353 QMAERQRQ 360
Cdd:COG3599 117 EIEELKRQ 124
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
264-419 |
7.62e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 264 ERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMdeke 343
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL---- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVrriEKARKKSEMEKKERE 419
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA---ERKQLQAKLQQTEEE 186
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-523 |
7.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 197 SEDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGvEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVA 276
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEW--------QREIARQKAEMDEKEK---- 344
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaalllagLRGLAGAVAVLIGVEAayea 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 -------QRQVEIARQMAERQRQEEELLRQQE---VALQEAERQKKERERQKEIARQVVERK------------------ 396
Cdd:COG1196 539 aleaalaAALQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvl 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 397 -KQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREE 475
Cdd:COG1196 619 gDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 597837628 476 AEKEEMRKRKIeeerlrKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196 699 LLAEEEEEREL------AEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
220-413 |
8.02e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 220 EEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQ----KEREELE-------- 287
Cdd:pfam02029 118 EEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEvkdeKIKKEKKvkyeskvf 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 288 WQQEIARQEAERQRKEEE----------MRRQQEYAQQMAEMQRAQKEMEWQRE-IARQKAEMDEKE----KQRQVEIAR 352
Cdd:pfam02029 198 LDQKRGHPEVKSQNGEEEvtklkvttkrRQGGLSQSQEREEEAEVFLEAEQKLEeLRRRRQEKESEEfeklRQKQQEAEL 277
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 353 QMAERQRQEEELLRqqevALQEAERQKKERERQKEIARQVVERKKQEEV--RRIEKARKKSEM 413
Cdd:pfam02029 278 ELEELKKKREERRK----LLEEEEQRRKQEEAERKLREEEEKRRMKEEIerRRAEAAEKRQKL 336
|
|
| Spb1_C |
pfam07780 |
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of ... |
382-426 |
8.21e-04 |
|
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of FtsJ-like methyltransferases. Members of this family are involved in 60S ribosomal biogenesis, for example Swiss:P25582.
Pssm-ID: 462264 Cd Length: 209 Bit Score: 41.83 E-value: 8.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 382 RERQKEI-AR---QVVE---RKKQEEVRRIEKARKKSEM-----EKKERERQQEIAR 426
Cdd:pfam07780 97 KEKLRALnARpikKVAEakaRKKMRAAKRLEKAKKKAELinedeDMSEREKAKQIEK 153
|
|
| Lipase_chap |
pfam03280 |
Proteobacterial lipase chaperone protein; |
263-383 |
8.40e-04 |
|
Proteobacterial lipase chaperone protein;
Pssm-ID: 427230 [Multi-domain] Cd Length: 185 Bit Score: 41.14 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 263 LERQR-QQEIARQVAERQQKereeleWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQ---------RAQKEMEWQREI 332
Cdd:pfam03280 64 LERLAiAQDSALSAEEKQQR------LAALRAQLPEDLRAAREAQQRLQELAARTAQLQkagaspqqlRQARAQLVGPEA 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 597837628 333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEEllrqqevALQEAERQKKERE 383
Cdd:pfam03280 138 AQRLAALDQQRAAWQQRLDDYLAERQQINAA-------GLSEQERQAAIAQ 181
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
258-381 |
8.71e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQ------QKEREELE-WQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEM---- 326
Cdd:PRK09039 66 ADLLSLERQGNQDLQDSVANLRaslsaaEAERSRLQaLLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELlnqq 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 327 --EWQREIARQKAEMDEKEKQRQveiarqmaERQRQEEELLRQQEVAL----QEAERQKKE 381
Cdd:PRK09039 146 iaALRRQLAALEAALDASEKRDR--------ESQAKIADLGRRLNVALaqrvQELNRYRSE 198
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
261-398 |
8.87e-04 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 42.36 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKERE--ELEWQQEIARQeaeRQRKEEEMRRQQEYAQ-QMAEMQRAQKEMEWQReiarQKA 337
Cdd:PRK10927 112 EQLTPEQRQLLEQMQADMRQQPTQlvEVPWNEQTPEQ---RQQTLQRQRQAQQLAEqQRLAQQSRTTEQSWQQ----QTR 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ 398
Cdd:PRK10927 185 TSQAAPVQAQPRQSKPASTQQPYQDLLQTPAHTTAQSKPQQAAPVTRAADAPKPTAEKKDE 245
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
283-426 |
9.21e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 283 REELEWQQEIARQEAERQRKEEEMRR-----QQEYAQQMAEMQRAQKEmewqREIARQKAEMDEKEKQRQVEIARQMAER 357
Cdd:pfam13851 22 RNNLELIKSLKEEIAELKKKEERNEKlmseiQQENKRLTEPLQKAQEE----VEELRKQLENYEKDKQSLKNLKARLKVL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 358 QRQEEELLRQQEVALQEAERQKKER----ERQKEIARQVVERKKQEEV---RRIEKARKksEMEKKERERQQEIAR 426
Cdd:pfam13851 98 EKELKDLKWEHEVLEQRFEKVERERdelyDKFEAAIQDVQQKTGLKNLlleKKLQALGE--TLEKKEAQLNEVLAA 171
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
283-343 |
9.53e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 41.11 E-value: 9.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 283 REELEWQQEiARQEAERQRKEEEMRRqQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam05266 101 KDRQTKLLE-ELKKLEKKIAEEESEK-RKLEEEIDELEKKILELERQLALAKEKKEAADKE 159
|
|
| PRK03963 |
PRK03963 |
V-type ATP synthase subunit E; Provisional |
269-369 |
1.02e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 167649 [Multi-domain] Cd Length: 198 Bit Score: 41.28 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQvAERqqkereELEWQQEIARQEAERQrKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQV 348
Cdd:PRK03963 9 QEINRE-AEQ------KIEYILEEAQKEAEKI-KEEARKRAESKAEWILRKAKTQAELEKQRIIANAKLEVRRKRLAVQE 80
|
90 100
....*....|....*....|.
gi 597837628 349 EIARQMAERQRQEEELLRQQE 369
Cdd:PRK03963 81 ELISEVLEAVRERLAELPEDE 101
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
323-518 |
1.04e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.66 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEMEWQREIARQKAEMDEKEK---QRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQE 399
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARKRlvaKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 400 EVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKE 479
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 597837628 480 EMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAR 518
Cdd:PRK07735 164 KAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAK 202
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
280-364 |
1.11e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.47 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 280 QKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQ--------KEMEWQREIARQKAEMDEKEKQR----- 346
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDlikfdkflKENDAKRRRALKKAEEETKLKKEkekei 82
|
90 100
....*....|....*....|.
gi 597837628 347 ---QVEIARQMAERQRQEEEL 364
Cdd:pfam13863 83 kklTAQIEELKSEISKLEEKL 103
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
258-398 |
1.12e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAER-----QRKEEEMRRQQEYAQQMAEMQRAQKE--MEWQR 330
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRereelQREEERLVQKEEQLDARAEKLDNLENqlEEREK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 331 EIARQKAEMDEKEKQRQ---VEIARQMAERQRQeeELLRQQEvalQEAERQKKER-ERQKEIARQVVERKKQ 398
Cdd:PRK12705 113 ALSARELELEELEKQLDnelYRVAGLTPEQARK--LLLKLLD---AELEEEKAQRvKKIEEEADLEAERKAQ 179
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
265-414 |
1.14e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 40.46 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIarqkAEMDEKEK 344
Cdd:pfam07321 8 KHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYAEIQGKLVLLKELEKVKQQV----ALLRENEA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 QRQVEIArQMAERQRQEEELLRQQEVALQEAERQKkerERQKEIARQVverkkQEEVRRIEKARKKSEME 414
Cdd:pfam07321 84 DLEKQVA-EARQQLEAEREALRQARQALAEARRAV---EKFAELVRLV-----QAEELRQQERQEEQELE 144
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
225-457 |
1.31e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 225 EERRRGG-VEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKE 303
Cdd:PRK12678 56 KEARGGGaAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQEYAQQMAEmqraqkemewqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERE 383
Cdd:PRK12678 136 AARRGAARKAGEGGE---------------QPATEARADAAERTEEEERDERRRRGDRED--RQAEAERGERGRREERGR 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEarlFAERQKKERER 457
Cdd:PRK12678 199 DGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGR---GGRRGRRFRDR 269
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
215-391 |
1.34e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 215 AINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNfeEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIAR 294
Cdd:PRK07735 47 ALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT--EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 QEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQE 374
Cdd:PRK07735 125 AAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAK 204
|
170
....*....|....*..
gi 597837628 375 AERQKKERERQKEIARQ 391
Cdd:PRK07735 205 AKAAAAAKAKAAALAKQ 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-517 |
1.42e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKaemdeKEKQRQVEIARQMAERQRQEEELlrQQEVALQEAERQ 378
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELE------RQL-----KSLERQAEKAERYKELKAELREL--ELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 379 KKERERQKEIARQVVER---------KKQEEVRRIEKArkKSEMEKKERERQ-------QEIAR--QHAERQRKEEEARR 440
Cdd:TIGR02168 238 REELEELQEELKEAEEEleeltaelqELEEKLEELRLE--VSELEEEIEELQkelyalaNEISRleQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 441 QEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERR-----IEEQL 515
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqLELQI 395
|
..
gi 597837628 516 AA 517
Cdd:TIGR02168 396 AS 397
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
253-431 |
1.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 253 EGSSNAEMEQLeRQRQQEIARQVAERQQKEREelewQQEIARQEAERQrkeEEMRRQQEYAQQMAE---MQRAQkEMEWQ 329
Cdd:COG3096 831 APDPEAELAAL-RQRRSELERELAQHRAQEQQ----LRQQLDQLKEQL---QLLNKLLPQANLLADetlADRLE-ELREE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 330 REIARQ-KAEMDEKEKQ-RQVEIARQMAERQRQEEELLRQQevaLQEAERQKKERERQKEIARQVVERKK----QEEVRR 403
Cdd:COG3096 902 LDAAQEaQAFIQQHGKAlAQLEPLVAVLQSDPEQFEQLQAD---YLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
170 180 190
....*....|....*....|....*....|....*
gi 597837628 404 I-------EKARKKSEMEKKERERQQEIARQHAER 431
Cdd:COG3096 979 LgensdlnEKLRARLEQAEEARREAREQLRQAQAQ 1013
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
384-517 |
1.62e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIAR-QHAERQRKEEEARRQEEARLFAERQKKERERQEEI- 461
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERaEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEe 407
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 462 ARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEqriEAQRKAEEERR---IEEQLAA 517
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE---EAERAEAEKQRqkeLEMQLAE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
258-522 |
1.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIAR------QVAERQQKEREELEWQQEIARQEAERQRKEEEM---------RRQQEYAQQMAEMQRA 322
Cdd:COG4717 132 QELEALEAELAELPERleeleeRLEELRELEEELEELEAELAELQEELEELLEQLslateeelqDLAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEME-WQREIARQKAEMDEKEKQRQVE----------------------------------------------IARQMA 355
Cdd:COG4717 212 EEELEeAQEELEELEEELEQLENELEAAaleerlkearlllliaaallallglggsllsliltiagvlflvlglLALLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQV-----VERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 431 RQRKEEEARRQEEARLFA-----ERQKKERERQEEIARQMEEE---EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEA- 501
Cdd:COG4717 372 IAALLAEAGVEDEEELRAaleqaEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEEl 451
|
330 340
....*....|....*....|..
gi 597837628 502 -QRKAEEERRIEEQLAAREVEN 522
Cdd:COG4717 452 rEELAELEAELEQLEEDGELAE 473
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
258-380 |
1.76e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEiARQVAERQQkereelEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKeMEWQREIARQKA 337
Cdd:pfam09787 75 TELQELEAQQQEE-AESSREQLQ------ELEEQLATERSARREAEAELERLQEELRYLEEELRRSK-ATLQSRIKDREA 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 597837628 338 EMdekEKQRQVEIARQMAERQRQE-EELLRQqevaLQEAERQKK 380
Cdd:pfam09787 147 EI---EKLRNQLTSKSQSSSSQSElENRLHQ----LTETLIQKQ 183
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
269-397 |
1.78e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.20 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQkEREELEwqQEIARQEAERQRKEEEMRrqqeyaqqmAEMQRAQKEmewqreiarqKAEMDEKEKQ-RQ 347
Cdd:COG2825 32 QRILQESPEGKA-AQKKLE--KEFKKRQAELQKLEKELQ---------ALQEKLQKE----------AATLSEEERQkKE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 VEIARQMAERQRQEEEllRQQEVALQEAERQKKERERQKEIARQVVERKK 397
Cdd:COG2825 90 RELQKKQQELQRKQQE--AQQDLQKRQQELLQPILEKIQKAIKEVAKEEG 137
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
259-419 |
1.78e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARQVAERQQK--------EREELEWQQEIARQEAERQRkEEEMRRQQEYAQQMAEMQRAQ-KEMEWQ 329
Cdd:PRK04863 936 QFEQLKQDYQQAQQTQRDAKQQAfaltevvqRRAHFSYEDAAEMLAKNSDL-NEKLRQRLEQAEQERTRAREQlRQAQAQ 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 330 REIARQ-----KAEMDEKEKQRQvEIARQMAERQRQ----EEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEE 400
Cdd:PRK04863 1015 LAQYNQvlaslKSSYDAKRQMLQ-ELKQELQDLGVPadsgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
170
....*....|....*....
gi 597837628 401 VRRIEKARKKSEMEKKERE 419
Cdd:PRK04863 1094 TKKLRKLERDYHEMREQVV 1112
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
258-522 |
1.83e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEiARQVAERQQKEREELEWQQEiaRQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA 337
Cdd:pfam02029 2 EDEEEAARERRRR-AREERRRQKEEEEPSGQVTE--SVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 338 EMDEKEKQRQ-----VEIARQMAERQRQEEELlrQQEVALQEAERQKkERERQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:pfam02029 79 LQEALERQKEfdptiADEKESVAERKENNEEE--ENSSWEKEEKRDS-RLGRYKEEETEIREKEYQENKWSTEVRQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 413 MEKKEreRQQEIARQHAERQRKEEEARRQEEAR---------LFAERQKKERERQEEIARQMEEEEKRQREEaekeeMRK 483
Cdd:pfam02029 156 GEEEE--DKSEEAEEVPTENFAKEEVKDEKIKKekkvkyeskVFLDQKRGHPEVKSQNGEEEVTKLKVTTKR-----RQG 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 597837628 484 RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVEN 522
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEK 267
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
261-361 |
1.89e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 41.09 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQeiarqVAERQQKEREELE--WQQEIARQEAERQRKEEEM-----RRQQEYAQQmAEMQRAQKEMEWQREIA 333
Cdd:pfam15397 123 ANLVRQLQQ-----LKDSQQDELDELEemRRMVLESLSRKIQKKKEKIlsslaEKTLSPYQE-SLLQKTRDNQVMLKEIE 196
|
90 100 110
....*....|....*....|....*....|...
gi 597837628 334 RQKAEMDEKEK-----QRQVEIARQMAERQRQE 361
Cdd:pfam15397 197 QFREFIDELEEeipklKAEVQQLQAQRQEPREV 229
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
252-386 |
1.97e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 41.96 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQ--QEYAQQMAEMQRAQKEmewQ 329
Cdd:PRK12903 788 TEILSDGINNSDINDRPQELIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNlkQEIKLELSEIQEAEEE---I 864
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 330 REIARQKAEMDEKEKQ----RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQK 386
Cdd:PRK12903 865 QNINENKNEFVEFKNDpkklNKLIIAKDVLIKLVISSDEIKQDEKTTKKKKKDLEKTDEEA 925
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
306-396 |
2.06e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 41.64 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 306 MRRQQEYA-QQMAEMQRAQKEMEwQREIARQKAEMDEK-EKQRQVEIARQMAERQRQEeelLRQQevALQEAERQKKERE 383
Cdd:PRK13428 30 MAARQDTVrQQLAESATAADRLA-EADQAHTKAVEDAKaEAARVVEEAREDAERIAEQ---LRAQ--ADAEAERIKVQGA 103
|
90
....*....|...
gi 597837628 384 RQKEIARQVVERK 396
Cdd:PRK13428 104 RQVQLLRAQLTRQ 116
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
366-431 |
2.19e-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: 38.96 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 366 RQQEVA--LQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEmekKERERQQEIARQHAER 431
Cdd:cd06503 31 REEKIAesLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAE---KIKEEILAEAKEEAER 95
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
270-347 |
2.22e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 41.01 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 270 EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaQQMAEMQRAQkemewQREIarqkaemDEKEKQRQ 347
Cdd:pfam07946 257 EALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKERE--EKLAKLSPEE-----QRKY-------EEKERKKE 320
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
313-427 |
2.33e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.80 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 313 AQQMAEMQRAQKEMEwqREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQV 392
Cdd:pfam02050 4 ARELAEAQRELQQAE--EKLEELQQYRAEYQQQLSGAGQGISAAELRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 597837628 393 VeRKKQEEVRRIEK--ARKKSEMEKKERERQQ----EIARQ 427
Cdd:pfam02050 82 W-QEARQERKSLEKlrEREKKEERKEQNRREQkqldELAAR 121
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
294-395 |
2.47e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.22 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 294 RQEAeRQRKEEEMRRQQEYAQQMAEMQR------AQKEMEWQReIARQKAEMDEKEKQRQVEIARQMAERQRQEeellrq 367
Cdd:PRK07353 45 RAEA-KERLAEAEKLEAQYEQQLASARKqaqaviAEAEAEADK-LAAEALAEAQAEAQASKEKARREIEQQKQA------ 116
|
90 100
....*....|....*....|....*...
gi 597837628 368 qevALQEAERQkkererQKEIARQVVER 395
Cdd:PRK07353 117 ---ALAQLEQQ------VDALSRQILEK 135
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
259-386 |
2.47e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 39.08 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEIARqvAERQQK-EREELEWQQEIA-RQEAERQRKEEEMRrqqeyaqqMAEMQRAQKEmewqrEIARQK 336
Cdd:pfam12474 15 ERQQLKKRYEKELEQ--LERQQKqQIEKLEQRQTQElRRLPKRIRAEQKKR--------LKMFRESLKQ-----EKKELK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEKQRQVEIARQMAERQRQEEellRQQEVALQEAERQKKERERQK 386
Cdd:pfam12474 80 QEVEKLPKFQRKEAKRQRKEELELEQ---KHEELEFLQAQSEALERELQQ 126
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
269-374 |
2.47e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQqeyAQQMAEMQRAQKEmewqREIARQKAEMDEKEKQRQV 348
Cdd:smart00935 11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKD---AATLSEAAREKKE----KELQKKVQEFQRKQQKLQQ 83
|
90 100
....*....|....*....|....*...
gi 597837628 349 EIARQMAERQRQEEELLRQ--QEVALQE 374
Cdd:smart00935 84 DLQKRQQEELQKILDKINKaiKEVAKKK 111
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
268-377 |
2.61e-03 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 41.57 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 268 QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyaqqmAEMQRAQKEmewqREIARQKAEMDEKEKQRQ 347
Cdd:pfam14817 69 AESRQSAAARRLELQKEIERLRAEISRLDKQLEARELELSREE------AERERALDE----ISDSRHRQLLLEAYDQQC 138
|
90 100 110
....*....|....*....|....*....|
gi 597837628 348 VEIARQMAERQRQEEELLRQQEVALQEAER 377
Cdd:pfam14817 139 EEARKILAEDHQRLQGQLQQLRDAARKAEK 168
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
373-423 |
2.65e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 38.81 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 597837628 373 QEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:pfam04696 23 KEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKREEREELFEERRAEQI 73
|
|
| FliH |
COG1317 |
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular ... |
284-380 |
2.86e-03 |
|
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440928 [Multi-domain] Cd Length: 172 Bit Score: 39.52 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 284 EELEWQQEIARQEAERQRKEEEMRRQQEYAQQmaEMQRAQKEME-WQREIARQKAEMDEKEKQRQVEIARQMAER----- 357
Cdd:COG1317 2 EELEALREEAREEGYAEGYEEGLEEGRAEAEA--EIAEALEQLQaLLEQLQAPLEELDEELEEELVELALAIARKvigre 79
|
90 100
....*....|....*....|....
gi 597837628 358 -QRQEEELLRQQEVALQEAERQKK 380
Cdd:COG1317 80 lALDPEAILALVREALAALREAEE 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
345-529 |
2.94e-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: 41.50 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 QRQVEIARQMAERQRQEEE------LLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRiEKARKKSEMEKKER 418
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEeeaagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-AKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 419 ERQQEIARQHAERQRKEEEARRQEEARLfAERQKKERERQEEIARQMEEEEKRQREeaeKEEMRKRKIEEERLRKEEEQR 498
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLR-DEQEEIESSKQEIEKEEEKLAQVLKEN---KEEEKEKKLQEEELKLLAKEE 295
|
170 180 190
....*....|....*....|....*....|.
gi 597837628 499 IEAQRKAEEERRIEEQLAAREVENQSTVVNP 529
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
275-408 |
3.00e-03 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 41.32 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 275 VAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEmqraqkemewqreiaRQKAEMDEKEKQRQVEIARQM 354
Cdd:PRK13709 1627 NSVQPGAGNGEPVTAEVLAQRQAEEAIRRETERRADEIVRKMAE---------------NKPDLPDGKTEQAVRDIAGQE 1691
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 355 AERQRQEEELLRQQEVALQEaerQKKERERQKEIARQVVERKK-----QEEVRRIEKAR 408
Cdd:PRK13709 1692 RDRAAISEREAALPESVLRE---PQREREAVREVARENLLRERlqqmeRDMVRDLQKEK 1747
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
269-389 |
3.03e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQ-QEIARQEA-ERQRKEEemrRQQEYAQQMAEMQRAQKEME----WQREIARQKAEMDEK 342
Cdd:PRK09039 41 QFFLSREISGKDSALDRLNSQiAELADLLSlERQGNQD---LQDSVANLRASLSAAEAERSrlqaLLAELAGAGAAAEGR 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 --EKQRQVEIARQMAERQRQEEELLRQQ-----------EVALQEAErqKKERERQKEIA 389
Cdd:PRK09039 118 agELAQELDSEKQVSARALAQVELLNQQiaalrrqlaalEAALDASE--KRDRESQAKIA 175
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
265-357 |
3.22e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.83 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREeLEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQR---AQKEmEWQREIARQKAEMDE 341
Cdd:PRK07353 42 RTNRAEAKERLAEAEKLEAQ-YEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAeaqASKE-KARREIEQQKQAALA 119
|
90
....*....|....*.
gi 597837628 342 KEKQRQVEIARQMAER 357
Cdd:PRK07353 120 QLEQQVDALSRQILEK 135
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
257-332 |
3.29e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 3.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 257 NAEMEQLERQRQQEIARQVAErQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQR--AQKEMEWQREI 332
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlQKRQQEELQKI 96
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
262-422 |
3.36e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKEMEWQREIARQKAEM 339
Cdd:PRK04863 488 EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfcKRLGKNLDDEDELEQLQEELEARL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 340 DEKEKQrqVEIARQMAERQRQEEELLRQQE----------VALQEAERQKKE--------RERQKEIARQVVERKKQEEV 401
Cdd:PRK04863 568 ESLSES--VSEARERRMALRQQLEQLQARIqrlaarapawLAAQDALARLREqsgeefedSQDVTEYMQQLLERERELTV 645
|
170 180
....*....|....*....|.
gi 597837628 402 RRIEKARKKSEMEKKERERQQ 422
Cdd:PRK04863 646 ERDELAARKQALDEEIERLSQ 666
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
200-523 |
3.61e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 200 EFLKQLVRIVEaHQVAINKIEEQVGE--------ERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEI 271
Cdd:TIGR00618 287 NRARKAAPLAA-HIKAVTQIEQQAQRihtelqskMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 272 ARQVAERQQKEREE--LEWQQEI-ARQEAERQRKEEEMRRQQEYAQQMAEMQR----------AQKEMEWQREIARQKAE 338
Cdd:TIGR00618 366 SIREISCQQHTLTQhiHTLQQQKtTLTQKLQSLCKELDILQREQATIDTRTSAfrdlqgqlahAKKQQELQQRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 339 MDEKEKQRQVE---IARQMAERQRQEEELLRQQEV-ALQEAERQKKERERQKEIARQVVERKKQEevRRIEKARKKSEME 414
Cdd:TIGR00618 446 AITCTAQCEKLekiHLQESAQSLKEREQQLQTKEQiHLQETRKKAVVLARLLELQEEPCPLCGSC--IHPNPARQDIDNP 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 415 KKERERQQEIARQHAERQRKEEEARRQEEARLfaeRQKKERERQEEIARQmEEEEKRQREEAEKEEMRKRKIEEERLRKE 494
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSER---KQRASLKEQMQEIQQ-SFSILTQCDNRSKEDIPNLQNITVRLQDL 599
|
330 340
....*....|....*....|....*....
gi 597837628 495 EEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
258-318 |
3.88e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 3.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 258 AEMEQLERQRqqeiARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE 318
Cdd:pfam20492 62 EEKERLEESA----EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
|
|
| Activator_LAG-3 |
pfam11498 |
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ... |
296-432 |
4.04e-03 |
|
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.
Pssm-ID: 151935 [Multi-domain] Cd Length: 476 Bit Score: 40.72 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMewqREIARQKAEMDEKEKQRQVEIARQMAERQRQEEE-----LLRQQEV 370
Cdd:pfam11498 302 EAGGDRMPQSAPPPAMNPQHIAQLAQQQNKM---RLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEHQqqqmlLQQQQQM 378
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 371 -ALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam11498 379 hQLQQHHQMNGGGQFATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHHQQAQQQHQQPAQHGQ 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-528 |
4.37e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 294 RQEAERQ--RKEEEMRRQQEYAqqmAEMQRAQKEMEWQREIARQKAEMdeKEKQRQVEIARQMAERQRQEEELlRQQEVA 371
Cdd:TIGR02168 174 RKETERKleRTRENLDRLEDIL---NELERQLKSLERQAEKAERYKEL--KAELRELELALLVLRLEELREEL-EELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 372 LQEAERQKKERERQKeiarqvveRKKQEEVRRIEKARkkSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQ 451
Cdd:TIGR02168 248 LKEAEEELEELTAEL--------QELEEKLEELRLEV--SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 452 KKERERQEEIARQMeeeekrqreeaeKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVN 528
Cdd:TIGR02168 318 LEELEAQLEELESK------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
299-464 |
4.47e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.45 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEwQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQ 378
Cdd:TIGR02473 9 DLREKEEEQAKLELAKAQAEFERLETQLQ-QLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQLDQRIQQQQQELALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 379 KKERERQKEIARQvverkKQEEVRRIEKARkksemEKKERERQqeiarqhaerqrkeeearrqeearlfAERQKKERERQ 458
Cdd:TIGR02473 88 QQEVEAKRERLLE-----ARRELKALEKLK-----EKKQKEYR--------------------------AEEAKREQKEM 131
|
....*.
gi 597837628 459 EEIARQ 464
Cdd:TIGR02473 132 DELATQ 137
|
|
| DUF1387 |
pfam07139 |
Protein of unknown function (DUF1387); This family represents a conserved region approximately ... |
236-414 |
4.62e-03 |
|
Protein of unknown function (DUF1387); This family represents a conserved region approximately 300 residues long within a number of hypothetical proteins of unknown function that seem to be restricted to mammals.
Pssm-ID: 462100 Cd Length: 311 Bit Score: 40.11 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 236 EHPAGSFRKQGPSGNFEEGSSnAEMEQLERQRQQEIARQVAERQQKEREELewQQEIARQEAERQRKEEEM----RRQQe 311
Cdd:pfam07139 122 LSRNASKPKSRPSSNKSLLED-APLSSTDDKLGSSIEKKVGPNIEKSVKDL--QRCTVSLTRYRVVIKEEMdasiKKIK- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 312 yaQQMAEMQRAQKEMEwqreiARQKAEMDeKEKQRQVEIarqMAERQRQEEELLRQQEVALQEAERQKKE-RERQKEIar 390
Cdd:pfam07139 198 --ATFAELQSCLMDRE-----VALLAEMD-KVKAEAMEI---LTARQKKAEELKRLTDLAVQMSEEQLVElRADIKHF-- 264
|
170 180
....*....|....*....|....
gi 597837628 391 qVVERKKQEEVRRIekARKKSEME 414
Cdd:pfam07139 265 -VSERKYDEELGRA--ARFTCDLE 285
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
233-513 |
4.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 233 EDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQ--EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ 310
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 311 EYAQQMAEMQRaQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAErqrQEEELLRQQEVALQEAERQKKERERQKEIAR 390
Cdd:TIGR00618 625 QDLQDVRLHLQ-QCSQELALKLTALHALQLTLTQERVREHALSIRV---LPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 391 QVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQE----------- 459
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalqtgael 780
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 460 -----EIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:TIGR00618 781 shlaaEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
334-432 |
5.00e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 38.31 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVAL-QEAERQKKERERqkeiarqvvERKKQEEVRRIEKARKKSE 412
Cdd:pfam12474 11 RFEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELrRLPKRIRAEQKK---------RLKMFRESLKQEKKELKQE 81
|
90 100
....*....|....*....|
gi 597837628 413 MEKKERERQQEIARQHAERQ 432
Cdd:pfam12474 82 VEKLPKFQRKEAKRQRKEEL 101
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
268-355 |
5.18e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 39.82 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 268 QQEIARQVAERQQKEREELEWQ----QEIARQEAERQRKEEEMRrqqeyAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:COG0330 170 QDAMEDRMKAEREREAAILEAEgyreAAIIRAEGEAQRAIIEAE-----AYREAQILRAEGEAEAFRIVAEAYSAAPFVL 244
|
90
....*....|..
gi 597837628 344 KQRQVEIARQMA 355
Cdd:COG0330 245 FYRSLEALEEVL 256
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
374-464 |
5.62e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 40.49 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 374 EAERQKKERERQKEIARQVVERKKQEEVRRIEKAR-KKSEMEKKERERqqeIARQHAERQRkeeearrqeearlfAERQK 452
Cdd:PTZ00266 436 ERARIEKENAHRKALEMKILEKKRIERLEREERERlERERMERIERER---LERERLERER--------------LERDR 498
|
90
....*....|..
gi 597837628 453 KERERQEEIARQ 464
Cdd:PTZ00266 499 LERDRLDRLERE 510
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
215-435 |
5.69e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 215 AINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIAR 294
Cdd:pfam02029 92 TIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 Q-------EAERQRKEEEM------------RRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEiARQMA 355
Cdd:pfam02029 172 EnfakeevKDEKIKKEKKVkyeskvfldqkrGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-AEQKL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQeeellRQQEVALQEAERQkkeRERQKEIARQVVERKKQEEVRRieKARkksemEKKERERQQEiarqHAERQRKE 435
Cdd:pfam02029 251 EELRR-----RRQEKESEEFEKL---RQKQQEAELELEELKKKREERR--KLL-----EEEEQRRKQE----EAERKLRE 311
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
336-423 |
5.80e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 39.15 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAERQRQEEELLRQqevalQEAERQKKERERQKEIARQVVERKKQEEVRR------------ 403
Cdd:pfam06391 67 EKKIEQYEKENKDLILKNKMKLSQEEEELEEL-----LELEKREKEERRKEEKQEEEEEKEKKEKAKQelidelmtsnkd 141
|
90 100
....*....|....*....|....
gi 597837628 404 ----IEKARKKSEMEKKERERQQE 423
Cdd:pfam06391 142 aeeiIAQHKKTAKKRKSERRRKLE 165
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
320-438 |
5.97e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 38.52 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 QRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiarqvVERKKQE 399
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKE-----KERREKK 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 597837628 400 EVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEA 438
Cdd:pfam11600 76 EKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEK 114
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
319-415 |
6.25e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 38.77 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 319 MQRAQKEMEWQREIARQKAE--MDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERK 396
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEkiLEEAEEEAE-EIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEA 90
|
90
....*....|....*....
gi 597837628 397 KQeevrRIEKARKKSEMEK 415
Cdd:COG1390 91 LE----KLKNLPKDPEYKE 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
252-463 |
6.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKER----------EELEWQQEI--------ARQEAERQ-----------RK 302
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQqlceeknalqEQLQAETELcaeaeemrARLAARKQeleeilhelesRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 303 EEEMRRQQEYAQQMAEMQRAQKEMEWQ---REIARQKAEM-----DEKEKQRQVEI-------ARQMAERQRQEEELLRQ 367
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQldeEEAARQKLQLekvttEAKIKKLEEDIllledqnSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQK---KERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeearrqeEA 444
Cdd:pfam01576 165 TSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------IA 232
|
250
....*....|....*....
gi 597837628 445 RLFAERQKKERERQEEIAR 463
Cdd:pfam01576 233 ELRAQLAKKEEELQAALAR 251
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
390-519 |
6.31e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 390 RQVVERKKQEEVRRIEkARKKSEMEKKERERQQEIARQHAERQRKEEEArrqeearlfAERQKKERERQEEIARQmeeee 469
Cdd:COG2268 192 RKIAEIIRDARIAEAE-AERETEIAIAQANREAEEAELEQEREIETARI---------AEAEAELAKKKAEERRE----- 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 470 krqREE---------AEKEEMRKRKIEEERLRKEEEQRIEAQRKaEEERRIEEQLAARE 519
Cdd:COG2268 257 ---AETaraeaeaayEIAEANAEREVQRQLEIAEREREIELQEK-EAEREEAELEADVR 311
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
295-432 |
6.53e-03 |
|
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: 38.11 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 QEAERQRKEEEMRRQQEyaqqMAEMQRAQKEMEwqreiaRQKAEMdEKEKQRQVEIARQMAERQRqEEELLRQQEVAL-- 372
Cdd:pfam15346 1 KEAESKLLEEETARRVE----EAVAKRVEEELE------KRKDEI-EAEVERRVEEARKIMEKQV-LEELEREREAELee 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 373 ----QEAERQKKE------RERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15346 69 errkEEEERKKREelerilEENNRKIEEA---QRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQ 135
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
257-327 |
6.64e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 39.59 E-value: 6.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 257 NAEMEQLERQRQQEIARQVAerqqkereELEWQQEIARQEAERQRK--EEEMRRQQEYAQQMAEMQRAQKEME 327
Cdd:cd03406 191 EAETERKRAVIEAEKDAEVA--------KIQMQQKIMEKEAEKKISeiEDEMHLAREKARADAEYYRALREAE 255
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
287-397 |
6.79e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.95 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 287 EWQQEIARQEAERQRKEEEMRRQQEYAQQMAEmqraqkemewqrEIARQKAEMDEKEKQ-RQVEIARQMAERQRQEEELl 365
Cdd:smart00935 15 AGKAAQKQLEKEFKKRQAELEKLEKELQKLKE------------KLQKDAATLSEAAREkKEKELQKKVQEFQRKQQKL- 81
|
90 100 110
....*....|....*....|....*....|..
gi 597837628 366 rQQEVALQEAERQKKERERQKEIARQVVERKK 397
Cdd:smart00935 82 -QQDLQKRQQEELQKILDKINKAIKEVAKKKG 112
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
329-404 |
7.38e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDE--KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQ------------KKERERQKEIARQVVE 394
Cdd:PRK11448 148 QQEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQleqlqekaaetsQERKQKRKEITDQAAK 227
|
90
....*....|..
gi 597837628 395 RKK--QEEVRRI 404
Cdd:PRK11448 228 RLElsEEETRIL 239
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
342-431 |
8.53e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQVEIARQMAERQRQE-EELLRQQEVALQEAERQKKERERQKEIArQVVERKKQEEVRRIEKARKKSEM-EKKERE 419
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQlELQAREKAQSQALAEAQQQELVALEGLA-AELEEKQQELEAQLEQLQEKAAEtSQERKQ 216
|
90
....*....|..
gi 597837628 420 RQQEIARQHAER 431
Cdd:PRK11448 217 KRKEITDQAAKR 228
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
252-526 |
8.66e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQrqqEIARQVAERQ-----QKEREELE-WQQEIARQEA-------------ERQRKEEEMRRQQEY 312
Cdd:pfam12128 207 EDDGVVPPKSRLNRQ---QVEHWIRDIQaiagiMKIRPEFTkLQQEFNTLESaelrlshlhfgykSDETLIASRQEERQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 313 AQQMAEMQRAQKEMEWQREIARQKAEM-----DEKEKQRQVEIARQMAER----------QRQEEELLRQQEVALQEaER 377
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEKRDELNGELsaadaAVAKDRSELEALEDQHGAfldadietaaADQEQLPSWQSELENLE-ER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 378 QKKERERQKEIARQVVERK---KQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKE 454
Cdd:pfam12128 363 LKALTGKHQDVTAKYNRRRskiKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRL 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 455 RERQEEIARQMEEEEKRQREeaeKEEMRKRKIEEERLRKEEEqrieaQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:pfam12128 443 KSRLGELKLRLNQATATPEL---LLQLENFDERIERAREEQE-----AANAEVERLQSELRQARKRRDQASE 506
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
279-341 |
8.67e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 38.39 E-value: 8.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 279 QQKEREELewQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQ---KAEMDE 341
Cdd:COG3167 44 QLEELEEL--EAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELL------KQlpsKAEVPA 101
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-414 |
8.71e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 39.66 E-value: 8.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 343 EKQRQVEIARQMAERQRQEEELLRQQEVAlqeaeRQKKERERQkeiARQVVERKKQ-EEVRRIEKARKKSEME 414
Cdd:COG0488 238 LEQRAERLEQEAAAYAKQQKKIAKEEEFI-----RRFRAKARK---AKQAQSRIKAlEKLEREEPPRRDKTVE 302
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
356-464 |
8.84e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 38.53 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE------MEKKERERQQEIARQHA 429
Cdd:pfam13904 65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAesasksLAKPERKVSQEEAKEVL 144
|
90 100 110
....*....|....*....|....*....|....*
gi 597837628 430 ERQRKEEEARrqeearlfaERQKKERERQEEIARQ 464
Cdd:pfam13904 145 QEWERKKLEQ---------QQRKREEEQREQLKKE 170
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
260-384 |
8.87e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 38.49 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 260 MEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA-- 337
Cdd:pfam15665 62 LEQHERMKRQALTEFEQYKRRVEERELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkh 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 597837628 338 --EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERER 384
Cdd:pfam15665 142 rqEIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKEVEDLRKEKKK 190
|
|
| 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 ... |
266-358 |
9.04e-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: 37.29 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQV--AERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQ-RAQKEMEWQREIARQKAEMDEK 342
Cdd:pfam00430 30 KRRELIADEIaeAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVaAAEAEAERIIEQAAAEIEQEKD 109
|
90 100
....*....|....*....|.
gi 597837628 343 E-----KQRQVEIARQMAERQ 358
Cdd:pfam00430 110 RalaelRQQVVALAVQIAEKL 130
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
346-429 |
9.11e-03 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 39.92 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 346 RQVEIARQMAERQRQEEELLRQQEVALQeaeRQKKERERQ--KEIArqvvERKKQEEVRRIEKARKKSEMekKERER-QQ 422
Cdd:PRK11091 78 EQLEESRQRLSRLVAKLEEMRERDLELN---VQLKDNIAQlnQEIA----EREKAEEARQEAFEQLKNEI--KEREEtQI 148
|
....*..
gi 597837628 423 EIARQHA 429
Cdd:PRK11091 149 ELEQQSS 155
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
259-517 |
9.19e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 259 EMEQLERQRQQEI-ARQVAERQQKEREELEWQQEIAR-------QEAERQRKEEEMRRQQE----YAQQMAEMQRAQKEM 326
Cdd:pfam12128 269 SDETLIASRQEERqETSAELNQLLRTLDDQWKEKRDElngelsaADAAVAKDRSELEALEDqhgaFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 E--WQREIARQKAEMD-EKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVErkKQEEVRR 403
Cdd:pfam12128 349 LpsWQSELENLEERLKaLTGKHQDVTAKYN-RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ--ALESELR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEiarqmeEEEKRQREEAEKEEMRK 483
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEA------ANAEVERLQSELRQARK 499
|
250 260 270
....*....|....*....|....*....|....
gi 597837628 484 RKIEEERLRKEEEQRIEAQRKAEEErrIEEQLAA 517
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDE--LELQLFP 531
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
257-485 |
9.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIA--RQVAERQQKEREEL-EWQQEIARQEAERQRKEEEMR--RQQ--EYAQQMAEMQRAQKEM-EW 328
Cdd:COG1340 35 NEELKELAEKRDELNAqvKELREEAQELREKRdELNEKVKELKEERDELNEKLNelREEldELRKELAELNKAGGSIdKL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIAR-----QKAEMD-EKEKQRQVEIAR--QMAERQRQEEELLRQQEVALQEAERQKKE----RERQKEIARQVVERK 396
Cdd:COG1340 115 RKEIERlewrqQTEVLSpEEEKELVEKIKEleKELEKAKKALEKNEKLKELRAELKELRKEaeeiHKKIKELAEEAQELH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 397 KQ--EEVRRIEKARKKSEMEKKE-RERQQEIARQHAErqrkeeearrqeearlFAERQKKERERQEEIARqMEEEEKRQR 473
Cdd:COG1340 195 EEmiELYKEADELRKEADELHKEiVEAQEKADELHEE----------------IIELQKELRELRKELKK-LRKKQRALK 257
|
250
....*....|..
gi 597837628 474 EEAEKEEMRKRK 485
Cdd:COG1340 258 REKEKEELEEKA 269
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
297-389 |
9.50e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 39.13 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 297 AERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQV-------EIAR---QMAERQRQEEELLR 366
Cdd:pfam15991 1 AARPKMSEQMWRALK-RHIMRERERKKQEQEAKMEEERLRREREEREKEDRMtleetkeQILKlekKLADLKEEKHQLFL 79
|
90 100
....*....|....*....|...
gi 597837628 367 QQEVALQEAERQKKERERQKEIA 389
Cdd:pfam15991 80 QLKKVLHEDETRKRQLKEQSELF 102
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
261-425 |
9.76e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 38.21 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIArQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyAQQMAEMQRAQKEMEW-----QREIARQ 335
Cdd:pfam14988 21 EKLWNQYVQECE-EIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKE--LQALRPFAKLKESQEReiqdlEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAERQRQEEEL------------LRQQEVALQEAERQ----------KKERERQKEIARQVv 393
Cdd:pfam14988 98 RAETAEKDREAHLQFLKEKALLEKQLQELrilelgeratreLKRKAQALKLAAKQalsefcrsikRENRQLQKELLQLI- 176
|
170 180 190
....*....|....*....|....*....|..
gi 597837628 394 erkkqEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:pfam14988 177 -----QETQALEAIKSKLENRKQRLKEEQWYL 203
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
251-581 |
9.92e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 39.61 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKER--------------EELEWQQEIARQEAER-QRKEEEMRRQQEYAQQ 315
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyktlelEIAESDVEVKKAELELvKEEAKEPRDEEKIKQA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 316 MAEMQRAQKEMEWQREIA--RQKAEMDEKEKQ--RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ 391
Cdd:NF033838 210 KAKVESKKAEATRLEKIKtdREKAEEEAKRRAdaKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 392 V-----------VERKKQEEVRRIEKARKKSEMEKKERERQ-QEIARQHAERQRKEEEARRQEEARLFAERQKKERERQE 459
Cdd:NF033838 290 VgeetlpspslkPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 460 EIarqmeEEEKRQREEAEKEEMRKRKIEEERLRKEEeqriEAQRK-AEEERRIEEQLAAREVENQSTVVNPAFGMHIPGE 538
Cdd:NF033838 370 KI-----KQAKAKVESKKAEATRLEKIKTDRKKAEE----EAKRKaAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAE 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 597837628 539 TQAGEHSTDYYG---YSTNSDATktvlaglmsmSSRLTSTEPPQLE 581
Cdd:NF033838 441 QPKAEKPADQQAeedYARRSEEE----------YNRLTQQQPPKTE 476
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-525 |
9.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQ-----KEREELewQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKE--MEWQ 329
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEEleslqEEAEEL--QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEelKELE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 330 REIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARK 409
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 410 KSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEE 489
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
250 260 270
....*....|....*....|....*....|....*.
gi 597837628 490 RLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQST 525
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
|