|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
172-783 |
6.44e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 115.24 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 172 KKTELERMEKERLAAQSfSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADK 251
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEA-KKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 252 EKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEK 331
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 332 ERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEK-------ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 404
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeekkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 405 EKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERL 484
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 485 EKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERA 564
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 565 TKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKEnaKKEKENSERVEKERVAKERAEKERVAKESEKERMER 644
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE--KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 645 ERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVetEQLPKIEREQLPKAKAGKERAEK 724
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV--EQLKKKEAEEKKKAEELKKAEEE 1658
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 725 ERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAIRDLLKPKATKVNK 783
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
56-735 |
2.84e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.93 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 56 EAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLE 135
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAA 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 136 QLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLE 215
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 216 KERVAKEKAEKERIEKERA-------TKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKER 288
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKAdelkkaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 289 LEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKER 368
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 369 AAKEKAEKERI--EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK 446
Cdd:PTZ00121 1422 EAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 447 EKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE--KAEKERIEKERAAKEKA 524
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkkKAEEAKKAEEDKNMALR 1581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 525 EKERLEKERAAKEKAEKEGIEKERAAK----EKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKgrlek 600
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----- 1656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 601 erltKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEK 680
Cdd:PTZ00121 1657 ----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 681 ERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKE-RAEKERLLKEKIDGE 735
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELDEE 1788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
90-771 |
3.05e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.93 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 90 QEVAQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKER 169
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 170 IEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKE--RLEKERVAKEKAEKERIEKERATKEKAEKERIEKE 247
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEarKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 248 RADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE-KERLEKERAAKEKAEKERIVKERAAK 326
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEaKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 327 GKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAaKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 406
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 407 ERLEKERAAKEKAEKERIEKERAAKEKAEKERleKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEK 486
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 487 eRAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATK 566
Cdd:PTZ00121 1491 -KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 567 EKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTK-ENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERE 645
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 646 RVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKvETEQLPKIEREQLPKAKAGKERAEKE 725
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEEN 1728
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1955802949 726 RLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAIR 771
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
206-771 |
3.67e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 206 KEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAE 285
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 286 KERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 365
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 366 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 445
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 446 KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKERIE---KERAAKE 522
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK--KKADAAKKKAEEKKKAdeaKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 523 KAEKERLEKERAAKEKAE---KEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLE 599
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 600 KERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERErvAKERAEKERAEKEQQAKELAAKE 679
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE--AKKAEEKKKADELKKAEELKKAE 1561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 680 KERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFT 759
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
570
....*....|..
gi 1955802949 760 TTSKKEKIMAIR 771
Cdd:PTZ00121 1642 EAEEKKKAEELK 1653
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-678 |
2.02e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQ-SFSKEKAEKERLERERvakeKAEKERLEKERVAKEKAEKERIEKERATKEKA 239
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQaEEYELLAELARLEQDI----ARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 240 EKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 319
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 320 VKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 399
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 400 AKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKA 479
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 480 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI 559
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 560 EKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEK 639
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
490 500 510
....*....|....*....|....*....|....*....
gi 1955802949 640 ERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAK 678
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
148-684 |
1.59e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 148 QREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKE 227
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 228 RIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 307
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE 387
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 468 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 548 RAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKER 627
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 628 AEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAA 684
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-582 |
1.74e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 35 ELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQlvnALELKRQEVAQKAQEMLEAQLREEREQEEKR 114
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 115 EAERRAHEQAGK---ERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSK 191
Cdd:PTZ00121 1311 AEEAKKADEAKKkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 192 EKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERA---------------TKEKAEKERiEKERADKEKAEK 256
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeakkkaeeakkadeAKKKAEEAK-KAEEAKKKAEEA 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 257 ERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEK 336
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 337 ERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK 416
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 417 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 496
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 497 EGIEKERAAKE--KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERI 574
Cdd:PTZ00121 1710 KEAEEKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
....*...
gi 1955802949 575 EKERAAKE 582
Cdd:PTZ00121 1790 EKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
13-582 |
2.06e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 13 KSDESPGEVASKKNRTKEHPTRELGRKLKSALKEQLRMIHEKIEAQKIAEmALAEVRSILAKEEEERQLVNALELKRQEV 92
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 93 AQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEK 172
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 173 KTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATK-EKAEKERIEKERADK 251
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 252 EKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEK 331
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 332 ERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEK 411
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 412 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKErivKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAK 491
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 492 EKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEK 571
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
570
....*....|.
gi 1955802949 572 ERIEKERAAKE 582
Cdd:PTZ00121 1792 RRMEVDKKIKD 1802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-752 |
3.78e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 212 ERLEKERvakEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEK 291
Cdd:COG1196 203 EPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 292 ERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAK 371
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 372 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 451
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 452 ERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEK 531
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 532 ERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKE 611
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 612 KENSERVEKERVAKER-------AEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAA 684
Cdd:COG1196 600 AVDLVASDLREADARYyvlgdtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 685 VKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPE 752
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-643 |
1.38e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 100 LEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERM 179
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 180 EKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERI 259
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 260 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERA 339
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 340 AKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKA 419
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 420 EKERIEKERAAKEKAEKERLEKERAAK------EKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLE----KERA 489
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtlLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 490 AKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKA 569
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 570 EKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERME 643
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
308-639 |
2.14e-17 |
|
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: 84.20 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKgKAEKERIEKERAAKEKAEKERLEKERaakEKAEKEGIEKERAAKEKAEKER------IEK 381
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQ-IAEKKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKEEERKEERKRYRqeleeqIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 382 ERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAK 461
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 462 GKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 541
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREI-ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 542 EGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKE 621
Cdd:pfam13868 244 QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323
|
330
....*....|....*...
gi 1955802949 622 rvakERAEKERVAKESEK 639
Cdd:pfam13868 324 ----EAERRERIEEERQK 337
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
224-532 |
2.32e-17 |
|
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: 84.20 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 224 AEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKE---RIEKERAAKEKAEKERLEKERAAKEKAE 300
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 301 KERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI- 379
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 380 ---EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVK 456
Cdd:pfam13868 189 lraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLR 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 457 ERAAKGKAEKERIEKERaakEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKE 532
Cdd:pfam13868 269 KQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-781 |
3.90e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 270 EKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERL 349
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 350 EKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERA 429
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 430 AKEKAEKERLEKERAA--KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE 507
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 508 KAEKERIEKERAAKEKAEK-----ERLEKERAAKEKAEKEGIEKERAAKEKAEKER-----IEKERATKEKAEKERIEKE 577
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAaadeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeaKKKAEEDKKKADELKKAAA 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 578 RAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVA 657
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 658 KERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIER-EQLPKAKAGKERAEKERLLKEKIDGER 736
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1955802949 737 VVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAIRDLLKPKATKV 781
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
239-556 |
1.54e-16 |
|
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: 81.89 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 239 AEKERIEKERADKEKAEKERIEKERaakEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKER 318
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 319 IVkeraakgkaEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKerAAKEKAEKERLEKER 398
Cdd:pfam13868 106 IV---------ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE--YLKEKAEREEEREAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 399 AAKEKAEKERL------EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKE 472
Cdd:pfam13868 175 REEIEEEKEREiarlraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 473 RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE 552
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334
|
....
gi 1955802949 553 KAEK 556
Cdd:pfam13868 335 RQKK 338
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-573 |
2.20e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 34 RELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALEL----KRQEVAQKAQEMLEAQLREERE 109
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleeAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 110 QEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELE--RMEKERLAAQ 187
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 188 SFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKE 267
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 268 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKE---RIVKERAAKGKAEKERIEKERAAKEKA 344
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 345 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 424
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 425 EKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERA 504
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 505 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKER 573
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
209-522 |
3.22e-16 |
|
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: 80.73 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 209 AEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKE---RIEKERAAKEKAEKERIEKERAAKEKAE 285
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 286 KERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKerAAKEKAEKE-RLEKERAAKEKAEKEGI 364
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE--YLKEKAEREeEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 365 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 444
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 445 AKEKAEKERIVKERAAKgkaEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE 522
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEK---RRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
20-733 |
9.20e-16 |
|
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: 81.94 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 20 EVASKKNRTKEHPTRELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEM 99
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 100 LEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERM 179
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 180 EKERLAAQSFSKEKAEKERLERERVAKEKAEKERLE----KERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAE 255
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSrqklEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 256 KERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKE----RIVKERAAKGKAEK 331
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpILNLAQLDKATLEA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 332 ERIEKERAAKEKAEKERLEKERAAKEKAeKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEK 411
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKA-KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 412 ERAAKEKAEKERIEKERAAKEKAEKERLE---KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKER 488
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 489 AAKEKAEKEGIEKERAAKEKAEKErIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEK 568
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKA-QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 569 AEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVP 648
Cdd:pfam02463 854 EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 649 KGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEqlpkiEREQLPKAKAGKERAEKERLL 728
Cdd:pfam02463 934 EEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE-----ERYNKDELEKERLEEEKKKLI 1008
|
....*
gi 1955802949 729 KEKID 733
Cdd:pfam02463 1009 RAIIE 1013
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
269-589 |
1.24e-15 |
|
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: 79.19 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 269 AEKERIEKERAAKEKAEKERLEKERaakEKAEKERLEKERAAKEKAEKERivkeraakgKAEKERIEKERAAKEKAEKER 348
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKEEERKEERKRYR---------QELEEQIEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 349 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKER 428
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 429 AAKEKAEKERL----EKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERA 504
Cdd:pfam13868 177 EIEEEKEREIArlraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 505 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENE 584
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
....*
gi 1955802949 585 RLEKE 589
Cdd:pfam13868 337 KKLKE 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
44-757 |
6.51e-15 |
|
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: 79.25 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 44 LKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLE-AQLREEREQEEKREAERRAHE 122
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKkAEKELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 123 QAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERE 202
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 203 RVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKER-ADKEKAEKERIEKERAAKEKAEKERIEKERAAK 281
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDlLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 282 EKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 361
Cdd:pfam02463 507 SGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 362 EGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEK 441
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 442 ERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIE-KERAA 520
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLlKQKID 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 521 KEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEK 600
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 601 ERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEK 680
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 681 ERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEkidgERVVKEKRAKQAKEEMPEKNANN 757
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE----EEEERNKRLLLAKEELGKVNLMA 979
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
163-457 |
1.64e-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: 75.73 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVaKEKAEKERIEKERATKEKAEKE 242
Cdd:pfam13868 47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEK------ERAAKEKAEKERLEKERaaKEKAEKERLEKERAAKEKAEK 316
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekaEREEEREAEREEIEEEK--EREIARLRAQQEKAQDEKAER 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 317 ERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEK 396
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 397 ERaakEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 457
Cdd:pfam13868 284 RR---MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
126-768 |
2.83e-14 |
|
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: 77.32 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 126 KERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVA 205
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 206 KEKAEKERLEKERVAKEKAEKERIEKERatKEKAEKERIEKERADKEKAEKERiEKERAAKEKAEKERIEKERAAKEKAE 285
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENK--EEEKEKKLQEEELKLLAKEEEEL-KSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 286 KERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 365
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 366 KE-RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 444
Cdd:pfam02463 405 KEaQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 445 AKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKA 524
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 525 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLT 604
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 605 KENAKKEKENSE-RVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERA 683
Cdd:pfam02463 645 ESGLRKGVSLEEgLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 684 AVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSK 763
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
....*
gi 1955802949 764 KEKIM 768
Cdd:pfam02463 805 ALEEE 809
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
374-680 |
2.84e-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: 74.96 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 374 AEKERIEKERAAKEKAEKERLEKERaakEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKER 453
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 454 IVK----ERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERL 529
Cdd:pfam13868 106 IVEriqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKERE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 530 ------EKERAAKEKAEKEGIEKERAAKEKAEKERiEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKgrlEKERL 603
Cdd:pfam13868 186 iarlraQQEKAQDEKAERDELRAKLYQEEQERKER-QKEREEAEKKARQRQELQQAREEQIELKERRLAEEA---EREEE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 604 TKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVpKGKERERVAKERAEKERAEKEQQAKELAAKEK 680
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQ-RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
246-627 |
1.57e-13 |
|
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: 74.62 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 246 KERADKEKAEKERIEKERAAKEKAEKERiEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAA 325
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRK-KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 326 KGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 405
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 406 KERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLE 485
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 486 KERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAT 565
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 566 KEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKER 627
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
16-767 |
1.93e-13 |
|
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: 74.24 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 16 ESPGEVASKKNRTKEHPTRELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQK 95
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 96 AQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREA----------EEKAEKERLEKEKL 165
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKEsekekkkaekELKKEKEEIEELEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 166 EKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERI---EKERATKEKAEKE 242
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqlLLELARQLEDLLK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 402
Cdd:pfam02463 503 SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 403 KAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 482
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 483 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKE 562
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 563 RATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERM 642
Cdd:pfam02463 743 QKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 643 ERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKghLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERA 722
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE--ELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1955802949 723 EKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKI 767
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
261-748 |
3.14e-13 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 72.76 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 261 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLeKERAAKEKAEkerivkERAAKGKAEKERIEKERAA 340
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAE------EEAREAKAEAEQRAAELAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 341 KEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE 420
Cdd:COG3064 74 EAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 421 KERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAeKERLEKERAAKEKAEKEGIE 500
Cdd:COG3064 154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA-DAALLALAVAARAAAASREA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 501 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAA 580
Cdd:COG3064 233 ALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 581 KENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKER 660
Cdd:COG3064 313 AEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGIL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 661 AEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKE 740
Cdd:COG3064 393 AAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALD 472
|
....*...
gi 1955802949 741 KRAKQAKE 748
Cdd:COG3064 473 GGAVLADL 480
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
220-407 |
6.07e-13 |
|
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: 71.03 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 220 AKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 299
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 300 EKErlEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI 379
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*...
gi 1955802949 380 EKERAAKEKAEKERLEKERAAKEKAEKE 407
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
186-612 |
8.15e-13 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 71.61 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 186 AQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKeriekerADKEKAEKERIEKERAA 265
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-------AREAKAEAEQRAAELAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 266 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAE 345
Cdd:COG3064 74 EAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 346 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAeKERLEKERAAKEKAEKERIE 425
Cdd:COG3064 154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA-DAALLALAVAARAAAASREA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 426 KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAA 505
Cdd:COG3064 233 ALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 506 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENER 585
Cdd:COG3064 313 AEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGIL 392
|
410 420
....*....|....*....|....*..
gi 1955802949 586 LEKEQLAKEKGRLEKERLTKENAKKEK 612
Cdd:COG3064 393 AAAGGGGLLGLRLDLGAALLEAASAVE 419
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
236-422 |
8.57e-13 |
|
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: 70.26 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 236 KEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE 315
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 316 KERivKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLE 395
Cdd:TIGR02794 127 KQA--AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
170 180
....*....|....*....|....*..
gi 1955802949 396 KERAAKEKAEKERLEKERAAKEKAEKE 422
Cdd:TIGR02794 205 AAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
286-575 |
9.66e-13 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 71.95 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 286 KERLEKERAAKEKAeKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEkerlEKERAAKEKAEKEgIE 365
Cdd:TIGR00927 613 KEQLSRRPVAKVMA-LGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IP 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 366 KERAAKEKAEKERIEKEraAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 445
Cdd:TIGR00927 687 AERKGEQEGEGEIEAKE--ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKET 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 446 KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAE 525
Cdd:TIGR00927 765 EHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGE 844
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 526 KErlEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIE 575
Cdd:TIGR00927 845 AK--QDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
310-498 |
9.99e-13 |
|
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: 70.26 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 310 AKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKA 389
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 390 EKErlEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERI 469
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*....
gi 1955802949 470 EKERAAKEKAEKERLEKERAAKEKAEKEG 498
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEA 232
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
231-702 |
1.25e-12 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 70.84 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 231 KERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERI---EKERAAKEKAEKERLEKERAAKEKAEKERLEKE 307
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaelEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE 387
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 468 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIeKE 547
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV-LA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 548 RAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKER 627
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 628 AEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETE 702
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGG 474
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
220-685 |
2.56e-12 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 70.07 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 220 AKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERI---EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK 296
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaelEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 297 EKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 376
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 377 ERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVK 456
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 457 ERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKE-KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 535
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVvAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 536 KEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENS 615
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 616 ERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAV 685
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGG 474
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
267-542 |
2.86e-12 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 70.36 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 267 EKAEKERIEKERAAKEKAeKERLE--KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKeka 344
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIK--- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 345 ekerlekeraAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 424
Cdd:PRK05035 510 ----------AGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 425 EKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERiEKERAAKEKAEKERLEKERAAKEKAEKEgIEKERA 504
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR-AKAKKAEQQANAEPEEPVDPRKAAVAAA-IARAKA 657
|
250 260 270
....*....|....*....|....*....|....*...
gi 1955802949 505 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 542
Cdd:PRK05035 658 RKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
355-543 |
3.84e-12 |
|
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: 68.33 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 355 AKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKA 434
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 435 EKErlEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI 514
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*....
gi 1955802949 515 EKERAAKEKAEKERLEKERAAKEKAEKEG 543
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEA 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
340-527 |
3.87e-12 |
|
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: 68.33 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 340 AKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKA 419
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 420 EKEriEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGI 499
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*...
gi 1955802949 500 EKERAAKEKAEKERIEKERAAKEKAEKE 527
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
370-557 |
5.50e-12 |
|
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: 67.95 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 370 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 449
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 450 EKERivKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERL 529
Cdd:TIGR02794 126 AKQA--AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*...
gi 1955802949 530 EKERAAKEKAEKEGIEKERAAKEKAEKE 557
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
265-452 |
6.71e-12 |
|
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: 67.56 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 265 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKA 344
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 345 EKErlEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 424
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....*...
gi 1955802949 425 EKERAAKEKAEKERLEKERAAKEKAEKE 452
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
182-363 |
8.72e-12 |
|
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: 67.18 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 182 ERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKEriEK 261
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ--AA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 262 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAK 341
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180
....*....|....*....|..
gi 1955802949 342 EKAEKERLEKERAAKEKAEKEG 363
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEA 232
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
196-500 |
9.27e-12 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 68.87 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 196 KERLERERVAKEKAeKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEkeriEKERAAKEKAEKErIE 275
Cdd:TIGR00927 613 KEQLSRRPVAKVMA-LGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IP 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 276 KERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAA 355
Cdd:TIGR00927 687 AERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEH 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 356 KEKAEKEGIEKERaakekaekeriEKERAAKEKAEKERLEKERAAKEKaekerlEKERAAKEKAEKERIEKERAAKEKAE 435
Cdd:TIGR00927 767 EGETEAEGKEDED-----------EGEIQAGEDGEMKGDEGAEGKVEH------EGETEAGEKDEHEGQSETQADDTEVK 829
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 436 KERLEKERAAKEKAEKERivKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 500
Cdd:TIGR00927 830 DETGEQELNAENQGEAKQ--DEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
366-749 |
1.48e-11 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 67.37 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 366 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLeKERAAKEKAEKERIEKERAAKEKAEKERLEkerAA 445
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAE---AA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 446 KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKegiEKERAAKEKAEKERIEKERAAKEKAE 525
Cdd:COG3064 77 KKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKR---KAEEEAKRKAEEERKAAEAEAAAKAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 526 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTK 605
Cdd:COG3064 154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 606 ENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAV 685
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 686 KGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEE 749
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLL 377
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
237-497 |
1.70e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.67 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 237 EKAEKERIEKERADKEKAeKERIE--KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK--E 312
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKagA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 313 KAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKE 392
Cdd:PRK05035 513 RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 393 RLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKEraAKEKAEKERIVKERAAKGKAEKERIEKE 472
Cdd:PRK05035 593 KAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVD--PRKAAVAAAIARAKARKAAQQQANAEPE 670
|
250 260
....*....|....*....|....*
gi 1955802949 473 RAAKEKAEKERLEKERAAKEKAEKE 497
Cdd:PRK05035 671 EAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
162-437 |
1.82e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 68.10 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 162 KEKLEKERIEKKTELERMEKERLA-AQSFSKEKAEKERLERERVAKEKAEKE-----RLEKERVAKEKAEKErIEKERAT 235
Cdd:TIGR00927 613 KEQLSRRPVAKVMALGDLSKGDVAeAEHTGERTGEEGERPTEAEGENGEESGgeaeqEGETETKGENESEGE-IPAERKG 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 236 KEKAEKErIEKERADkEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE 315
Cdd:TIGR00927 692 EQEGEGE-IEAKEAD-HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 316 KERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLE 395
Cdd:TIGR00927 770 TEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDE 849
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1955802949 396 KERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKE 437
Cdd:TIGR00927 850 KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
187-450 |
1.98e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.67 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 187 QSFSKEKAEKERLERERVAKEKAeKERLE--KERVAKEKAEKEriekERAtKEKAEKERIEKERADKEKAEKERIEKERA 264
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAARE----ARH-KKAAEARAAKDKDAVAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 265 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAK--GKAEKERIEKERAAKE 342
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQqaANAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 343 KAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKErAAKEKAEKERLEKErAAKEKAEKE 422
Cdd:PRK05035 583 AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP-EEPVDPRKAAVAAA-IARAKARKA 660
|
250 260
....*....|....*....|....*...
gi 1955802949 423 RIEKERAAKEKAEKERLEKERAAKEKAE 450
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-682 |
2.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLE------KERVAKEKAEKERIEKERA 234
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 235 TKEKAEKERIEKERADKEKAEKERIEKEraaKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKA 314
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKR---LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 315 EKERIVKERAAKGKAEKERIEKERAakeKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKERIEKERAAKEKAEKERL 394
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKL---EKELEELEKAKEEIEEEISK--ITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 395 EKERAAKEKAEKERLEKERAAKEKAEKERIE-KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKER 473
Cdd:PRK03918 440 VCGRELTEEHRKELLEEYTAELKRIEKELKEiEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 474 AAKEKAEKERLeKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKEGIEKERAAKE 552
Cdd:PRK03918 520 LEKKAEEYEKL-KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 553 KAEKERIEKERATKEKaekeRIEKERAAKENERLEK--EQLAKEKGRLEKERlTKENAKKEKENSERVEKERVAKERAEK 630
Cdd:PRK03918 599 PFYNEYLELKDAEKEL----EREEKELKKLEEELDKafEELAETEKRLEELR-KELEELEKKYSEEEYEELREEYLELSR 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 631 ERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKER 682
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
178-442 |
2.54e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 178 RMEKERLAAQSFSKEKAEKERlERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKE 257
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAK-ARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 258 RIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK--EKAEKERIVKERAAKGKAEKERIE 335
Cdd:PRK05035 511 GARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQqaANAEAEEEVDPKKAAVAAAIARAK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 336 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiEKERAAKEKAEKERLEKErAAKEKAEKERLEKERAA 415
Cdd:PRK05035 591 AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA-NAEPEEPVDPRKAAVAAA-IARAKARKAAQQQANAE 668
|
250 260
....*....|....*....|....*..
gi 1955802949 416 KEKAEKERIEKERAAKEKAEKERLEKE 442
Cdd:PRK05035 669 PEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
323-589 |
2.74e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEK----AEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKER 398
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 399 AAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKErivKERAAKGKAEKERIEKERAAKEK 478
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQ---AANAEAEEEVDPKKAAVAAAIAR 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 479 AEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKErlekERAAKEKAEKEGIEKERAAKEKAEKER 558
Cdd:PRK05035 589 AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP----EEPVDPRKAAVAAAIARAKARKAAQQQ 664
|
250 260 270
....*....|....*....|....*....|.
gi 1955802949 559 IEKERATKEKAEKERIEKERAAKENERLEKE 589
Cdd:PRK05035 665 ANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
310-771 |
2.82e-11 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 66.60 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 310 AKEKAEKERIVKERAAKGKAEK-ERIEKERAAKEKAEKERLeKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEK 388
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKrAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 389 AEKERLEKERAAKEKAEKERLEKERAAKEKAEKEriekerAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKER 468
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAA------AEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 469 IEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKER------IEKERAAKEKAEKERLEKERAAKEKAEKE 542
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAalaaaaAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 543 GIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKER 622
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 623 VAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETE 702
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 703 QLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAIR 771
Cdd:COG3064 397 GGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGI 465
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
222-487 |
4.07e-11 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 66.51 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 222 EKAEKERIEKERATKEKAeKERIEkerADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 301
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFE---ARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 302 ERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE--RAAKEKAEKERI 379
Cdd:PRK05035 510 AGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVdpKKAAVAAAIARA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 380 EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERiEKERAAKEKAEKERLEKErAAKEKAEKERIVKERA 459
Cdd:PRK05035 590 KAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA-NAEPEEPVDPRKAAVAAA-IARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*...
gi 1955802949 460 AKGKAEKERIEKERAAKEKAEKERLEKE 487
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
161-608 |
4.24e-11 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 66.22 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:COG3064 14 AQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERlEKERAAKEKAEKERIV 320
Cdd:COG3064 94 AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA-ARAAAAAAAAAAAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 321 KERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 400
Cdd:COG3064 173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 401 KEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAE 480
Cdd:COG3064 253 DLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 481 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIE 560
Cdd:COG3064 333 GAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALL 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1955802949 561 KERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENA 608
Cdd:COG3064 413 EAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDAD 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-681 |
4.49e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 196 KERLERERVAKEKAEKERLEKERVAKEKaEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKeraAKEKAEKERIE 275
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLREINEISSELPELREELEKLEKEVKELEE---LKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 276 KERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKaEKERLEKERAA 355
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK-RLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 356 KEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAE 435
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 436 KERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE-KERAAKEKAEKERI 514
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEiEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 515 EKERAAKEK--AEKERLEKERAAKEKAEKEGIEKERAAKEKAEKeriEKERATKEKAEKERIEKERAAKENERLEKEQLA 592
Cdd:PRK03918 486 EKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK---LKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 593 KEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQA 672
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
....*....
gi 1955802949 673 KELAAKEKE 681
Cdd:PRK03918 643 EELRKELEE 651
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
61-397 |
1.89e-10 |
|
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: 63.01 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 61 AEMALAEVRSILAKEEEERQLVNALELKRQEvaqKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLERE 140
Cdd:pfam13868 13 SKLLAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 141 EKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVA 220
Cdd:pfam13868 90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 221 KEKAEKERIEKERatKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 300
Cdd:pfam13868 170 EREAEREEIEEEK--EREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 301 KERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERaakEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIE 380
Cdd:pfam13868 248 KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
330
....*....|....*..
gi 1955802949 381 KERAAKEKAEKERLEKE 397
Cdd:pfam13868 325 AERRERIEEERQKKLKE 341
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-497 |
2.23e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 32 PTRELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQE 111
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 112 EKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEK-LEKERIEKKTELERMEKERLAAQSFS 190
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 191 KEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKE---RIEKERADKEKAEKERIEKERAAKE 267
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrGLAGAVAVLIGVEAAYEAALEAALA 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 268 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 347
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 348 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKE 427
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 428 RAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 497
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
437-755 |
2.45e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 437 ERLEKERaakEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEK 516
Cdd:COG1196 203 EPLERQA---EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 517 ERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKG 596
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 597 RLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERvpkgkerervAKERAEKERAEKEQQAKELA 676
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE----------EALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 677 AKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNA 755
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
386-750 |
3.19e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 63.13 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 386 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKERIVKERAAKGKAE 465
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ--AEEEAREAKAEAEQRAAELAAEAAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 466 KERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 545
Cdd:COG3064 79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 546 KERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAK 625
Cdd:COG3064 159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 626 ERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLP 705
Cdd:COG3064 239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1955802949 706 KIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEM 750
Cdd:COG3064 319 AAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGAL 363
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
43-358 |
6.51e-10 |
|
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: 61.47 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 43 ALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEKREAERRAHE 122
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 123 QAGKERLEKEQLEQLEREEKERL-EKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLER 201
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 202 ERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAK 281
Cdd:pfam13868 189 LRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLR 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 282 EKAEKERLEKERAAKEKAEKERLekeraakeKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEK 358
Cdd:pfam13868 269 KQAEDEEIEQEEAEKRRMKRLEH--------RRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
323-428 |
1.19e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 62.06 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAK-EKAEKEGIEKERAakEKAEKERIEKERAAKEKAEKERLEKERAak 401
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1955802949 402 ekaekERLEKERAakEKAEKERIEKER 428
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-475 |
1.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 34 RELGRKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEK 113
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 114 REAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEK 193
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 194 AEKERLERERVAKEKAEKERLEkeRVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKER 273
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 274 IEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKER 353
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 354 AAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEK 433
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1955802949 434 AEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAA 475
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
463-716 |
1.34e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.50 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 463 KAEKERIEKERAAKEKAeKERLEkerAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 542
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEA-KARFE---ARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 543 GIEKERAAKEKAEKERIEKERATKEKAEKeriekerAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKER 622
Cdd:PRK05035 511 GARPDNSAVIAAREARKAQARARQAEKQA-------AAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 623 VAKERAEKERVAKESEKERMERERVPKGKERERVAK--ERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVE 700
Cdd:PRK05035 584 AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAaiARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQ 663
|
250
....*....|....*.
gi 1955802949 701 TEQLPKIEREQLPKAK 716
Cdd:PRK05035 664 QANAEPEEAEDPKKAA 679
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
301-595 |
1.51e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.94 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 301 KERLEKERAAKEKAeKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKeraAKEKAEKEGiEKERAAKEKAEKErIE 380
Cdd:TIGR00927 613 KEQLSRRPVAKVMA-LGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEE---SGGEAEQEG-ETETKGENESEGE-IP 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 381 KERAAKEKAEKERLEKEraAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERivkeraa 460
Cdd:TIGR00927 687 AERKGEQEGEGEIEAKE--ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVET------- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 461 kgKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKaekeriEKERAAKEKAEKERLEKERAAKEKAE 540
Cdd:TIGR00927 758 --EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEH------EGETEAGEKDEHEGQSETQADDTEVK 829
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 541 KEGIEKERAAKEKAEKERIEK--------ERATKEKAEKERIEKERAAKENERLEKEQLAKEK 595
Cdd:TIGR00927 830 DETGEQELNAENQGEAKQDEKgvdggggsDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
312-571 |
1.51e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.50 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 312 EKAEKERIVKERAAKGKAeKERIE--KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKA 389
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 390 EKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAekeRLEKERAAKEKAEKERIVKERAAKGKAEKERI 469
Cdd:PRK05035 513 RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARA---KAKKAAQQAANAEAEEEVDPKKAAVAAAIARA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 470 EKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiEKERAAKEKAEKERLEKE--RAAKEKAEKEGIEKE 547
Cdd:PRK05035 590 KAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQQANAE 668
|
250 260
....*....|....*....|....
gi 1955802949 548 RAAKEKAEKERIEKERAtKEKAEK 571
Cdd:PRK05035 669 PEEAEDPKKAAVAAAIA-RAKAKK 691
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
338-443 |
1.56e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 61.68 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 338 RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAK-EKAEKERIEKERAakEKAEKERLEKERAAKEKAEKERLEKERAak 416
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1955802949 417 ekaekERIEKERAakEKAEKERLEKER 443
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
203-308 |
1.63e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 61.68 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 203 RVAKEKAEKERLEKERVAKEKAEKERIEKERATK-EKAEKERIEKERAdkEKAEKERIEKERAAKEKAEKERIEKERAak 281
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1955802949 282 ekaekERLEKERAakEKAEKERLEKER 308
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
280-482 |
2.28e-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: 59.86 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 280 AKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERivkeraakgKAEKERIEKERAAKEKAEKERlEKERAAKEKA 359
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR---------AAEQARQKELEQRAAAEKAAK-QAEQAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 360 EKEGIEKERAAKEkaekeriEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERL 439
Cdd:TIGR02794 116 EKQKQAEEAKAKQ-------AAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955802949 440 EKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 482
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
357-602 |
3.14e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 60.35 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 357 EKAEKEGIEKERAAKEKAeKERIE--KERAAKEKAEKErlekERaAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKA 434
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAARE----AR-HKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 435 EKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE--RAAKEKAEKE 512
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVdpKKAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 513 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiEKERATKEKAEKERIEKERAAKENERLEKEQLA 592
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQA-NAEPEEPVDPRKAAVAAAIARAKARKAAQQQAN 666
|
250
....*....|
gi 1955802949 593 KEKGRLEKER 602
Cdd:PRK05035 667 AEPEEAEDPK 676
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
368-473 |
3.22e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 60.52 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 368 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAK-EKAEKERLEKERAakEKAEKERIEKERAAKEKAEKERLEKERAAK 446
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90 100
....*....|....*....|....*..
gi 1955802949 447 ekaekerivKERAAKGKAEKERIEKER 473
Cdd:PTZ00266 507 ---------LERERVDRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
233-338 |
4.53e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 60.14 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 233 RATKEKAEKERIEKERADKEKAEKERIEKERAAK-EKAEKERIEKERAakEKAEKERLEKERAAKEKAEKERLEKERAAK 311
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90 100
....*....|....*....|....*..
gi 1955802949 312 ekaekerivKERAAKGKAEKERIEKER 338
Cdd:PTZ00266 507 ---------LERERVDRLERDRLEKAR 524
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
247-530 |
4.75e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 60.01 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 247 ERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAK 326
Cdd:TIGR00927 609 ELWVKEQLSRRPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 327 GKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKerlEKERAAKEKAEK 406
Cdd:TIGR00927 689 RKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKH---EVETEGDRKETE 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 407 ERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKE---KAEKER 483
Cdd:TIGR00927 766 HEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQElnaENQGEA 845
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1955802949 484 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLE 530
Cdd:TIGR00927 846 KQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
458-563 |
5.60e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 59.75 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 458 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAK-EKAEKEGIEKERAakEKAEKERIEKERAAKEKAEKERLEKERAAK 536
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90 100
....*....|....*....|....*..
gi 1955802949 537 ekaekegieKERAAKEKAEKERIEKER 563
Cdd:PTZ00266 507 ---------LERERVDRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
353-448 |
9.03e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 59.37 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 353 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAK-EKAEKERLEKERAakEKAEKERLEKERAAKEKAEKERIEKERAAK 431
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90
....*....|....*...
gi 1955802949 432 -EKAEKERLEKERAAKEK 448
Cdd:PTZ00266 507 lERERVDRLERDRLEKAR 524
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
317-590 |
9.89e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 59.24 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 317 ERIVKERAAKGKAEK----ERIEKERAAKEKAEKERLEKEraAKEKAEKEGIEKERAAKEKAEKEriEKERAAKEKAEKE 392
Cdd:TIGR00927 609 ELWVKEQLSRRPVAKvmalGDLSKGDVAEAEHTGERTGEE--GERPTEAEGENGEESGGEAEQEG--ETETKGENESEGE 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 393 rLEKERAAKEKAEKERLEKEraAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKE 472
Cdd:TIGR00927 685 -IPAERKGEQEGEGEIEAKE--ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDR 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 473 RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE 552
Cdd:TIGR00927 762 KETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 553 KAEKERIEK-------------ERATKEKAEKERIEKERAAKENERLEKEQ 590
Cdd:TIGR00927 842 QGEAKQDEKgvdggggsdggdsEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
161-407 |
1.04e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:PRK05035 444 EKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAK-------EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEK 313
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAvaaaiarAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEP 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 314 AEKERIVKERAAKGKAEKERiEKERAAKEKAEKERLEKERAAKEKAEKEgIEKERAAKEKAEKERIEKERAAKEKAEKER 393
Cdd:PRK05035 604 EEQVAEVDPKKAAVAAAIAR-AKAKKAEQQANAEPEEPVDPRKAAVAAA-IARAKARKAAQQQANAEPEEAEDPKKAAVA 681
|
250
....*....|....
gi 1955802949 394 LEKERAAKEKAEKE 407
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
232-532 |
1.21e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 58.85 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 232 ERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKE-RLEKERAAKEKAEKER---LEKE 307
Cdd:TIGR00927 609 ELWVKEQLSRRPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGgEAEQEGETETKGENESegeIPAE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKekAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiekeraake 387
Cdd:TIGR00927 689 RKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE--AEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVET--------- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKaekerlEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:TIGR00927 758 EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEH------EGETEAGEKDEHEGQSETQADDTEVKDE 831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 468 RIEKERAAKEKAEKErlEKERAAKEKAEKEGIEKERaaKEKAEKERIEKERAAKEKAEKERLEKE 532
Cdd:TIGR00927 832 TGEQELNAENQGEAK--QDEKGVDGGGGSDGGDSEE--EEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
367-682 |
1.22e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 58.85 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 367 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKE-RIEKERAAKEKAEKER---LEKE 442
Cdd:TIGR00927 609 ELWVKEQLSRRPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGgEAEQEGETETKGENESegeIPAE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 443 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKekAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiekeraake 522
Cdd:TIGR00927 689 RKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE--AEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVET--------- 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 523 kaEKERLEKERAAKEKAEKEGIEKErAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKER 602
Cdd:TIGR00927 758 --EGDRKETEHEGETEAEGKEDEDE-GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGE 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 603 --LTKENAKKEKENSERVEkervakerAEKERVAKESEKERMERErvpkgKERERVAKERAEKERAEKEQQAKELAAKEK 680
Cdd:TIGR00927 835 qeLNAENQGEAKQDEKGVD--------GGGGSDGGDSEEEEEEEE-----EEEEEEEEEEEEEEEEEENEEPLSLEWPET 901
|
..
gi 1955802949 681 ER 682
Cdd:TIGR00927 902 RQ 903
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
402-674 |
1.23e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 402 EKAEKERLEKERAAKEKAeKERIEkeraakekAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEK 481
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFE--------ARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 482 ERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEK 561
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 562 ERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKER 641
Cdd:PRK05035 585 AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ 664
|
250 260 270
....*....|....*....|....*....|...
gi 1955802949 642 MERErvPKGKERERVAKERAEKERAEKEQQAKE 674
Cdd:PRK05035 665 ANAE--PEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
174-268 |
1.47e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 58.60 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 174 TELERMEKERLAAQSFSKEKAEKERLERervaKEKAEKERLEKERVakEKAEKERIEKERATKEKAEKERIEKERADK-E 252
Cdd:PTZ00266 435 AERARIEKENAHRKALEMKILEKKRIER----LEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDRlE 508
|
90
....*....|....*.
gi 1955802949 253 KAEKERIEKERAAKEK 268
Cdd:PTZ00266 509 RERVDRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
263-358 |
1.48e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 58.60 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 263 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAK-EKAEKERLEKERAakEKAEKERIVKERAAKGKAEKERIEKERAAK 341
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90
....*....|....*...
gi 1955802949 342 -EKAEKERLEKERAAKEK 358
Cdd:PTZ00266 507 lERERVDRLERDRLEKAR 524
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
417-685 |
2.27e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.65 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 417 EKAEKERIEKERAAKEKAeKERLE--KERAAKEKAEKErivkERAAKgKAEKERIEKERAAKEKAEKERLEKERAAKEKA 494
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFEarQARLEREKAARE----ARHKK-AAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 495 EKEGIEKERAAKEKAEKERIEKERAAKEKAEKerlekerAAKEKAEKEGIEkerAAKEKAEKERIEKERATKEKAEKERI 574
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQA-------AAAADPKKAAVA---AAIARAKAKKAAQQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 575 EKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKerAEKERVAKESEKERMERERVPkgKERE 654
Cdd:PRK05035 578 KKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKK--AEQQANAEPEEPVDPRKAAVA--AAIA 653
|
250 260 270
....*....|....*....|....*....|.
gi 1955802949 655 RVAKERAEKERAEKEQQAKELAAKEKERAAV 685
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAAVAAAI 684
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
471-783 |
2.71e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.97 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 471 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgiekerAA 550
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELA------AE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 551 KEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEK 630
Cdd:COG3064 75 AAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 631 ERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIERE 710
Cdd:COG3064 155 EAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 711 QLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAIRDLLKPKATKVNK 783
Cdd:COG3064 235 AAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAEL 307
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
398-493 |
5.55e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 56.67 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 398 RAAKEKAEKERLEKERAAKEKAEKERIEKERAAK-EKAEKERLEKERAakEKAEKERIVKERAAKGKAEKERIEKERAAK 476
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90
....*....|....*...
gi 1955802949 477 -EKAEKERLEKERAAKEK 493
Cdd:PTZ00266 507 lERERVDRLERDRLEKAR 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-616 |
6.18e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 165 LEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIE-KERATKEKAEKER 243
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 244 IEKER------ADKEKAEKERIEKERAAKEKAEKE---RIEKERAAKEKAEKE---RLEKERAAKEKAEKERLEKERAAK 311
Cdd:PRK02224 291 LEEERddllaeAGLDDADAEAVEARREELEDRDEElrdRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 312 EKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLE----KERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE 387
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNaedfLEELREERDELREREAELEATLRTARERVEEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKaEKERLEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:PRK02224 451 AGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 468 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 548 RAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSE 616
Cdd:PRK02224 610 RLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
18-233 |
7.35e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 56.28 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 18 PGEVASKKNRTKEHPTRELGRKlksalkeqlrmihEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQE---VAQ 94
Cdd:PTZ00266 318 PGAVVARRNPSKEHPGLQLAAM-------------EKAKHAEAANYGISPNTLINQRNEEQHGRRSSSCASRQSannVTN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 95 KAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKT 174
Cdd:PTZ00266 385 ITSITSVTSVASVASVASVPSKDDRKYPQDGATHCHAVNGHYGGRVDKDHAERARIEKENAHRKALEMKILEKKRIERLE 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 175 ELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEK-ERVAKEKAEKERIEKER 233
Cdd:PTZ00266 465 REERERLERERMERIERERLERERLERERLERDRLERDRLDRlERERVDRLERDRLEKAR 524
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
161-344 |
8.65e-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: 54.85 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERvAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKEriV 320
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAE--A 209
|
170 180
....*....|....*....|....
gi 1955802949 321 KERAAKGKAEKERIEKERAAKEKA 344
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADEAE 233
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
352-672 |
8.77e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 352 ERAAKEKAEKegIEKERAAKEKAEKERIEKERAAKEKAEKER-LEKERAAKEKAEKERLEKERaakeKAEKERIEKERAA 430
Cdd:pfam17380 286 ERQQQEKFEK--MEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAAIYAEQERMAMER----ERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 431 KEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKekaekeRLEKERAAKEKAEKEGIEKERAAKEKAE 510
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK------ILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 511 KERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEq 590
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 591 laKEKGRLEKERLTKENAKKEKENSERVEKE-RVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKE 669
Cdd:pfam17380 513 --RKRKLLEKEMEERQKAIYEEERRREAEEErRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
...
gi 1955802949 670 QQA 672
Cdd:pfam17380 591 YEA 593
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
407-703 |
9.16e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 407 ERLEKERAAKEKAEKERIEKERAAKEKAEKER-LEKERAAKEKAEKERIVKERaakgkaeKERIEKERAAKEKAEKERLE 485
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAAIYAEQERMAMER-------ERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 486 KERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAt 565
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 566 kEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERA--EKERVAKESEKERME 643
Cdd:pfam17380 446 -REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKLLEKEMEE 524
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 644 RERVPKGKERERVAKE--RAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQ 703
Cdd:pfam17380 525 RQKAIYEEERRREAEEerRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK 586
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
488-581 |
1.50e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 55.13 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 488 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAK-EKAEKERLEKERAakEKAEKEGIEKERAAKEKAEKERIEKERATK 566
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
|
90
....*....|....*.
gi 1955802949 567 -EKAEKERIEKERAAK 581
Cdd:PTZ00266 507 lERERVDRLERDRLEK 522
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
226-515 |
2.11e-07 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 54.67 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 226 KERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERiEKERAAKEKAEKERLEKERAAKEKAEKERLE 305
Cdd:PTZ00108 1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVE-EKEIAKEQRLKSKTKGKASKLRKPKLKKKEK 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 306 KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAA 385
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 386 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI-EKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKA 464
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGgSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKT 1339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 465 EKERIEKERAAKEKAEKERLEKEraaKEKAEKEGIEKERAAKEKAEKERIE 515
Cdd:PTZ00108 1340 RVKQASASQSSRLLRRPRKKKSD---SSSEDDDDSEVDDSEDEDDEDDEDD 1387
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
413-533 |
2.82e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 54.36 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 413 RAAKEKAEKERIEKERAAKEKAEKERLEKERAakEKAEKERIvkeraakgkaekERIEKERAakEKAEKERLEKERAAKE 492
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRI--ERLEREER------------ERLERERM--ERIERERLERERLERE 492
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1955802949 493 KAEKEGIEKERAakekaekERIEKERAakEKAEKERLEKER 533
Cdd:PTZ00266 493 RLERDRLERDRL-------DRLERERV--DRLERDRLEKAR 524
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
160-378 |
2.90e-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: 53.80 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 160 LEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVakEKAEKERIEKERATKEKA 239
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 240 EKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKeraaKEKAEKERLEKERAAKEKAEKERI 319
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK----KQQEEAERAEAEKQRQKELEMQLA 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 320 VKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKER 378
Cdd:pfam15709 463 EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
475-686 |
3.04e-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: 53.31 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 475 AKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKA 554
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 555 EKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVA 634
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 635 KESEKERmerervpkgKERERVAKERAEKERAEKEQQAKELAAKEKERAAVK 686
Cdd:TIGR02794 206 AAEAAAK---------AEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
269-481 |
3.22e-07 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 54.23 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 269 AEKERIEKE--RAAKEKAEKERLEKERAAKEKAEKERLEKERAakekaekeRIVKERAAKGKAEKERIEKERAAKEKAEK 346
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRA--------RAEELREKRGKLEAHRAMLSGSEANSARR 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 347 ERLEKERAAKEKAEKEGIEKErAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERA-AKEKAEKERIE 425
Cdd:PRK14900 914 DTMEIQNEQKPTQDGPAAEAQ-PAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRsVKKAAATRAAM 992
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 426 KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKerAAKEKAEK 481
Cdd:PRK14900 993 KKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKK--AAKKPARK 1046
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
313-640 |
3.57e-07 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 53.90 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 313 KAEKERIVKERAAKGKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKEGIEKERAAKE----------KAEKERIEKE 382
Cdd:PTZ00108 1030 NAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEE--EGAEEDDEADDEDDEEELGAAVSydyllsmpiwSLTKEKVEKL 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 383 RAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERiEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKG 462
Cdd:PTZ00108 1108 NAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVE-EKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSA 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 463 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGI----EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK-E 537
Cdd:PTZ00108 1187 DKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSdqedDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDlS 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 538 KAEKEGIEKERAAKEKAEKERIEKeRATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSER 617
Cdd:PTZ00108 1267 KEGKPKNAPKRVSAVQYSPPPPSK-RPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQAS 1345
|
330 340
....*....|....*....|...
gi 1955802949 618 VEKERVAKERAEKERVAKESEKE 640
Cdd:PTZ00108 1346 ASQSSRLLRRPRKKKSDSSSEDD 1368
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
533-627 |
3.68e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 53.97 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 533 RAAKEKAEKEGIEKERAAKEKAEKERIEKERATK-EKAEKERIEKERAAK-ENERLEKEQLAKEkgRLEKERLTKENAKK 610
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERMERiERERLERERLERE--RLERDRLERDRLDR 506
|
90
....*....|....*...
gi 1955802949 611 -EKENSERVEKERVAKER 627
Cdd:PTZ00266 507 lERERVDRLERDRLEKAR 524
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
430-610 |
3.89e-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: 52.93 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 430 AKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKA 509
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 510 EKEriEKERAAKEKAEKERLEKERAAKeKAEKEGIEKERA-AKEKAEKERIEKERATKEKAEKER---IEKERAAKENER 585
Cdd:TIGR02794 126 AKQ--AAEAKAKAEAEAERKAKEEAAK-QAEEEAKAKAAAeAKKKAEEAKKKAEAEAKAKAEAEAkakAEEAKAKAEAAK 202
|
170 180
....*....|....*....|....*
gi 1955802949 586 LEKEQLAKEKGRLEKERLTKENAKK 610
Cdd:TIGR02794 203 AKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
293-398 |
4.47e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 53.59 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 293 RAAKEKAEKERLEKERAAKEKAEKERIVKERAAKG-KAEKERIEKERAakEKAEKERLEKERAAKEKAEKEGIEKERAak 371
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERLeREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1955802949 372 ekaekERIEKERAakEKAEKERLEKER 398
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
212-503 |
4.58e-07 |
|
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: 53.59 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 212 ERLEKERVAKEKAEKERIEKERATKEKAEKER-IEKERADKEKAEKERIEKERaakeKAEKERIEKERAAKEKAEKERLE 290
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAAIYAEQERMAMER----ERELERIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 291 KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKgkaekeRIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAA 370
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERVRQELEAARKVK------ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 371 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKE-RAAKEKAEKERLEKERAAKEKA 449
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEME 523
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 450 EKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKerAAKEKAEKEGIEKER 503
Cdd:pfam17380 524 ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK--ATEERSRLEAMERER 575
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
443-750 |
8.41e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 443 RAAKEKAEKERIVKERAAKgKAEKERIEKERAAKEKAEKERLEKERaakEKAEKEGIEKERAAKEKAEKERIEKERAAKE 522
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQ-IAEKKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 523 KAEKERLEKERAAKEKAE-KEGIEKERAAKEKAEKERIEKERATKE---KAEKERIEKERAAKENERLEKEQLAKEKGRL 598
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQmDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 599 EKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKE--------- 669
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqareeq 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 670 -QQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKE 748
Cdd:pfam13868 245 iELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
..
gi 1955802949 749 EM 750
Cdd:pfam13868 325 AE 326
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
93-534 |
8.49e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 52.35 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 93 AQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEK 172
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 173 KTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKE 252
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 253 KAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKE 332
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 333 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 412
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 413 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKE 492
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1955802949 493 KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 534
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVA 442
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-675 |
9.01e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 262 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAK 341
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 342 EKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE-----------KERLE 410
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyldelreiekrLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 411 KERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKERivkERAAKGKAEKERIEKERA--AKEKAEKERLEKE 487
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEElKKKLKELEKRLEELEERHELY---EEAKAKKEELERLKKRLTglTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 488 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAtKE 567
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEK-ER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 568 KAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVE--KERVAKERAEKERVAKESEKErmerE 645
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklKEKLIKLKGEIKSLKKELEKL----E 552
|
410 420 430
....*....|....*....|....*....|
gi 1955802949 646 RVPKGKERERVAKERAEKERAEKEQQAKEL 675
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
460-638 |
9.58e-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: 51.77 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 460 AKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 539
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 540 EKEGIEKERAAKEKAEKERI-------EKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKK-- 610
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKeeaakqaEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAka 205
|
170 180
....*....|....*....|....*...
gi 1955802949 611 EKENSERVEKERVAKERAEKERVAKESE 638
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-557 |
9.64e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 42 SALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEKREAERRAH 121
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 122 EQAG-----KERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLA--AQSFSKEKA 194
Cdd:PRK03918 290 EKAEeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerHELYEEAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 195 EKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERatKEKAEKERIEKERADKEKAEKERIEKE-------RAAKE 267
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS--KITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 268 KAEKERIEKERAAKEKAEKERLE-KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEK 346
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEiEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 347 ERLeKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIE 425
Cdd:PRK03918 528 EKL-KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 426 KERAAKE------KAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGI 499
Cdd:PRK03918 607 LKDAEKElereekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 500 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKE 557
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
246-435 |
1.22e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 246 KERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAA 325
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 326 KGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEK-ERAAKEKAEKErlekeraAKEKA 404
Cdd:PRK09510 155 RAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKaAAEAKKKAAAE-------AKAAA 227
|
170 180 190
....*....|....*....|....*....|.
gi 1955802949 405 EKERLEKERAAKEKAEKERIEKERAAKEKAE 435
Cdd:PRK09510 228 AKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
122-302 |
1.46e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 122 EQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAE-KERLE 200
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEaKAKQA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 201 RERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAA 280
Cdd:TIGR02794 130 AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEA 209
|
170 180
....*....|....*....|..
gi 1955802949 281 KEKAEKERLEKERAAKEKAEKE 302
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADE 231
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
520-703 |
1.61e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 520 AKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLe 599
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 600 KERLTKENAKKEKENSERVEKERvAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKE 679
Cdd:TIGR02794 125 KAKQAAEAKAKAEAEAERKAKEE-AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180
....*....|....*....|....
gi 1955802949 680 KERAAVKGHLVKEKTAKAKVETEQ 703
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
329-551 |
1.72e-06 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 51.92 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 329 AEKERIEKE--RAAKEKAEKERLEKERAAKEKAEKEGIEKERAakekaekeRIEKERAAKEKAEKERLEKERAAKEKAEK 406
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRA--------RAEELREKRGKLEAHRAMLSGSEANSARR 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 407 ERLEKERAAKEKAEKERIEKErAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERA-AKEKAEKERLE 485
Cdd:PRK14900 914 DTMEIQNEQKPTQDGPAAEAQ-PAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRsVKKAAATRAAM 992
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 486 KERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKerlekerAAKEKAEKEGIEKERAAK 551
Cdd:PRK14900 993 KKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARK-------PAAKKAAKKPARKAAGRK 1051
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
492-749 |
1.87e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.49 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 492 EKAEKEGIEKERAAKEKAeKERIEkeraakekAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEK 571
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEA-KARFE--------ARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 572 ERIEKERAAKENerleKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAeKERVAKESEKERMERERVPKGK 651
Cdd:PRK05035 505 PIVIKAGARPDN----SAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARA-KAKKAAQQAANAEAEEEVDPKK 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 652 ERERVAKERAEKERAEK----EQQAKELAAKEKERAAVKGHLVKEKTAKAK---VETEQL---PKIEREQLPKAKAGKER 721
Cdd:PRK05035 580 AAVAAAIARAKAKKAAQqaasAEPEEQVAEVDPKKAAVAAAIARAKAKKAEqqaNAEPEEpvdPRKAAVAAAIARAKARK 659
|
250 260 270
....*....|....*....|....*....|....
gi 1955802949 722 AEKERLLKEKIDGERVVKEK------RAKQAKEE 749
Cdd:PRK05035 660 AAQQQANAEPEEAEDPKKAAvaaaiaRAKAKKAA 693
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
350-540 |
1.89e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 350 EKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKErieKERA 429
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA---AAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 430 AKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEK-ERAAKEKAEKEGIEK-ERAAKE 507
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKaEAEAKKKAAAEAKKKaAAEAKA 225
|
170 180 190
....*....|....*....|....*....|...
gi 1955802949 508 KAEKERIEKERAAKEKAEKERLEKERAAKEKAE 540
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
239-568 |
2.59e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 239 AEKERIEKERADKEKAEKERI-EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEK--ERAAKEKAE 315
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 316 KERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAK-EKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERL 394
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDsRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 395 EKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERA 474
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 475 AKEKAEKeRLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKA 554
Cdd:pfam02029 242 VFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKE 320
|
330
....*....|....
gi 1955802949 555 EKERIEKERATKEK 568
Cdd:pfam02029 321 EIERRRAEAAEKRQ 334
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
68-558 |
2.80e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.81 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 68 VRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEK 147
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 148 QREAEEKAekerlEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKE 227
Cdd:COG3064 81 EAEKAAAE-----AEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 228 RIEKERAtKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 307
Cdd:COG3064 156 AARAAAA-AAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE 387
Cdd:COG3064 235 AAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:COG3064 315 EAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 468 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:COG3064 395 AGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGG 474
|
490
....*....|.
gi 1955802949 548 RAAKEKAEKER 558
Cdd:COG3064 475 AVLADLLLLGG 485
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
268-468 |
3.19e-06 |
|
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: 50.72 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 268 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE---RAAKGKAEKERIEKERAAKEKA 344
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 345 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKERL--------EKERAAK 416
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKK--QQEEAERAEAEKQRQkelemqlaEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 417 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKER 468
Cdd:pfam15709 470 EMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
199-582 |
4.08e-06 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 50.06 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 199 LERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKER 278
Cdd:pfam04747 58 LELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQERIQKEQEKKE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 279 AAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEK 358
Cdd:pfam04747 138 ADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 359 AEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKER 438
Cdd:pfam04747 218 KNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQKKNK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 439 LEKERAAKEKAEKERIVKERAAKGKAEKER--------IEKERAAKEKAEKERLEKERAAKEKAEKEgIEKERAAKEKAE 510
Cdd:pfam04747 298 KDKKKSESEKVVEEPVQAEAPKSKKPTADDnmdfldfvTAKEEPKDEPAETPAAPVEEVVENVVENV-VEKSTTPPATEN 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 511 KERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKE 582
Cdd:pfam04747 377 KKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQAAPSSKK 448
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
548-651 |
4.38e-06 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 50.51 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 548 RAAKEKAEKERIEKERATKEKAEKERIEKERAakenERLEKEQLAK-EKGRLEkeRLTKENAKKEKENSERVEKERVAKE 626
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRI----ERLEREERERlERERME--RIERERLERERLERERLERDRLERD 502
|
90 100
....*....|....*....|....*
gi 1955802949 627 RAEKervAKESEKERMERERVPKGK 651
Cdd:PTZ00266 503 RLDR---LERERVDRLERDRLEKAR 524
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
290-482 |
6.09e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.42 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 290 EKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgieKERA 369
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA---AAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 370 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 449
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|...
gi 1955802949 450 EKERIVKERAAKGKAEKERIEKERAAKEKAEKE 482
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
163-332 |
6.64e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEkERATKEKAEKE 242
Cdd:PRK09510 90 EELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAA-AAAKKAAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:PRK09510 169 KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAE 248
|
170
....*....|
gi 1955802949 323 RAAKGKAEKE 332
Cdd:PRK09510 249 KAAAAKAAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
403-593 |
6.70e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 403 KAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE---RAAKGKAEKERIEKERAAKEKA 479
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 480 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKER 558
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190
....*....|....*....|....*....|....*
gi 1955802949 559 IEKERATKEKAEKERIEKERAAKENERLEKEQLAK 593
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
252-453 |
6.99e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 252 EKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKE---RAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGK 328
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 329 AEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKERIEKEraakekaEKERLEKERAAKEKAEKER 408
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEFRRKLQELQRKK--QQEEAERAEAEKQRQKEL-------EMQLAEEQKRLMEMAEEER 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955802949 409 LEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKER 453
Cdd:pfam15709 477 LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
335-525 |
7.18e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 335 EKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKErlekERA 414
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA----AAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 415 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKE-- 492
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEak 224
|
170 180 190
....*....|....*....|....*....|....
gi 1955802949 493 -KAEKEGIEKERAAKEKAEKERIEKERAAKEKAE 525
Cdd:PRK09510 225 aAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
209-406 |
7.32e-06 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 49.61 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 209 AEKERLEKE--RVAKEKAEKERIEKERATKEKAEKERIEKERADKE--KAEKERIEKERAAKEKAE----KERIEKERAA 280
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEansaRRDTMEIQNE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 281 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERA-AKEKAEKERLEKERAAKEKA 359
Cdd:PRK14900 922 QKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRsVKKAAATRAAMKKKVAKKAP 1001
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1955802949 360 EKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKerAAKEKAEK 406
Cdd:PRK14900 1002 AKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKK--AAKKPARK 1046
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
250-703 |
7.40e-06 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 49.29 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 250 DKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKA 329
Cdd:pfam04747 49 DQRKEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRAEAEAKKRAAQEEEHKQWKAEQER 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 330 EKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERL 409
Cdd:pfam04747 129 IQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 410 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERA 489
Cdd:pfam04747 209 QEITGKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 490 AKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKE---RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEK----- 561
Cdd:pfam04747 289 ASENQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADdnmDFLDFVTAKEEPKDEPAETPAAPVEEVVENVVENvveks 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 562 -ERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKE 640
Cdd:pfam04747 369 tTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQAAPSSKK 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 641 RMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQ 703
Cdd:pfam04747 449 PTADDNMDFLDFVTAKPDKSESVEEHIAAPMIVEPAHADEETAAAAEGKKKNKKDKKKKESEK 511
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
448-749 |
7.98e-06 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 49.66 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 448 KAEKERIVKERAAKGKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKEGIEKERAAKE----------KAEKERIEKE 517
Cdd:PTZ00108 1030 NAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEE--EGAEEDDEADDEDDEEELGAAVSydyllsmpiwSLTKEKVEKL 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 518 RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGR 597
Cdd:PTZ00108 1108 NAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSAD 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 598 LEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAA 677
Cdd:PTZ00108 1188 KSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSK 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 678 KEKERAAVK-GHLVKEKTAKAKVETEQLPKI-------EREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEE 749
Cdd:PTZ00108 1268 EGKPKNAPKrVSAVQYSPPPPSKRPDGESNGgskpsspTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASAS 1347
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
243-582 |
8.29e-06 |
|
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: 49.24 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKEriekerAAKEKAEKERLEKERAAKEkAEKERLEKERAAKEKAEKERIVKE 322
Cdd:NF033838 95 DIKTEYLYELNVLKEKSEAELTSKTKKELD------AAFEQFKKDTLEPGKKVAE-ATKKVEEAEKKAKDQKEEDRRNYP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKeKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 402
Cdd:NF033838 168 TNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 403 KAEKERLEKERAAKEKAEKER-IEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEK 481
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRgVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 482 ER--------------LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:NF033838 327 DRrnyptntyktleleIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKA 406
|
330 340 350
....*....|....*....|....*....|....*
gi 1955802949 548 RAAKEKAEKERIEKERATKEKAEKERIEKERAAKE 582
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQ 441
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
437-730 |
1.10e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 437 ERLEKERAAKEKAEKERIVKERAAKGKAEKER-IEKERAAKEKAEKERLEKERAAKekaekegIEKERAAKEKAEKERIE 515
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEKARqAEMDRQAAIYAEQERMAMERERE-------LERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 516 KERAAKEKA---EKERLEKERAAKEKAEKEGIEKERAAKEKaEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLA 592
Cdd:pfam17380 367 QEEIAMEISrmrELERLQMERQQKNERVRQELEAARKVKIL-EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 593 KEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQA 672
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 673 KELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKE 730
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
299-526 |
1.16e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 49.22 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 299 AEKERLEKE--RAAKEKAEKERIVKERAAKGKAEKERIEKERAakeKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 376
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRA---RAEELREKRGKLEAHRAMLSGSEANSARRDTMEI 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 377 ERIEKERAAKEKAEKErlekerAAKEKAEKERLEKERAAKEKAEKeriekeraAKEKAEKERLEKERAAKEKAEKeRIVK 456
Cdd:PRK14900 919 QNEQKPTQDGPAAEAQ------PAQENTVVESAEKAVAAVSEAAQ--------QAATAVASGIEKVAEAVRKTVR-RSVK 983
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 457 ERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKeRAAKEKAEKERIEKerAAKEKAEK 526
Cdd:PRK14900 984 KAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAK-KVARKPAAKKAAKK--PARKAAGR 1050
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
456-741 |
1.17e-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: 49.20 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 456 KERAAKGKAEKERIEKERAAKE----KAEKERLEKERAAKEKAEKEGIEK---ERAAKEKAEKERIEKERAAKEKAEKER 528
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELIIDLeelKLQELKLKEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 529 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLaKEKGRLEKERLTKENA 608
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE-EELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 609 KKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGH 688
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 689 LVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEK 741
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
531-784 |
1.28e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 531 KERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKgrlEKERLTKENAKK 610
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAE---QRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 611 EKENSERVEKERVAKERAEKERVAKESEKERMERervpkgKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLV 690
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAE------KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 691 KEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKNANNFTTTSKKEKIMAI 770
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250
....*....|....
gi 1955802949 771 RDLLKPKATKVNKK 784
Cdd:COG3064 232 AALAAVEATEEAAL 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
512-749 |
1.37e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 512 ERIEKERAAKEKAEKER-LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERatkeKAEKERIEKERAAKENERLEKEQ 590
Cdd:pfam17380 294 EKMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER----ERELERIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 591 LAKEKGRL-EKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAK----------E 659
Cdd:pfam17380 370 IAMEISRMrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeraremE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 660 RAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEKIDGER--V 737
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQkaI 529
|
250
....*....|..
gi 1955802949 738 VKEKRAKQAKEE 749
Cdd:pfam17380 530 YEEERRREAEEE 541
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
207-417 |
1.92e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.02 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 207 EKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKEraakekaEKERIEKERAAKEKAEK 286
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELE-------QQRRFEEIRLRKQRLEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 287 ERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKgkaeKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEK 366
Cdd:pfam15709 399 ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 367 ERAAKEKAEKERIEKeraAKEKAEKERLEKERAAKEKAEKERLEKERAAKE 417
Cdd:pfam15709 475 ERLEYQRQKQEAEEK---ARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
38-560 |
2.02e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 38 RKLKSALKEQLRMIHEKIEAQKIAEMALAEVRSILAKEEEERQLVNALELKRQEVAQKAQEMLEAQLREEREQEEKREAE 117
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 118 RRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERlEKEKLEKERIEKktELERMEKERLAAQSFSKEKAEKE 197
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 198 RLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIE-KERAAKEKAEKERIEK 276
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEiEEKERKLRKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 277 ERAAKEK--AEKERLEKERAAKEKAEKERLEKERAAKEKAEKeriVKERAAKGKAEKERIEKERAAKEKAEKERLEKERA 354
Cdd:PRK03918 488 VLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK---LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 355 AKE-KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE-KAEKERLEKERAAKEKAEKERIEKERAAKE 432
Cdd:PRK03918 565 LDElEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKElEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 433 -KAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEK--ERLEKERAAKEKAEKEgIEKERAAKEKA 509
Cdd:PRK03918 645 lRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKE-LEKLEKALERV 723
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 510 EKERiEKERAAKEKAEKERLEK-ERAAKEKAEKEGIEKERAAKEKAEKERIE 560
Cdd:PRK03918 724 EELR-EKVKKYKALLKERALSKvGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
375-552 |
2.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 375 EKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE-KERIEKERAAKEKAEKERLEKERAAKE-KAEKE 452
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDAlREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 453 RIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKE 532
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|
gi 1955802949 533 RAAKEKAEKEGIEKERAAKE 552
Cdd:COG4913 407 LAEAEAALRDLRRELRELEA 426
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
187-390 |
2.35e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 187 QSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKEradKEKAEKERIEKERAAK 266
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ---KQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 267 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKErivkeraAKGKAEKERIEK-ERAAKEKAE 345
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-------AKKKAEAEAKKKaAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1955802949 346 KErlekeraAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAE 390
Cdd:PRK09510 221 AE-------AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
320-457 |
2.42e-05 |
|
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: 45.45 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 320 VKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKeraaKEKAEKERLEK-ER 398
Cdd:pfam11600 2 RSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 399 AAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 457
Cdd:pfam11600 78 DEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
163-461 |
2.50e-05 |
|
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: 47.70 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKE 242
Cdd:NF033838 172 KTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKER-IEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVK 321
Cdd:NF033838 252 NVATSEQDKPKRRAKRgVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNY 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 322 ERAAKGKAEKERIEKERAAKEkAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK 401
Cdd:NF033838 332 PTNTYKTLELEIAESDVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEED 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 402 EKAEKERLEKERAAKEKAEKERIEKERAAK----EKAEKERLEKERAAKEKAEKERIVKERAAK 461
Cdd:NF033838 411 KVKEKPAEQPQPAPAPQPEKPAPKPEKPAEqpkaEKPADQQAEEDYARRSEEEYNRLTQQQPPK 474
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
608-663 |
2.59e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.84 E-value: 2.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 608 AKKEKENSERVEKERVAKERAEKERvAKESEKERmERERvpkgkERERVAkERAEK 663
Cdd:pfam03154 586 AKKREEALEKAKREAEQKAREEKER-EKEKEKER-ERER-----EREREA-ERAAK 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-418 |
2.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 232 ERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK 311
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 312 EkAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEK 391
Cdd:COG4913 322 R-EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180
....*....|....*....|....*..
gi 1955802949 392 ERLEkERAAKEKAEKERLEKERAAKEK 418
Cdd:COG4913 401 EALE-EALAEAEAALRDLRRELRELEA 426
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
466-751 |
3.18e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 47.68 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 466 KERIEKERAAKEKAEKERLEKERA-AKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKaekerlEKERAAKEKAEKEgI 544
Cdd:TIGR00927 613 KEQLSRRPVAKVMALGDLSKGDVAeAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG------ETETKGENESEGE-I 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 545 EKERAAKEKAEKERIEKERATKEKAEKERIEKERAAK-ENERLEKEQLAKEKGRL-EKERLTKENAKKEKE-NSERVEKE 621
Cdd:TIGR00927 686 PAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEaEGTEDEGEIETGEEGEEvEDEGEGEAEGKHEVEtEGDRKETE 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 622 RVAKERAEKERVAKESEKERMERERVpKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHlVKEKTAKAKVET 701
Cdd:TIGR00927 766 HEGETEAEGKEDEDEGEIQAGEDGEM-KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQG 843
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 702 EQLPKIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMP 751
Cdd:TIGR00927 844 EAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEP 893
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
329-643 |
3.60e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 329 AEKERIEKERAAKEKAEKERL-EKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEK--ERAAKEKAE 405
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 406 KERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK------EKAEKERIVKERAAKGKAEKERIEKERAAKEK- 478
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDsrlgryKEEETEIREKEYQENKWSTEVRQAEEEGEEEEd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 479 --AEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 556
Cdd:pfam02029 162 ksEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 557 ERIEKERAtkekaeKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKK------EKENSERVEKERVAKERAEK 630
Cdd:pfam02029 242 VFLEAEQK------LEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERrklleeEEQRRKQEEAERKLREEEEK 315
|
330
....*....|...
gi 1955802949 631 ERVAKESEKERME 643
Cdd:pfam02029 316 RRMKEEIERRRAE 328
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
389-596 |
3.78e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 47.29 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 389 AEKERLEKE--RAAKEKAEKERLEKERAAKEKAEKERIEKERAakekaekeRLEKERAAKEKAEKERIVKERAAKGKAEK 466
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRA--------RAEELREKRGKLEAHRAMLSGSEANSARR 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 467 ERIEKERAAKEKAEKERLEKErAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA-AKEKAEKEGIE 545
Cdd:PRK14900 914 DTMEIQNEQKPTQDGPAAEAQ-PAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRsVKKAAATRAAM 992
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 546 KERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKG 596
Cdd:PRK14900 993 KKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKKAAKKP 1043
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
463-643 |
4.41e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 463 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE---RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 539
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 540 EKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKE---QLAKEKGRL----EKERLTKENAKKEK 612
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKElemQLAEEQKRLmemaEEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|.
gi 1955802949 613 ENSERVEKERVAKERAEKERVAKESEKERME 643
Cdd:pfam15709 487 EEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
263-418 |
4.46e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 263 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKE 342
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 343 KAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKErIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEK 418
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAE-LEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRA 345
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
371-648 |
4.50e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 371 KEKAEKERIEKERAAKEKAeKERLEKERAAKEKAEKERLEKERAAKEKAEkeriekERAAKEKAEKERLEKEraAKEKAE 450
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSLE------ELIKDVEEELEKIEKE--IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 451 KERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKE---RAAKEKAEKEGIEKERAAKEKAEKERIEKER------AAK 521
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvVLK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 522 EKAEK--ERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERatkekaekERIEKERAAKENERLEKEQLAKEKGRLE 599
Cdd:PRK05771 188 ELSDEveEELKKLGFERLELEEEGTPSELIREIKEELEEIEKER--------ESLLEELKELAKKYLEELLALYEYLEIE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 600 KERltkENAKKEKENSER-------VEKERVAK-----ERAEKERVAKESEKERMERERVP 648
Cdd:PRK05771 260 LER---AEALSKFLKTDKtfaiegwVPEDRVKKlkeliDKATGGSAYVEFVEPDEEEEEVP 317
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
337-471 |
4.60e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 44.68 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 337 ERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKeraaKEKAEKERLEK-ERAA 415
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 416 KEKAEKERIEKEraaKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEK 471
Cdd:pfam11600 80 KEKAEKLRLKEE---KRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
332-613 |
5.18e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 332 ERIEKERAAKEKAEKER-LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERaakekaeKERLEKERAAKEKAEKERLE 410
Cdd:pfam17380 294 EKMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER-------ERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 411 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAA 490
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 491 K---------EKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKeKAEKERIEK 561
Cdd:pfam17380 447 EmervrleeqERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEER 525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 562 ERATKEKAEKERIEKERaAKENERLEKEQLAKEKGRLEKERLTKENAKKEKE 613
Cdd:pfam17380 526 QKAIYEEERRREAEEER-RKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
169-303 |
5.51e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 44.29 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 169 RIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKeratKEKAEKERIEK-E 247
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 248 RADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKER 303
Cdd:pfam11600 77 KDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
343-572 |
6.10e-05 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 46.78 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 343 KAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKE 422
Cdd:PLN03237 1174 KAEEAREKLQRAAARGESGAAKKVSRQAPKKPAPKKTTKKASESETTEETYGSSAMETENVAEVVKPKGRAGAKKKAPAA 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 423 RIEKERAAKEKAEKERLEKER---AAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKER--LEKERAAKEKAEKE 497
Cdd:PLN03237 1254 AKEKEEEDEILDLKDRLAAYNldsAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDSDDDDddFAVEVSLAERLKKK 1333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 498 GIEKERAAKEKAEKERIEKERAAKEKAeKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKE 572
Cdd:PLN03237 1334 GGRKPAAANKKAAKPPAAAKKRGPATV-QSGQKLLTEMLKPAEAIGISPEKKVRKMRASPFNKKSGSVLGRAATN 1407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-710 |
6.22e-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: 46.60 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 410 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERaaKGKAEKERIEKERAAKEKaEKERLEKERA 489
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE--KREYEGYELLKEKEALER-QKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 490 AKEKaEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKA 569
Cdd:TIGR02169 248 SLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 570 EKERIEKERAAKEN-------ERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERM 642
Cdd:TIGR02169 327 LEAEIDKLLAEIEElereieeERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 643 ERERVPKGKERERVAKERAEKERAEKEQQAKELaakeKERAAVKGHLVKEKTAKAKVETEQLPKIERE 710
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
191-553 |
6.26e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 191 KEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAE 270
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 271 KERIEKERAAKEKAEKERLEKERAAKEKAEK--ERLEKERAA-KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 347
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEelEELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 348 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKE 427
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 428 RAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE 507
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1955802949 508 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEK 553
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
383-566 |
6.53e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.02 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 383 RAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAakg 462
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAA--- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 463 kAEKERIEKERAAKEKAEKERLEKERAAKEKAekegIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERaAKEKAEKE 542
Cdd:COG2268 268 -YEIAEANAEREVQRQLEIAEREREIELQEKE----AEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR-AKGLAEAE 341
|
170 180
....*....|....*....|....
gi 1955802949 543 GIEKERAAKEKAEKERIEKERATK 566
Cdd:COG2268 342 GKRALAEAWNKLGDAAILLMLIEK 365
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
372-552 |
6.79e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 372 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE---RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEK 448
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 449 AEKERIVKERAAKGKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKEGIEKERAAKEK-----AEKERIEKERAAKE 522
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEFRRKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKrlmemAEEERLEYQRQKQE 485
|
170 180 190
....*....|....*....|....*....|....*..
gi 1955802949 523 KAEKERLE-------KERAAKEKAEKEGIEKERAAKE 552
Cdd:pfam15709 486 AEEKARLEaeerrqkEEEAARLALEEAMKQAQEQARQ 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
310-493 |
7.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 310 AKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKERIEKERAAKEkA 389
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--LRAELARLEAELERLEARLDALR-E 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 390 EKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERI 469
Cdd:COG4913 324 ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180
....*....|....*....|....
gi 1955802949 470 EkERAAKEKAEKERLEKERAAKEK 493
Cdd:COG4913 404 E-EALAEAEAALRDLRRELRELEA 426
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
215-487 |
7.83e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 215 EKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKErAAKEKAEKERLEKERA 294
Cdd:PRK07735 3 PEKDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAA-AAKAKAAALAKQKREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 295 AKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEkEGIEKERAAKEKA 374
Cdd:PRK07735 82 TEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKR-EGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 375 EKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERI 454
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAI 240
|
250 260 270
....*....|....*....|....*....|...
gi 1955802949 455 VkerAAKGKAEKERIEKERAAKEKAEKERLEKE 487
Cdd:PRK07735 241 A---AAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
161-371 |
8.14e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 46.14 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:PRK14900 843 ETARVDKEIGKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKRGKLEAHRAMLSGSEANSARRDTMEIQNEQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEK----ERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA-AKEKAEKERLEKERAAKEKAE 315
Cdd:PRK14900 923 KPTQDGPAAEAQPAQEntvvESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRsVKKAAATRAAMKKKVAKKAPA 1002
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 316 KERIVKERAAKGKAEKERIEKERAAKEKAEKerlekerAAKEKAEKEGIEKERAAK 371
Cdd:PRK14900 1003 KKAAAKKAAAKKAAAKKKVAKKAPAKKVARK-------PAAKKAAKKPARKAAGRK 1051
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
397-754 |
8.85e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 397 ERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAK 476
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 477 EKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKegieKERAAKEKAEK 556
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY----LDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 557 ERIEKERATKEKAEKERIEKERAAKENERLEKEqLAKEKGRLEKERLTKENAKKEKENSERVEKER--VAKERAEKERVA 634
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 635 KESEKERMERERVPKGKERERVAKERAEKERAEKEQQA---------KELAAKEKERAAVKGHLVKEKTAKAKVETEQLP 705
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1955802949 706 KIEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKEEMPEKN 754
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
160-432 |
9.02e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 160 LEKEKLEKERIEKKTELERMEK------------ERLAAQSFSKEKAEKER---LERERVAKEKAEKERLEKERVAKEKA 224
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRKleeaekarqaemDRQAAIYAEQERMAMERereLERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 225 EKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKerl 304
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 305 EKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERaakeKAEKEGIEKERAAKEKAEKERIEKERA 384
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL----EERKQAMIEEERKRKLLEKEMEERQKA 528
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1955802949 385 AKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKE 432
Cdd:pfam17380 529 IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
254-587 |
9.79e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 254 AEKERIEKERAAKEKAEKERI-EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVK--ERAAKGKAE 330
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 331 KERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERaakekaekeRIEKERAAKEKAEKERLEKERAAKEKAEKERLE 410
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEE---------KRDSRLGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 411 KERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAA 490
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 491 KEKAEKEGiEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAE 570
Cdd:pfam02029 233 SQEREEEA-EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLRE 311
|
330
....*....|....*..
gi 1955802949 571 KERIEKERAAKENERLE 587
Cdd:pfam02029 312 EEEKRRMKEEIERRRAE 328
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
380-582 |
1.01e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 380 EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKErivkERA 459
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA----AAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 460 AKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgiekeraAKEKAEKEriEKERAAKEKAEKERLEKERAAKEKA 539
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE-------AKKKAEAE--AAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1955802949 540 EKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKE 582
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
470-676 |
1.02e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 470 EKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKaeKERLEKERAAKEKAEKEGIEKERA 549
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQ--LERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 550 AKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEK--EQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKER 627
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRklQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1955802949 628 AEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELA 676
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
170-365 |
1.09e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 170 IEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERA 249
Cdd:TIGR00927 699 IEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 250 DKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK---EKAEKERIVKERAAK 326
Cdd:TIGR00927 779 DEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEnqgEAKQDEKGVDGGGGS 858
|
170 180 190
....*....|....*....|....*....|....*....
gi 1955802949 327 GKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 365
Cdd:TIGR00927 859 DGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLE 897
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
324-513 |
1.20e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 45.35 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 324 AAKGKAEKERIEkeraAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEK 403
Cdd:PRK13108 275 APKGREAPGALR----GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 404 AEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKErivkERAAKGKAEKERIEKERAAKE--KAEK 481
Cdd:PRK13108 351 QVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAapIPDP 426
|
170 180 190
....*....|....*....|....*....|..
gi 1955802949 482 ERLEKERAAKEKAEKEGIEKERAAKEKAEKER 513
Cdd:PRK13108 427 AKPDELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
367-495 |
1.25e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 43.14 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 367 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKeraaKEKAEKERLEK-ERAA 445
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 446 KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 495
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
374-686 |
1.28e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 374 AEKERIEKERAAKEKAEKERL-EKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEK--ERAAKEKAE 450
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKreERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 451 KERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEkERAAKEKAEKERIEKERAAKEKAEKERLE 530
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 531 KERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKK 610
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 611 EKENSERVEKERVAKERAEKERVAKESEKERM---ERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVK 686
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqeaELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMK 319
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
426-681 |
1.42e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.42 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 426 KERAAKEKAEKERLEKERAAKEKAEKERIVKERAAK---------GKAEKERIEKERAAKEKAEKE-RLEKERAAKEKAE 495
Cdd:PTZ00108 1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDLDKfeealeeqeEVEEKEIAKEQRLKSKTKGKAsKLRKPKLKKKEKK 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 496 KEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIE 575
Cdd:PTZ00108 1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 576 KERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERER 655
Cdd:PTZ00108 1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTR 1340
|
250 260
....*....|....*....|....*.
gi 1955802949 656 VAKERAEKERAEKEQQAKELAAKEKE 681
Cdd:PTZ00108 1341 VKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
284-343 |
1.49e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 45.48 E-value: 1.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 284 AEKERLEKERAAKEKaEKERLEK--------ERAAKEKAEKERivkERAAKGKAEKERIEKERAAKEK 343
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-682 |
1.52e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 382 ERAAKEKAEKERLEKERAAKE----KAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 457
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 458 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 537
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 538 KAEKegIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERL--EKEQLAKEKGRLEKERLTKENAKKEKENS 615
Cdd:TIGR02168 373 RLEE--LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 616 ERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKER 682
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
221-582 |
1.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 221 KEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 300
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 301 KERLEKERAAKEKAEKERI--VKERAAKGKAEKERIEKERAA-KEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKE 377
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELesLQEEAEELQEELEELQKERQDlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 378 RIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 457
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 458 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 537
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1955802949 538 KAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKE 582
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
206-336 |
1.68e-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: 42.75 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 206 KEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERiEKERADKEKAEKERIEKERAAKEKAEKERIEK-ERAAKEKA 284
Cdd:pfam11600 5 KSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLK-EEAKAEKERAKEEARRKKEEEKELKEKERREKkEKDEKEKA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 285 EKERLEKEraaKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEK 336
Cdd:pfam11600 84 EKLRLKEE---KRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
193-453 |
1.73e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 193 KAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKE 272
Cdd:pfam02029 70 KREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 273 RIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKE 352
Cdd:pfam02029 150 RQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 353 RAAKEKAEKEGIEKERAAKekaEKERIEKERAAKEKAEKERLeKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKE 432
Cdd:pfam02029 230 LSQSQEREEEAEVFLEAEQ---KLEELRRRRQEKESEEFEKL-RQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEA 305
|
250 260
....*....|....*....|.
gi 1955802949 433 KAEKERLEKERAAKEKAEKER 453
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIERRR 326
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
389-441 |
1.86e-04 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 45.04 E-value: 1.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 389 AEKERLEKERAAKEKaEKERLEK--------ERAAKEKAEKERiEKERAAKEKAEK--ERLEK 441
Cdd:COG0525 815 AERARLEKELAKLEK-EIARVEKklsnegfvAKAPAEVVEKER-EKLAEAEAKLEKleEQLAR 875
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
398-587 |
1.88e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 398 RAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKErLEKERAAKEKAEKERIVKERAAKGK---AEKERIEKERA 474
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-LEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 475 AKEKAEKERLEKERAAKE-KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEK-ERAAKEKAEKEGIEK-ERAAK 551
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKaEAEAKKKAAAEAKKKaAAEAK 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955802949 552 EKAEKERIEKERATKEKAEKERIEKERAAKENERLE 587
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-576 |
1.91e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 222 EKAEKERIEKERATKEKAEKERIEKERADK-EKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAE 300
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQlERLRREREKAERYQALLKEKREYEGYELLKEKEALER-QKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 301 KERlEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIE 380
Cdd:TIGR02169 249 LEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 381 KERAAKEKAEKERLEKERAakekAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAA 460
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIE----EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 461 KGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKErLEKERAAKEKAE 540
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE-LYDLKEEYDRVE 482
|
330 340 350
....*....|....*....|....*....|....*.
gi 1955802949 541 KEGIEKERAAKEKAEKERIEKERATKEKAEKERIEK 576
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
232-360 |
1.94e-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: 42.75 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 232 ERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKeraaKEKAEKERLEK-ERAA 310
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 311 KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 360
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
187-302 |
1.98e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 44.46 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 187 QSFSKEKAEKERLERERVAKEKAEKERLEKER---------VAKEKAEKERIEKERATKEKAEKERiEKERADKEKAEKE 257
Cdd:PRK00247 281 DEFKEHHAEQRAQYREKQKEKKAFLWTLRRNRlrmiitpwrAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAER 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955802949 258 RIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 302
Cdd:PRK00247 360 EINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
442-573 |
2.01e-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: 42.75 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 442 ERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKeraaKEKAEKERIEK-ERAA 520
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 521 KEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKER 573
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
393-446 |
2.05e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 2.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 393 RLEKERaaKEKAEKERLEKERAAKEKAEKERiEKERAAKEKAEKERlEKERAAK 446
Cdd:pfam03154 584 KLAKKR--EEALEKAKREAEQKAREEKEREK-EKEKERERERERER-EAERAAK 633
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
389-448 |
2.14e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 44.71 E-value: 2.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 389 AEKERLEKERAAKEKaEKERLEK--------ERAAKEKAEKERiekERAAKEKAEKERLEKERAAKEK 448
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
328-537 |
2.24e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 328 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERaaKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 407
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQ--LERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 408 RLEKERAAKEKAEKERIEKERAAKEKAEKERLEKeraaKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKE 487
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQQEEFRRKLQELQRK----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 488 RAAKEKAEKegiekeraAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 537
Cdd:pfam15709 481 RQKQEAEEK--------ARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
307-438 |
2.55e-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: 42.37 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 307 ERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKeraaKEKAEKERIEK-ERAA 385
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 386 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKER 438
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
302-429 |
2.55e-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: 42.37 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 302 ERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKEGIEKERaakeKAEKERIE 380
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEaKAEKERAKEEARRKKEEEKELKEKER----REKKEKDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1955802949 381 KERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERA 429
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKA 128
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
252-532 |
2.63e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 252 EKAEKERIEKERAAKekaEKERIEKERAAKEKAEKERLEKERAAKEKAEkerlekERAAKEKAEKERIVKERAAKGKAEK 331
Cdd:PRK07735 3 PEKDLEDLKKEAARR---AKEEARKRLVAKHGAEISKLEEENREKEKAL------PKNDDMTIEEAKRRAAAAAKAKAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 332 ERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEkERLEK 411
Cdd:PRK07735 74 LAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKR-EGTEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 412 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAK 491
Cdd:PRK07735 153 VTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1955802949 492 EKAEKEGIEkerAAKEKAEKERIEKERAAKEKAEKERLEKE 532
Cdd:PRK07735 233 EDAKAKAIA---AAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
262-393 |
2.64e-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: 42.37 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 262 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKErivKERAAKGKAEKERIEKERAAK 341
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRK---KEEEKELKEKERREKKEKDEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 342 EKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKER 393
Cdd:pfam11600 81 EKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
419-558 |
2.71e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 44.07 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 419 AEKERIEKERAAKEKAEKERLEKERAAKekaekeRIVKERAAKGKAEKERIEKERAAKEKAEKER----LEKERAAKEKA 494
Cdd:PRK00247 288 AEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRTAEKNEAKARkkeiAQKRRAAEREI 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 495 EKEGIEKERAAKEKAEKERieKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKER 558
Cdd:PRK00247 362 NREARQERAAAMARARARR--AAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEATTTAEPNR 423
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
479-594 |
2.71e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 479 AEKERLEKERAAKEkaekegIEKERAAKEKAEKeriEKERAAKEKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKER 558
Cdd:COG0542 411 EELDELERRLEQLE------IEKEALKKEQDEA---SFERLAELRDELAELEEELEALKARWEA--EKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|....*.
gi 1955802949 559 IEKERATKEKAEKERIEKERAAKENERLEKEQLAKE 594
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEVTEE 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-532 |
2.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 268 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 347
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 348 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKE 427
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 428 RAAKEKAEKERLE--KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAA 505
Cdd:TIGR02168 398 LNNEIERLEARLErlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260
....*....|....*....|....*..
gi 1955802949 506 KEKAEKERIEKERAAKEKAEKERLEKE 532
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGF 504
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
297-572 |
3.18e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 297 EKAEKERLEKERAA--KEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKA 374
Cdd:PRK07735 3 PEKDLEDLKKEAARraKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 375 EKERIEKERAAKEKAEKERLEKeraAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERI 454
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAAAKAK---AAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 455 VKERAAKGKAekeriekerAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 534
Cdd:PRK07735 160 TDKEKAKAKA---------AAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDS 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1955802949 535 AKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKE 572
Cdd:PRK07735 231 GDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQ 268
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
122-402 |
3.25e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 122 EQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKEKlEKERI---EKKTELERMEKERLAAQSFSKEKAEKER 198
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER-ELERIrqeERKRELERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 199 LERERvakeKAEKERLEKERVAKEKAekerIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKER 278
Cdd:pfam17380 385 MERQQ----KNERVRQELEAARKVKI----LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 279 AAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERaakgKAEKERIEKERAAKEKAEKERLEKERAAKEK 358
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL----EERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1955802949 359 AEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 402
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-454 |
3.35e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKE 242
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKeKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 402
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 403 KAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERI 454
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
163-538 |
3.58e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKE 242
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAaKEKAEKERLEKERAAKEKAEKERlekeraAKEKAEKERIVKE 322
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE-ELQKERQDLEQQRKQLEAQIAEL------QSEIAEREEELKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE 402
Cdd:COG4372 155 LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 403 KAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 482
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 483 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEK 538
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
420-602 |
3.65e-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: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 420 EKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAE-KERIEKERAAKEKAEKERLEKERAAKE-KAEKE 497
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDAlREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 498 GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKE 577
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*
gi 1955802949 578 RAAKENERlekEQLAKEKGRLEKER 602
Cdd:COG4913 407 LAEAEAAL---RDLRRELRELEAEI 428
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
441-557 |
3.79e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.69 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 441 KERAAKEKAE-KERIVKERAAKGKAEKER----IEKERAAKEKAEKERLEKERAAKEKAEKEGiEKERAAKEKAEKERIE 515
Cdd:PRK00247 284 KEHHAEQRAQyREKQKEKKAFLWTLRRNRlrmiITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAEREIN 362
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1955802949 516 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKE 557
Cdd:PRK00247 363 REARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
226-347 |
3.83e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.69 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 226 KERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKERLE 305
Cdd:PRK00247 284 KEHHAEQRAQYREKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAEREIN 362
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1955802949 306 KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 347
Cdd:PRK00247 363 REARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
283-407 |
3.86e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.69 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 283 KAEKERLEKERAAKEKAEKERLekeRAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKE 362
Cdd:PRK00247 284 KEHHAEQRAQYREKQKEKKAFL---WTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAER 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955802949 363 GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 407
Cdd:PRK00247 360 EINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
282-547 |
3.88e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.82 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 282 EKAEKERLEKERAA--KEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKA 359
Cdd:PRK07735 3 PEKDLEDLKKEAARraKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 360 EKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERL 439
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 440 EKER---AAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEk 516
Cdd:PRK07735 163 EKAKakaAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIA- 241
|
250 260 270
....*....|....*....|....*....|.
gi 1955802949 517 erAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:PRK07735 242 --AAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-358 |
4.04e-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: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERiEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEkaeke 242
Cdd:COG4913 242 EALEDAR-EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLE----- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 riekERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:COG4913 316 ----ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*.
gi 1955802949 323 RAAKGKAEKERIEkERAAKEKAEKERLEKERAAKEK 358
Cdd:COG4913 392 LLEALEEELEALE-EALAEAEAALRDLRRELRELEA 426
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
444-674 |
4.15e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 444 AAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEkAEKEGIEKERAAKEKAEKERIEKERAAKEK 523
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAA-AAAEAASAPEAAQARERRERGEAARRGAAR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 524 AEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERleKEQLAKEKGRLEKERL 603
Cdd:PRK12678 144 KAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDR--RDRREQGDRREERGRR 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 604 TKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERvpKGKERERvAKERAEKERAEKEQQAKE 674
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR--RFRDRDR-RGRRGGDGGNEREPELRE 289
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
450-575 |
4.17e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 450 EKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEkERL 529
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-ERE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1955802949 530 EKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKeKAEKERIE 575
Cdd:pfam05672 90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ-QEEQERLE 134
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
375-488 |
4.17e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 375 EKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERI 454
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....
gi 1955802949 455 vKERAAKGKAEKERIEKERAAKEKAEKERLEKER 488
Cdd:pfam05672 91 -REQEEQERLQKQKEEAEAKAREEAERQRQEREK 123
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
520-592 |
4.19e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 43.99 E-value: 4.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 520 AKEKAEKERLEkeraAKEKAEKEGiekERAAKEKAEKERiEKERATKEKAEKERiEKERAAKENE-----RLEKEQLA 592
Cdd:pfam03154 581 AGSKLAKKREE----ALEKAKREA---EQKAREEKEREK-EKEKERERERERER-EAERAAKASSsshegRMGDPQLA 649
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
330-453 |
4.25e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 330 EKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEkERL 409
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-ERE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1955802949 410 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKeKAEKER 453
Cdd:pfam05672 90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ-QEEQER 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-485 |
4.33e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 152 EEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEK 231
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 232 ERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK 311
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 312 EKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKE------RAA 385
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerledRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 386 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAE 465
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330 340
....*....|....*....|
gi 1955802949 466 KERIEKERAAKEKAEKERLE 485
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSG 517
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
382-519 |
4.40e-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: 41.60 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 382 ERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKeraaKEKAEKERivkeraak 461
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKER-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 462 gKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERA 519
Cdd:pfam11600 72 -REKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKA 128
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
165-433 |
4.54e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 165 LEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEkeriEKERATKEKAEKERI 244
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE----ETEIREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 245 EKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERA 324
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 325 AKGKAEKERIEKERAAKEKAEKeRLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKA 404
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEA 305
|
250 260
....*....|....*....|....*....
gi 1955802949 405 EKERLEKERAAKEKAEKERIEKERAAKEK 433
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
374-497 |
4.75e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.30 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 374 AEKERIEKERAAKEKAEKERLEKERAAKekaekeRLEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKER 453
Cdd:PRK00247 288 AEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAERE 360
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1955802949 454 IVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 497
Cdd:PRK00247 361 INREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
312-584 |
4.91e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 312 EKAEKERIVKERAAKGKAE--KERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKA 389
Cdd:PRK07735 3 PEKDLEDLKKEAARRAKEEarKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 390 EKERLEKERAAKEKAEKErlEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERI 469
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAA--AKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 470 EKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERA 549
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAI 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1955802949 550 AKEKAEKERIEKERATKEKAEKERIEKERAAKENE 584
Cdd:PRK07735 241 AAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQ 275
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
344-396 |
4.92e-04 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 43.89 E-value: 4.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 344 AEKERLEKERAAKEKaEKEGIEK--------ERAAKEKAEKERiEKERAAKEKAEK--ERLEK 396
Cdd:COG0525 815 AERARLEKELAKLEK-EIARVEKklsnegfvAKAPAEVVEKER-EKLAEAEAKLEKleEQLAR 875
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
166-411 |
4.94e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 166 EKERIEKKTELERMEKErlaaqsfsKEKAEKERLERERVAKEKA---EKERLEKERVAKEKAEKERIEKERATKEKaEKE 242
Cdd:pfam17380 340 ERMAMERERELERIRQE--------ERKRELERIRQEEIAMEISrmrELERLQMERQQKNERVRQELEAARKVKIL-EEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKER-LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK 401
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA 570
|
250
....*....|
gi 1955802949 402 EKAEKERLEK 411
Cdd:pfam17380 571 MEREREMMRQ 580
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
84-573 |
5.07e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 84 ALELKRQEVAQKAQEMLEAQLREEREQEEKREAERRAHEQAGKERLEKEQLEQLEREEKERLEKQREAEEKAEKERLEKE 163
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 164 KLEKERIEKKTELERmEKERLAAQSfskEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKER 243
Cdd:COG3064 81 EAEKAAAEAEKKAAA-EKAKAAKEA---EAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 244 IEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAeKERLEKERAAKEKAEKERIVKER 323
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA-DAALLALAVAARAAAASREAALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 324 AAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEK 403
Cdd:COG3064 236 AVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 404 AEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKER 483
Cdd:COG3064 316 AVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 484 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKER 563
Cdd:COG3064 396 GGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGA 475
|
490
....*....|
gi 1955802949 564 ATKEKAEKER 573
Cdd:COG3064 476 VLADLLLLGG 485
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
250-313 |
5.24e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 43.56 E-value: 5.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 250 DKEkAEKERIEKERAAKEKaEKERIEK--------ERAAKEKAEKERlekERAAKEKAEKERLEKERAAKEK 313
Cdd:PRK05729 808 DVE-AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
284-340 |
5.26e-04 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 43.50 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 284 AEKERLEKERAAKEKaEKERLEK--------ERAAKEKAEKERivkERAAKGKAEKERIEKERAA 340
Cdd:COG0525 815 AERARLEKELAKLEK-EIARVEKklsnegfvAKAPAEVVEKER---EKLAEAEAKLEKLEEQLAR 875
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
437-564 |
5.46e-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: 41.60 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 437 ERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKEGIEKERaakeKAEKERIE 515
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEaKAEKERAKEEARRKKEEEKELKEKER----REKKEKDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1955802949 516 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERA 564
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKA 128
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
522-646 |
5.65e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 522 EKAEKERLEKERAAKEKAEKEgiEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKE 601
Cdd:pfam05672 10 EEAARILAEKRRQAREQRERE--EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955802949 602 RLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERER 646
Cdd:pfam05672 88 REQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQER 132
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
501-594 |
5.69e-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: 43.55 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 501 KERAAKEKaEKERIEKERAAK--EKAEKERLEKERAAKEKAEKegiekerAAKEKAEKERIEKERATKEKAEKERIEKER 578
Cdd:NF033875 196 KDLAAKEK-EVDQLQKEQAKKiaQQAAELKAKNEKIAKENAEI-------AAKNKAEKERYEKEVAEYNKHKNENGYVNE 267
|
90
....*....|....*.
gi 1955802949 579 AAKENERLEKEQLAKE 594
Cdd:NF033875 268 AISKNLVFDQSVVTKD 283
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-602 |
5.87e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 337 ERAAKEKAEKERLEKERAAKEKAEKEGiEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAK 416
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 417 EKAEK-----ERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAK 491
Cdd:TIGR02168 292 ALANEisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 492 EKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEgIEKERAAKEKAEKERIEKERATKEKAEK 571
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE-IEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270
....*....|....*....|....*....|.
gi 1955802949 572 ERIEKERAAKENERLEKEQLAKEKGRLEKER 602
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
317-482 |
6.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 317 ERIVKERAAKGKAEKERIEKEraAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKaEKERIEKERAAKEKaeKERLEK 396
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE--AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRER-RNELQKLEKRLLQK--EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 397 ERAAKEKaEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE--KERIVKERAAKGKAEKERI--EKE 472
Cdd:PRK12704 101 KLELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAVLikEIE 179
|
170
....*....|
gi 1955802949 473 RAAKEKAEKE 482
Cdd:PRK12704 180 EEAKEEADKK 189
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
202-335 |
6.58e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 202 ERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKeraAK 281
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEE---AE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 282 EKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIE 335
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIE 140
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-647 |
6.64e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 296 KEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAE 375
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 376 KERIEKERAAKEKAEKERLEKERAAKEKAEK--ERLEKERAA------KEKAEKERIEKERAAKEKAEKERLEKERAAKE 447
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEelEELQKERQDleqqrkQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 448 KAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKEraAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKE 527
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE--AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 528 RLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKEN 607
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1955802949 608 AKKEKENSERVEKERVAKERAEKERVAKESEKERMERERV 647
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
472-748 |
6.66e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 472 ERAAKEKAEKERLEKERAAKEKAEKEgIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERaakeKAEKEGIEKERAAK 551
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKARE-VERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER----ERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 552 EKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTK--------ENAKKEKENSERVEKERV 623
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKiqqqkvemEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 624 AKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAK--EKERAAVKGHLVKEKTAKAKVET 701
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1955802949 702 EQLpkiEREQLPKAKAGKERAEKERLLKEKIDGERVVKEKRAKQAKE 748
Cdd:pfam17380 521 EME---ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
464-668 |
6.82e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 43.44 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 464 AEKERIEKE--RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKE--KAEKERIEKERAAKEKAEKERLeKERAAKEKA 539
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEANSA-RRDTMEIQN 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 540 EKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKG--RLEKERLTKENAKKEKENSER 617
Cdd:PRK14900 921 EQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTvrRSVKKAAATRAAMKKKVAKKA 1000
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 618 VEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEK 668
Cdd:PRK14900 1001 PAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKPAAKKAAKKPARKAAGRK 1051
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
378-511 |
6.98e-04 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 41.30 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 378 RIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 457
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 458 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 511
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-497 |
7.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 186 AQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERatkEKAEKERIEKERADKEKAEKERIEKERAA 265
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 266 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKeKAE 345
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 346 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKE--KAEKER 423
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalALLRSE 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 424 IEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 497
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
277-408 |
7.67e-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: 40.83 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 277 ERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKeraaKEKAEKERLEK-ERAA 355
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 356 KEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKER 408
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-441 |
7.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 255 EKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE-KERLEKERAAKEKAEKER-IVKERAAKGKAEKE 332
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELeRLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 333 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 412
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*....
gi 1955802949 413 RAAKEKAEKEriEKERAAKEKAEKERLEK 441
Cdd:COG4913 407 LAEAEAALRD--LRRELRELEAEIASLER 433
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
307-440 |
7.80e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 307 ERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKeraAK 386
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEE---AE 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 387 EKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLE 440
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIE 140
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
261-422 |
8.00e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 261 KERAAKEKAekERIEKEraAKEKAEKERLEKERAAKEKAEKERLEKEraaKEKAEKERIVKERAAKGKAEKERIEKERAA 340
Cdd:PRK12704 32 KIKEAEEEA--KRILEE--AKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 341 KEKaEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAA---KEKAEKERLE--KERAAKEKAEKERlEKERAA 415
Cdd:PRK12704 105 LEK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltAEEAKEILLEkvEEEARHEAAVLIK-EIEEEA 182
|
....*..
gi 1955802949 416 KEKAEKE 422
Cdd:PRK12704 183 KEEADKK 189
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
464-615 |
8.05e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.53 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 464 AEKERIEKERAAKEKAEKERLEKERAAKEkaekegIEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKEG 543
Cdd:PRK00247 288 AEQRAQYREKQKEKKAFLWTLRRNRLRMI------ITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAERE 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 544 IEKERAAKEKAEKERIEKERATKEKAEKERIEKeraakeNERLEKEQLAKEKGRLEKERLTKENAKKEKENS 615
Cdd:PRK00247 361 INREARQERAAAMARARARRAAVKAKKKGLIDA------SPNEDTPSENEESKGSPPQVEATTTAEPNREPS 426
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
256-625 |
8.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 256 KERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERlEKERAAKEKAEKERIVKERAAKGKAEKERIE 335
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE-ELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 336 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERaAKEKAEKERLEKERAAKEKAEKERLEKERAA 415
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 416 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 495
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 496 KEGIEKERAAKEKAEKERIEKERAAkeKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIE 575
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAI--LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 576 KERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAK 625
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
344-403 |
8.16e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 43.17 E-value: 8.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 344 AEKERLEKERAAKEKaEKEGIEK--------ERAAKEKAEKERiekERAAKEKAEKERLEKERAAKEK 403
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
508-606 |
8.21e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 508 KAEKERIEKERAAKEKaEKERLEKERAAKEKAEKEGIEKERAA-KEKAEKERIEKERATKEKAEKERIEKERAAKENERL 586
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEAlKARWEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90 100
....*....|....*....|
gi 1955802949 587 EKEQLAKEKGRLEKERLTKE 606
Cdd:COG0542 496 ELEEELAELAPLLREEVTEE 515
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
400-573 |
8.71e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.66 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 400 AKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKA 479
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 480 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKEriekERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI 559
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
|
170
....*....|....*.
gi 1955802949 560 EKE--RATKEKAEKER 573
Cdd:PRK13108 443 EPDgiRRQDDFSSRRR 458
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
423-556 |
9.48e-04 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.92 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 423 RIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 502
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 503 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 556
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
343-451 |
9.57e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.53 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 343 KAEKERLEKERAAKEKAEKEgieKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERlEKERAAKEKAEKE 422
Cdd:PRK00247 284 KEHHAEQRAQYREKQKEKKA---FLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAER 359
|
90 100
....*....|....*....|....*....
gi 1955802949 423 RIEKERAAKEKAEKERLEKERAAKEKAEK 451
Cdd:PRK00247 360 EINREARQERAAAMARARARRAAVKAKKK 388
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
303-436 |
9.75e-04 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.92 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 303 RLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKE 382
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 383 RAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEK 436
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
371-691 |
9.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 371 KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 450
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 451 KERIVKERAAKGKAEKERIEKERAAKEKAEK--ERLEKERAAKEKAEKegieKERAAKEKAEKERIEKERAAKEKAEKER 528
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEelEELQKERQDLEQQRK----QLEAQIAELQSEIAEREEELKELEEQLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 529 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENA 608
Cdd:COG4372 161 SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 609 KKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVKGH 688
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
...
gi 1955802949 689 LVK 691
Cdd:COG4372 321 LLE 323
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
374-433 |
1.00e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.78 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 374 AEKERIEKERAAKEKaEKERLEK--------ERAAKEKAEKERlekERAAKEKAEKERIEKERAAKEK 433
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
425-611 |
1.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 425 EKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERA 504
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 505 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENE 584
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAA 228
|
170 180
....*....|....*....|....*..
gi 1955802949 585 RLEKEQLAKEKGRLEKERLTKENAKKE 611
Cdd:PRK09510 229 KAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
316-437 |
1.05e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 316 KERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERiEKERAAKEKAEKERLE 395
Cdd:PRK00247 284 KEHHAEQRAQYREKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAEREIN 362
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1955802949 396 KERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKE 437
Cdd:PRK00247 363 REARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
226-394 |
1.08e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 226 KERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLE 305
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 306 KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAA---KEKAEKEGIEKERAAKEKAEKERIEKE 382
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAaeaEAEAEAEAIRAKGLAEAEGKRALAEAW 350
|
170
....*....|..
gi 1955802949 383 RAAKEKAEKERL 394
Cdd:COG2268 351 NKLGDAAILLML 362
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
148-365 |
1.09e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 148 QREAEEKAEKERLEKEKLEKE---RIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKA 224
Cdd:TIGR00927 674 ETKGENESEGEIPAERKGEQEgegEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKH 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 225 EKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERL 304
Cdd:TIGR00927 754 EVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 305 EKERAAKEKAEKERivKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIE 365
Cdd:TIGR00927 834 EQELNAENQGEAKQ--DEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
333-466 |
1.11e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.92 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 333 RIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 412
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 413 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEK 466
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
243-376 |
1.15e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.92 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 243 RIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKE 322
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 323 RAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEK 376
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
440-697 |
1.24e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 440 EKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERA 519
Cdd:PRK07735 13 EAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 520 AKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLE 599
Cdd:PRK07735 93 AKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 600 KERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKE 679
Cdd:PRK07735 173 AKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAAR 252
|
250
....*....|....*...
gi 1955802949 680 KERAAVKGHLVKEKTAKA 697
Cdd:PRK07735 253 AKTKGAEGKKEEEPKQEE 270
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
366-482 |
1.25e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.15 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 366 KERAAKEKAE-KERIEKERAAKEKAEKER----LEKERAAKEKAEKERLEKERAAKEKAEKERiEKERAAKEKAEKERLE 440
Cdd:PRK00247 284 KEHHAEQRAQyREKQKEKKAFLWTLRRNRlrmiITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAEREIN 362
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1955802949 441 KERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKE 482
Cdd:PRK00247 363 REARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENE 404
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
363-501 |
1.25e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.53 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 363 GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKE 442
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 443 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEK 501
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAAST 141
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
241-431 |
1.40e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKEriv 320
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAA--- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 321 keraakgkAEKERIEKERAAKEKAEKERLEKERAAKEKAekegIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERaA 400
Cdd:COG2268 268 --------YEIAEANAEREVQRQLEIAEREREIELQEKE----AEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR-A 334
|
170 180 190
....*....|....*....|....*....|.
gi 1955802949 401 KEKAEKERLEKERAAKEKAEKERIEKERAAK 431
Cdd:COG2268 335 KGLAEAEGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
183-347 |
1.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 183 RLAAQSFSKEKAEKERLERERV---AKEKAEKERLEKERVAKEKAEKERIEKERATKEKaekeRIEKERADKEKAEKERI 259
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEEEAKRIleeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRER----RNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 260 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE--KERIVKERAAKGKAEKERI--E 335
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAVLikE 177
|
170
....*....|..
gi 1955802949 336 KERAAKEKAEKE 347
Cdd:PRK12704 178 IEEEAKEEADKK 189
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
427-558 |
1.41e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.06 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 427 ERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKEgiEKERAAK 506
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKK-EEEKELKEKERRE--KKEKDEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 507 EKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKER 558
Cdd:pfam11600 81 EKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
505-664 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 505 AKEKAEKERIEKERAAKEKAEKERLEKErAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENE 584
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAE-AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 585 RLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAE-------KERVAKESEKErMERERVPKGKERERVA 657
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeaKEILLEKVEEE-ARHEAAVLIKEIEEEA 182
|
....*..
gi 1955802949 658 KERAEKE 664
Cdd:PRK12704 183 KEEADKK 189
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
412-540 |
1.52e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.06 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 412 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKeraaKEKAEKERLEK-ERAA 490
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREKkEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1955802949 491 KEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 540
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
343-440 |
1.53e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 343 KAEKERLEKERAAKEKaEKEGIEKERAAKEKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKERLEKERAAKEKAEKE 422
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARWEA--EKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|....*...
gi 1955802949 423 RIEKERAAKEKAEKERLE 440
Cdd:COG0542 494 LAELEEELAELAPLLREE 511
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
329-388 |
1.56e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.01 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 329 AEKERIEKERAAKEKaEKERLEK--------ERAAKEKAEKEgieKERAAKEKAEKERIEKERAAKEK 388
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKE---REKLAEYEEKLAKLKERLARLKA 874
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
295-450 |
1.62e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.89 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 295 AKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKA 374
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 375 EKERIEKERAAKEKAEKERLEKERAAKEKAEKErlekERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAE 450
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPG 438
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
200-459 |
1.63e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.50 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 200 ERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERA 279
Cdd:PRK07735 13 EAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 280 AKEKAEKErlEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKA 359
Cdd:PRK07735 93 AKAKAAAA--AKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 360 EKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERL 439
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAA 250
|
250 260
....*....|....*....|
gi 1955802949 440 EKERAAKEKAEKERIVKERA 459
Cdd:PRK07735 251 ARAKTKGAEGKKEEEPKQEE 270
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
479-538 |
1.73e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.01 E-value: 1.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 479 AEKERLEKEraaKEKAEKEgieKERAAK--------EKAEKERIEKERAAKEKAEK--ERLEKERAAKEK 538
Cdd:PRK05729 811 AELARLEKE---LAKLEKE---IERVEKklsnegfvAKAPEEVVEKEREKLAEYEEklAKLKERLARLKA 874
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
288-421 |
1.73e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.15 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 288 RLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 367
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1955802949 368 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEK 421
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAK 136
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
455-593 |
1.79e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.06 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 455 VKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKeraaKEKAEKERLEKera 534
Cdd:pfam11600 2 RSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREK--- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 535 aKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAK 593
Cdd:pfam11600 75 -KEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
336-700 |
1.81e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 336 KERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIE-KERAAKEKAEKERLEKERAAKEKAEKERLEKERA 414
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQlREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 415 AKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKER-IVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKE 492
Cdd:COG4372 85 LNEQLQAAQAELAQAQEElESLQEEAEELQEELEELQKERqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 493 KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKEraAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKE 572
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE--AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 573 RIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKE 652
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1955802949 653 RERVAKERAEKERAEKEQQAKELAAKEKERAAVKGHLVKEKTAKAKVE 700
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
433-525 |
1.83e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 433 KAEKERLEKERAAKEKaEKERIVKERAAKGKAEKERIEKERAAKE---KAEKERLEKERAAKEKAEKEGIEKERAAKEKA 509
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*.
gi 1955802949 510 EKERIEKERAAKEKAE 525
Cdd:COG0542 496 ELEEELAELAPLLREE 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
298-390 |
1.83e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 298 KAEKERLEKERAAKEKaEKERIVKERAAKGKAEKERIEKERAAKE---KAEKERLEKERAAKEKAEKEGIEKERAAKEKA 374
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*.
gi 1955802949 375 EKERIEKERAAKEKAE 390
Cdd:COG0542 496 ELEEELAELAPLLREE 511
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
250-380 |
1.83e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 250 DKEKAEKERIEKERAAKEKAEKEriEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKA 329
Cdd:pfam05672 8 DAEEAARILAEKRRQAREQRERE--EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 330 EKERiEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKeKAEKERIE 380
Cdd:pfam05672 86 EERE-QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ-QEEQERLE 134
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
365-678 |
1.84e-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: 41.75 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 365 EKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 444
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 445 AKEKAEKERIVKERAAKgKAEKERIEKERAAKEKAE--KERLEKERAAKEKAEKEGIEKERAAKEKAEKE-RIEKERAAK 521
Cdd:pfam12128 294 TLDDQWKEKRDELNGEL-SAADAAVAKDRSELEALEdqHGAFLDADIETAAADQEQLPSWQSELENLEERlKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 522 EKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQ----LAKEKGR 597
Cdd:pfam12128 373 VTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRlksrLGELKLR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 598 LEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEkERMERERVPKGKERERVAKERAEKERAEKEQQAKELAA 677
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSE-LRQARKRRDQASEALRQASRRLEERQSALDELELQLFP 531
|
.
gi 1955802949 678 K 678
Cdd:pfam12128 532 Q 532
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
198-315 |
1.84e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 198 RLERERVAKEKAEKERlekeRVAKEKAEKERIEKERATKEKAEKERIEKERADKekaeKERIEKERaAKEKAEKERIEKE 277
Cdd:COG0542 403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDELAEL----EEELEALK-ARWEAEKELIEEI 473
|
90 100 110
....*....|....*....|....*....|....*...
gi 1955802949 278 RAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAE 315
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
385-544 |
1.93e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 385 AKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKA 464
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 465 EKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAA-KEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEG 543
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEaHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDG 446
|
.
gi 1955802949 544 I 544
Cdd:PRK13108 447 I 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-471 |
1.96e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAaqSFSKEKAEKERLERERVAKEKaEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:TIGR02169 206 EREKAERYQALLKEKREYEGYELLK--EKEALERQKEAIERQLASLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE------RLEKERAAKEKA 314
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 315 EKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERL 394
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 395 EKERAAKEKAEKERLEKERAAKEKAEKErIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEK 471
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQE-LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
408-546 |
2.05e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 40.15 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 408 RLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKE 487
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 488 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEK 546
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAAST 141
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
280-447 |
2.05e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.50 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 280 AKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKA 359
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 360 EKEGIEKERAAKEKAEKERIEKERAAKEKAEKErlekERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERL 439
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
|
....*...
gi 1955802949 440 EKERAAKE 447
Cdd:PRK13108 443 EPDGIRRQ 450
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
250-350 |
2.15e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 250 DKEKAEKERIEKERAAKEKaEKERIEKERAAKEKAEKERLEKERAAKEKAEKErlEKERAAKEKAEKERIVKERAAKGKA 329
Cdd:COG0542 414 DELERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARWEA--EKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|.
gi 1955802949 330 EKERIEKERAAKEKAEKERLE 350
Cdd:COG0542 491 EKELAELEEELAELAPLLREE 511
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
237-402 |
2.27e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 41.12 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 237 EKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEK 316
Cdd:PRK13108 289 EYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 317 ERIVKERAAKGKAEKERIEKERAAKEKAEKErlekERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEK 396
Cdd:PRK13108 369 ADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEP 444
|
....*.
gi 1955802949 397 ERAAKE 402
Cdd:PRK13108 445 DGIRRQ 450
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
209-268 |
2.28e-03 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 41.58 E-value: 2.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 209 AEKERLEKERvAKEKAEKERIEKeratK-------EKAEKERIEKERADKEKAEkERIEKERAAKEK 268
Cdd:COG0525 815 AERARLEKEL-AKLEKEIARVEK----KlsnegfvAKAPAEVVEKEREKLAEAE-AKLEKLEEQLAR 875
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
373-465 |
2.38e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 373 KAEKERIEKERAAKEKaEKERLEKERAAKEKAEKERLEKERAAKE---KAEKERIEKERAAKEKAEKERLEKERAAKEKA 449
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*.
gi 1955802949 450 EKERIVKERAAKGKAE 465
Cdd:COG0542 496 ELEEELAELAPLLREE 511
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
524-576 |
2.50e-03 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 41.58 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 524 AEKERLEKERAAKEKaEKEGIEK--------ERAAKEKAEKERiEKERATKEKAEK--ERIEK 576
Cdd:COG0525 815 AERARLEKELAKLEK-EIARVEKklsnegfvAKAPAEVVEKER-EKLAEAEAKLEKleEQLAR 875
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
523-626 |
2.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 523 KAEKERLEKERAAKEKaEKEGIEKERAAKEKAEKERIEKERAtkekAEKERIEKERAAKENERLEKEQLAKEKGRLEKER 602
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELE----ALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100
....*....|....*....|....
gi 1955802949 603 LTKENAKKEKENSERVEKERVAKE 626
Cdd:COG0542 492 KELAELEEELAELAPLLREEVTEE 515
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
417-533 |
2.77e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 417 EKAEKERIEKERAAKEKAEKERLEKEraakEKAEKERIVKERAAKgKAEKERIEKERAAKEKAEKERLEKERAAKEKAEK 496
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERL----EKEEEERLRKEELRR-RAEEERARREEEARRLEEERRREEEERQRKAEEE 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1955802949 497 --EGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKER 533
Cdd:pfam05672 85 aeEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREK 123
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
488-632 |
2.86e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 39.29 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 488 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKEGIEKERAAKEKAEKERIEKeratKE 567
Cdd:pfam11600 2 RSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLK-EEAKAEKERAKEEARRKKEEEKELKEKERREK----KE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 568 KAEKERIEKERAAKENERLEKEQLakekgrlekERLTKENAKKEKENSERVEKERVAKERAEKER 632
Cdd:pfam11600 77 KDEKEKAEKLRLKEEKRKEKQEAL---------EAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
216-316 |
2.87e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.99 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 216 KERVAKEKAE-KERIEKERATKEKAEKER----IEKERADKEKAEKERIEKERAAKEKAEKERiEKERAAKEKAEKERLE 290
Cdd:PRK00247 284 KEHHAEQRAQyREKQKEKKAFLWTLRRNRlrmiITPWRAPELHAENAEIKKTRTAEKNEAKAR-KKEIAQKRRAAEREIN 362
|
90 100
....*....|....*....|....*.
gi 1955802949 291 KERAAKEKAEKERLEKERAAKEKAEK 316
Cdd:PRK00247 363 REARQERAAAMARARARRAAVKAKKK 388
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
217-353 |
2.97e-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: 39.29 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 217 ERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKeraaKEKAEKERLEKeraaK 296
Cdd:pfam11600 4 QKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEE----KELKEKERREK----K 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 297 EKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKER 353
Cdd:pfam11600 76 EKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
404-585 |
3.01e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 404 AEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKER 483
Cdd:PRK12678 54 AIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 484 LEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAkekaekerlekERAAKEKAEKEGIEKERAAKEKAEKERIEKER 563
Cdd:PRK12678 134 GEAARRGAARKAGEGGEQPATEARADAAERTEEEERD-----------ERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
170 180
....*....|....*....|..
gi 1955802949 564 ATKEKAEKERIEKERAAKENER 585
Cdd:PRK12678 203 RDRRDRREQGDRREERGRRDGG 224
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
224-283 |
3.03e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 41.24 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 224 AEKERIEKERATKEKaEKERIEKERADK---EKAEKERIEKERAAKEKAEK--ERIEKERAAKEK 283
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKKLSNEgfvAKAPEEVVEKEREKLAEYEEklAKLKERLARLKA 874
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
388-485 |
3.08e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 388 KAEKERLEKERAAKEKaEKERLEKERAAKEKAEKERIEKERAAKEKAEKErlEKERAAKEKAEKERIVKERAAKGKAEKE 467
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARWEA--EKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|....*...
gi 1955802949 468 RIEKERAAKEKAEKERLE 485
Cdd:COG0542 494 LAELEEELAELAPLLREE 511
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
344-683 |
3.10e-03 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 41.39 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 344 AEKERLEKERAAKEKA-EKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKE 422
Cdd:PLN03237 1133 ADRDKLNIEVEDLKKTtPKSLWLKDLDALEKELDKLDKEDAKAEEAREKLQRAAARGESGAAKKVSRQAPKKPAPKKTTK 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 423 RIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAA-KEKAEKERLEKERAAKEKAEKEGIEK 501
Cdd:PLN03237 1213 KASESETTEETYGSSAMETENVAEVVKPKGRAGAKKKAPAAAKEKEEEDEILDlKDRLAAYNLDSAPAQSAKMEETVKAV 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 502 ERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAK 581
Cdd:PLN03237 1293 PARRAAARKKPLASVSVISDSDDDDDDFAVEVSLAERLKKKGGRKPAAANKKAAKPPAAAKKRGPATVQSGQKLLTEMLK 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 582 ENERLekeqlakekgrlekerltkeNAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKER-ERVAKER 660
Cdd:PLN03237 1373 PAEAI--------------------GISPEKKVRKMRASPFNKKSGSVLGRAATNKETESSENVSGSSSSEKdEIDVSAK 1432
|
330 340
....*....|....*....|...
gi 1955802949 661 AEKERAEKEQQAKELAAKEKERA 683
Cdd:PLN03237 1433 PRPQRANRKQTTYVLSDSESESA 1455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-673 |
3.10e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 338 RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAkekAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKE 417
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSS---LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 418 KAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKE 497
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 498 ---GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKErIEKERATKEKAEKERI 574
Cdd:TIGR02169 817 ieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-LESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 575 EKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERMERERVPKGKERE 654
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330
....*....|....*....
gi 1955802949 655 RVAKERAEKERAEKEQQAK 673
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEK 994
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
275-399 |
3.11e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 39.29 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 275 EKERAAKEKAEKERLEKERAAKEKAEKERLEKERAaKEKAEKERIVKERAAKGKAEKERIEKERaakeKAEKERLEKERA 354
Cdd:pfam11600 9 SQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKE-EAKAEKERAKEEARRKKEEEKELKEKER----REKKEKDEKEKA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955802949 355 AKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 399
Cdd:pfam11600 84 EKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKA 128
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
328-420 |
3.27e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 328 KAEKERIEKERAAKEKaEKERLEKERAAKEKAEKEGIEKERAAKE---KAEKERIEKERAAKEKAEKERLEKERAAKEKA 404
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*.
gi 1955802949 405 EKERLEKERAAKEKAE 420
Cdd:COG0542 496 ELEEELAELAPLLREE 511
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
296-519 |
3.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 296 KEKAEKERLEKERAAKEKAeKERIVKERAAkgkAEKERIEKERaaKEKAEKERLEkERAAKEKAEKEGIEKEraAKEKAE 375
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKL-SEALDKLRSY---LPKLNPLREE--KKKVSVKSLE-ELIKDVEEELEKIEKE--IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 376 KERIEKERAAKEKAEKERLE------------------KERAAKEKAEKERLEKERAAKEKAEKERIEKER------AAK 431
Cdd:PRK05771 108 EISELENEIKELEQEIERLEpwgnfdldlslllgfkyvSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvVLK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 432 EKAEK--ERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERaakekaekERLEKEraAKEKAEKEGIEKeRAAKEKA 509
Cdd:PRK05771 188 ELSDEveEELKKLGFERLELEEEGTPSELIREIKEELEEIEKER--------ESLLEE--LKELAKKYLEEL-LALYEYL 256
|
250
....*....|
gi 1955802949 510 EkerIEKERA 519
Cdd:PRK05771 257 E---IELERA 263
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-453 |
3.41e-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: 41.20 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 148 QREAEEKAEKERLEKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKE 227
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 228 RIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 307
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLE--KERAAKEKAEKEGIEKERAAKEKAEKERIEKERAA 385
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 386 KEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKER 453
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
265-432 |
3.46e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 265 AKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKA 344
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 345 EKERLEKERAAKEKAEKEGIEKERAAKEKAEKEriekERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 424
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPA 442
|
....*...
gi 1955802949 425 EKERAAKE 432
Cdd:PRK13108 443 EPDGIRRQ 450
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
524-583 |
3.50e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 40.86 E-value: 3.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 524 AEKERLEKERAAKEKaEKEGIEK--------ERAAKEKAEKERiekERATKEKAEKERIEKERAAKEN 583
Cdd:PRK05729 811 AELARLEKELAKLEK-EIERVEKklsnegfvAKAPEEVVEKER---EKLAEYEEKLAKLKERLARLKA 874
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
161-426 |
3.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKErVAKEKAEKERIEKERAtKEKAE 240
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE-LEELQKERQDLEQQRK-QLEAQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIV 320
Cdd:COG4372 138 IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 321 KERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 400
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
250 260
....*....|....*....|....*.
gi 1955802949 401 KEKAEKERLEKERAAKEKAEKERIEK 426
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLE 323
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
194-300 |
3.65e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 194 AEKERLEReRVAKEKAEKERLEKErvakekaeKERIEKERATKEKAEKERIEKERADKE---KAEKERIEKERAAKEKAE 270
Cdd:COG0542 411 EELDELER-RLEQLEIEKEALKKE--------QDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELE 481
|
90 100 110
....*....|....*....|....*....|
gi 1955802949 271 KERIEKERAAKEKAEKERLEKERAAKEKAE 300
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
284-421 |
3.67e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 39.38 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 284 AEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEG 363
Cdd:pfam07382 4 AQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1955802949 364 IEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEK 421
Cdd:pfam07382 84 VAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAAST 141
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
387-542 |
3.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 387 EKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKaekeRLEKERAAKEKAEKERIVKERAAKGKAEK 466
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRER----RNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 467 ERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERL----EKERAAKEKAEKE 542
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAvlikEIEEEAKEEADKK 189
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
472-599 |
3.72e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 472 ERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKegiEKERAAK 551
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---KAEEEAE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1955802949 552 EKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLE 599
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLE 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-616 |
3.97e-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: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 297 EKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERaakekaekERLEKERAAKEKAEKEGIEKERAAKEKAEK 376
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL--------EELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 377 ERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKErIEKERAAKEKAEKERLEKERAAKEKAEKERIVK 456
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 457 ERAAKGKAEKERIEKERAAKEKaekerlEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAK 536
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATER------RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 537 EKaeKEGIEKERAAKEKAEKERIEKERATKEKAEK-ERIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENS 615
Cdd:TIGR02168 891 LL--RSELEELSEELRELESKRSELRRELEELREKlAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
.
gi 1955802949 616 E 616
Cdd:TIGR02168 969 E 969
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
246-369 |
4.09e-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: 38.90 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 246 KERADKEKAEKERIEKERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKERLEKERaakeKAEKERIVKERA 324
Cdd:pfam11600 8 QSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEaKAEKERAKEEARRKKEEEKELKEKER----REKKEKDEKEKA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1955802949 325 AKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERA 369
Cdd:pfam11600 84 EKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKA 128
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
413-588 |
4.11e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 413 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKE 492
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 493 KAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKErLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKE 572
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAE-LEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEA 349
|
170
....*....|....*.
gi 1955802949 573 RIEKERAAKENERLEK 588
Cdd:COG2268 350 WNKLGDAAILLMLIEK 365
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
190-258 |
4.21e-03 |
|
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: 40.85 E-value: 4.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955802949 190 SKEKAEKERlERERVAKEKAEKErleKERVAKEKAEKERIEKERA---TKEKAEKERIEKERADKEKAEKER 258
Cdd:NF033875 195 SKDLAAKEK-EVDQLQKEQAKKI---AQQAAELKAKNEKIAKENAeiaAKNKAEKERYEKEVAEYNKHKNEN 262
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
383-446 |
4.39e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 40.63 E-value: 4.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 383 RAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKER-----AAKEKAEKERLEKERAAK 446
Cdd:PLN03086 6 RRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRrldaiEAQIKADQQMQESLQAGR 74
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
503-560 |
4.47e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 40.63 E-value: 4.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955802949 503 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKER-----AAKEKAEKERIE 560
Cdd:PLN03086 6 RRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRrldaiEAQIKADQQMQE 68
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
655-755 |
4.53e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 40.49 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 655 RVAKERAEKERAEKE---QQAKELAAKEKERAAVKghlvkEKTAKAKVETEQLPKIEREQLPKAKAGKERAEKERLLKEK 731
Cdd:PTZ00266 429 RVDKDHAERARIEKEnahRKALEMKILEKKRIERL-----EREERERLERERMERIERERLERERLERERLERDRLERDR 503
|
90 100
....*....|....*....|....
gi 1955802949 732 IDGERVVKEKRAKQAKEEMPEKNA 755
Cdd:PTZ00266 504 LDRLERERVDRLERDRLEKARRNS 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-703 |
4.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 363 GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIEKERAAKEKAE--KERLE 440
Cdd:TIGR02169 164 GVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALErqKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 441 KERAAKEKaEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAA 520
Cdd:TIGR02169 244 RQLASLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 521 KEKAEKERLEKERAAKEKAEKEgIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKENERLEKEQLAKEKGRLEK 600
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 601 ERLTKENAKKEKENSERVEKERVAKERAEKERVAKESEKERME--RERVPKGKERERVAKERAEKERAEKEQQAKELAAK 678
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340
....*....|....*....|....*
gi 1955802949 679 EKERAAVKGHLVKEKTAKAKVETEQ 703
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERV 506
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
463-555 |
4.63e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 463 KAEKERIEKERAAKEKaEKERLEKERAAKEKAEKEGIEKERAAKE---KAEKERIEKERAAKEKAEKERLEKERAAKEKA 539
Cdd:COG0542 417 ERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*.
gi 1955802949 540 EKEGIEKERAAKEKAE 555
Cdd:COG0542 496 ELEEELAELAPLLREE 511
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
163-275 |
4.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 163 EKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKE 242
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110
....*....|....*....|....*....|....
gi 1955802949 243 RI-EKERADKEKAEKERIEKERAAKEKAEKERIE 275
Cdd:PRK00409 603 SVkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
205-378 |
5.02e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.35 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 205 AKEKAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKA 284
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEET 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 285 EKERLEKERAAKEKAEKERLEKERAAKEKAEKErivkERAAKGKAEKERIEKERAAKE--KAEKERLEKERAAKEKAEKE 362
Cdd:PRK13108 367 SEADIEREQPGDLAGQAPAAHQVDAEAASAAPE----EPAALASEAHDETEPEVPEKAapIPDPAKPDELAVAGPGDDPA 442
|
170
....*....|....*.
gi 1955802949 363 GIEKERAAKEKAEKER 378
Cdd:PRK13108 443 EPDGIRRQDDFSSRRR 458
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
344-450 |
5.31e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 344 AEKERLEKERAAKEkaekegIEKERAAKEKAEKeriEKERAAKEKAEKERLEKERAAKE---KAEKERLEKERAAKEKAE 420
Cdd:COG0542 411 EELDELERRLEQLE------IEKEALKKEQDEA---SFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELE 481
|
90 100 110
....*....|....*....|....*....|
gi 1955802949 421 KERIEKERAAKEKAEKERLEKERAAKEKAE 450
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
160-270 |
5.58e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 160 LEKEKLEKERIEKKTELERMEKERLAAQSfSKEKAEKERLE--RERVAKEKAEKERLEkervAKEKAEKERIEKERATKE 237
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEALKK-EQDEASFERLAelRDELAELEEELEALK----ARWEAEKELIEEIQELKE 478
|
90 100 110
....*....|....*....|....*....|...
gi 1955802949 238 KAEKERIEKERADKEKAEKERIEKERAAKEKAE 270
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
228-366 |
5.71e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 38.61 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 228 RIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKE 307
Cdd:pfam07382 3 GAQKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 308 RAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEK 366
Cdd:pfam07382 83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAAST 141
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-473 |
5.91e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKeKAEKERIEKERATKEKAE 240
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKE-KAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERI 319
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 320 VKERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERA 399
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 400 AKEKAEKERLEKERAA----KEKAEKERIEKERAAKE----KAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEK 471
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEElsleDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
..
gi 1955802949 472 ER 473
Cdd:TIGR02169 1015 KK 1016
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
161-547 |
6.13e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 40.05 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKERIEKKTELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKEKAE 240
Cdd:pfam04747 125 EQERIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERIV 320
Cdd:pfam04747 205 AEQVQEITGKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 321 KERAAKGKAEKERIEKERAAKEKAEKERLEKEraaKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 400
Cdd:pfam04747 285 TTPPASENQKKNKKDKKKSESEKVVEEPVQAE---APKSKKPTADDNMDFLDFVTAKEEPKDEPAETPAAPVEEVVENVV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 401 KEKAEKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAE 480
Cdd:pfam04747 362 ENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQ 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 481 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKE 547
Cdd:pfam04747 442 AAPSSKKPTADDNMDFLDFVTAKPDKSESVEEHIAAPMIVEPAHADEETAAAAEGKKKNKKDKKKKE 508
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
434-493 |
6.14e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 40.09 E-value: 6.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 434 AEKERLEKEraaKEKAEKErivKERAAK--------GKAEKERIEKERAAKEKAEK--ERLEKERAAKEK 493
Cdd:PRK05729 811 AELARLEKE---LAKLEKE---IERVEKklsnegfvAKAPEEVVEKEREKLAEYEEklAKLKERLARLKA 874
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
487-741 |
6.51e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 39.98 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 487 ERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEG-IEKERAAKEKAEKER---IEKE 562
Cdd:TIGR00927 609 ELWVKEQLSRRPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGeAEQEGETETKGENESegeIPAE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 563 RATKEKAEKErIEKERAAKENERLEKEQLAKEKGrlEKERLTKENAKKEKENSERVEKERVAKERAEKErvaKESEKERm 642
Cdd:TIGR00927 689 RKGEQEGEGE-IEAKEADHKGETEAEEVEHEGET--EAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHE---VETEGDR- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 643 erervpkgKERERVAKERAEKERAEKEQQAKelAAKEKERAAVKGHLVKEKTAKAKVETEQLPKIEREQLPKAKAGKERA 722
Cdd:TIGR00927 762 --------KETEHEGETEAEGKEDEDEGEIQ--AGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE 831
|
250
....*....|....*....
gi 1955802949 723 EKERLLKEKIDGERVVKEK 741
Cdd:TIGR00927 832 TGEQELNAENQGEAKQDEK 850
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
178-684 |
6.66e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 178 RMEKERLAAQSFSKEKAEKERLERErvAKEKAEKERLEKeRVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKE 257
Cdd:NF041483 650 RAEGENVAVRLRSEAAAEAERLKSE--AQESADRVRAEA-AAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEA 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 258 RIEKERAAKEKAEKERIEKERAAKEKAEKERLEKER--------AAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKA 329
Cdd:NF041483 727 DQERERAREQSEELLASARKRVEEAQAEAQRLVEEAdrratelvSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAA 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 330 EKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI------EKERAAKEKAEKERLEKERAAKEK 403
Cdd:NF041483 807 ERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTvseaiaEAERLRSDASEYAQRVRTEASDTL 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 404 AEKERLEKERAAKEKAEKERIEKERAAKEK---AEKERLEKERAAKEKAEKERIVKERAAKgkAEKERIEKERAAKEKAE 480
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRSDAAAQADrliGEATSEAERLTAEARAEAERLRDEARAE--AERVRADAAAQAEQLIA 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 481 KERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKE-RAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERI 559
Cdd:NF041483 965 EATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEaAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLIT 1044
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 560 EKERATKEKAEKERIEKERAAKENERLEKEQLA---KEKGRLEKERLTKENAKKEKENSERVE-------KERVAKERAE 629
Cdd:NF041483 1045 EAAAEADQLTAKAQEEALRTTTEAEAQADTMVGaarKEAERIVAEATVEGNSLVEKARTDADEllvgarrDATAIRERAE 1124
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1955802949 630 KERVAKESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAA 684
Cdd:NF041483 1125 ELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVS 1179
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
227-350 |
6.81e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.10 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 227 ERIEKERATKEKAEKERIEKERADKEKAEKERiekERAAKEKAEKERIEKERAAKEKAEKE--RLEKERAAKEKAEKERL 304
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEERLRKEELR---RRAEEERARREEEARRLEEERRREEEerQRKAEEEAEEREQREQE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1955802949 305 EKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLE 350
Cdd:pfam05672 95 EQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIE 140
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
239-298 |
6.98e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 40.09 E-value: 6.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 239 AEKERIEKEradKEKAEKErieKERAAK--------EKAEKERIEKERAAKEKAEK--ERLEKERAAKEK 298
Cdd:PRK05729 811 AELARLEKE---LAKLEKE---IERVEKklsnegfvAKAPEEVVEKEREKLAEYEEklAKLKERLARLKA 874
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
368-431 |
7.66e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 39.86 E-value: 7.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955802949 368 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKER-----AAKEKAEKERIEKERAAK 431
Cdd:PLN03086 6 RRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRrldaiEAQIKADQQMQESLQAGR 74
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
208-435 |
8.01e-03 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 39.85 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 208 KAEKERLEKERVAKEKAEKERIEKERATKEKAEKERIEKERADKEKAEKERIEKERAAKEKAEKERIEKERAAKEKAEKE 287
Cdd:PLN03237 1174 KAEEAREKLQRAAARGESGAAKKVSRQAPKKPAPKKTTKKASESETTEETYGSSAMETENVAEVVKPKGRAGAKKKAPAA 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 288 RLEKERAAKEKAEKERLEKER---AAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKER--LEKERAAKEKAEKE 362
Cdd:PLN03237 1254 AKEKEEEDEILDLKDRLAAYNldsAPAQSAKMEETVKAVPARRAAARKKPLASVSVISDSDDDDddFAVEVSLAERLKKK 1333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955802949 363 GIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKERAAKEKA----EKERIEKERAAKEKAE 435
Cdd:PLN03237 1334 GGRKPAAANKKAAKPPAAAKKRGPATVQSGQKLLTEMLKPAEAIGISPEKKVRKMRAspfnKKSGSVLGRAATNKET 1410
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
353-488 |
8.18e-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: 38.13 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 353 RAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERlEKERAAKEKAEKERLEKERAAKEKAEKERIEKeraaKE 432
Cdd:pfam11600 2 RSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLK-EEAKAEKERAKEEARRKKEEEKELKEKERREK----KE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 433 KAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERLEKER 488
Cdd:pfam11600 77 KDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
385-448 |
8.38e-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: 39.09 E-value: 8.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955802949 385 AKEKAEKERLEKERAAKEKAEKERLEKERAAKEKAEKERiEKERAAKEKAEKER--LEKERAAKEK 448
Cdd:pfam07946 258 ALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKE-REEKLAKLSPEEQRkyEEKERKKEQR 322
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
161-686 |
9.49e-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: 39.44 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 161 EKEKLEKeriekktELERMEKERLAAQSFSKEKAEKERLERERVAKEKAEKERLEKERVAKEKAEKERIEKERATKeKAE 240
Cdd:pfam12128 242 EFTKLQQ-------EFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGEL-SAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 241 KERIEKERADKEKAE--KERIEKERAAKEKAEKERIEKERAAKEKAEKE-RLEKERAAKEKAEKERLEKERAAKEKAEKE 317
Cdd:pfam12128 314 DAAVAKDRSELEALEdqHGAFLDADIETAAADQEQLPSWQSELENLEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 318 RIVKERAakgkAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKE 397
Cdd:pfam12128 394 GIKDKLA----KIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 398 RAAKEKAeKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKE 477
Cdd:pfam12128 470 DERIERA-REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 478 KAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKER--AAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAE 555
Cdd:pfam12128 549 QSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 556 KERIEKERATKEkaekerIEKERAAKENERLEKEQLAKEKGRLEKERLTKENAKKEKENSERVEKERVAKERAEKERVAK 635
Cdd:pfam12128 629 QANGELEKASRE------ETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWL 702
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1955802949 636 ESEKERMERERVPKGKERERVAKERAEKERAEKEQQAKELAAKEKERAAVK 686
Cdd:pfam12128 703 EEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-484 |
9.64e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 329 AEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKE----KA 404
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 405 EKERLEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERIVKERAAKGKAEKERIEKERAAKEKAEKERL 484
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
263-317 |
9.74e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 39.47 E-value: 9.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 263 RAAKEKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKERLEKER-----AAKEKAEKE 317
Cdd:PLN03086 6 RRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAIEAAQRSRrldaiEAQIKADQQ 65
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
299-405 |
9.80e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 299 AEKERLEKERAAKEKaEKERIVKEraakgkaeKERIEKERAAKEKAEKERLEKERAAKE---KAEKEGIEKERAAKEKAE 375
Cdd:COG0542 411 EELDELERRLEQLEI-EKEALKKE--------QDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELE 481
|
90 100 110
....*....|....*....|....*....|
gi 1955802949 376 KERIEKERAAKEKAEKERLEKERAAKEKAE 405
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
434-540 |
9.80e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 434 AEKERLEKERAAKEKaEKERIVKEraakgkaeKERIEKERAAKEKAEKERLEKERAAKE---KAEKEGIEKERAAKEKAE 510
Cdd:COG0542 411 EELDELERRLEQLEI-EKEALKKE--------QDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELE 481
|
90 100 110
....*....|....*....|....*....|
gi 1955802949 511 KERIEKERAAKEKAEKERLEKERAAKEKAE 540
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| HC2 |
pfam07382 |
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ... |
456-582 |
9.94e-03 |
|
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.
Pssm-ID: 369339 [Multi-domain] Cd Length: 187 Bit Score: 37.84 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955802949 456 KERAAKGKAEKERIEKERAAKEKAEKERLEKERAAKEKAEKEGIEKERAAKEKAEKERIEKERAAKEKAEKERLEKERAA 535
Cdd:pfam07382 6 KKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAVA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1955802949 536 KEKAEKEGIEKERAAKEKAEKERIEKERATKEKAEKERIEKERAAKE 582
Cdd:pfam07382 86 KKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKK 132
|
|
|