|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-776 |
1.80e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQE-ERKAAIKKRQEEARKhgKAETGLKQRPLNKE-QEKRSALRRELKPRPQHKAPNAI 547
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKK--KAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 548 EKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQkeyeKDRLKKQESLKKINDQSDESTNltALRNQNRRTGQRSKKRE 627
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKAD 1537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 628 TGHQTLMKRQGEKVlqptNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVK 707
Cdd:PTZ00121 1538 EAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488310544 708 QVTQVDVPQTHSTPQRVQPKVNEPITRMNRHNTPIIKKEKRTKQSPVVRRERKKPGTQKITNKPKGVRQ 776
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
473-761 |
5.81e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 473 MRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQR---PLNKEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 AQEGLRQAHE-KGRMQEQKSEEQLKRQQHESARQKEYEK--DRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKR 626
Cdd:PTZ00121 1400 AEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 627 ETGHQT-LMKRQGEkvlQPTNKPKDMKKQVVARSprrtgQPTTRQNIQPKVAAQTVKRSGGTLGSNPAyRRPEVRKKMDQ 705
Cdd:PTZ00121 1480 EEAKKAdEAKKKAE---EAKKKADEAKKAAEAKK-----KADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADE 1550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488310544 706 VKQVTQVDvpQTHSTPQRVQPKVNEPITRMNRHNTPIIKK--EKRTKQSPVVRRERKK 761
Cdd:PTZ00121 1551 LKKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKK 1606
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-711 |
5.23e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKhgKAETGLKqrplnKEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAAKK-----KAEEKKKADEAKKKAEEDKKKADELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 AQEGLRQAHE-KGRMQEQKSEEQLKRQQHESARQKEYEK--DRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKR 626
Cdd:PTZ00121 1413 AAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 627 ETGHQTlmKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSggtlgsnPAYRRPEVRKKMDQV 706
Cdd:PTZ00121 1493 EEAKKK--ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA-------DELKKAEELKKAEEK 1563
|
....*
gi 488310544 707 KQVTQ 711
Cdd:PTZ00121 1564 KKAEE 1568
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-708 |
2.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKhgkaetglkqrplnkEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK---------------AEEKKKADEAKKKAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 AQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRETG 629
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 630 HQT---LMKRQGEKvlqptNKPKDMKKQVvarSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQV 706
Cdd:PTZ00121 1404 KKKadeLKKAAAAK-----KKADEAKKKA---EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
..
gi 488310544 707 KQ 708
Cdd:PTZ00121 1476 KK 1477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-627 |
2.18e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHgKAETGLKQRPLNKEQEKRSALRRELKprpqHKAPNAIEK 549
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK-EAEEKKKAEELKKAEEENKIKAEEAK----KEAEEDKKK 1745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 AQEGLRQAHEKGRMQEQKSEEQLK----RQQHESARQKEY-EKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSK 624
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKaeeiRKEKEAVIEEELdEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
...
gi 488310544 625 KRE 627
Cdd:PTZ00121 1826 EME 1828
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
476-642 |
2.55e-09 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 60.05 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 476 AAREQKQENKERRKQAQ---EERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSA-LRRELKPRPQHKAPNAIEK-- 549
Cdd:pfam15558 15 ARHKEEQRMRELQQQAAlawEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKArLGREERRRADRREKQVIEKes 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 -------AQEGLRQAH-EKGRMQeqksEEQLKRQQHESARQKEYEKDRLKKQESLkkindQSDESTNLTALRNQNRRTGQ 621
Cdd:pfam15558 95 rwreqaeDQENQRQEKlERARQE----AEQRKQCQEQRLKEKEEELQALREQNSL-----QLQERLEEACHKRQLKEREE 165
|
170 180
....*....|....*....|.
gi 488310544 622 RSKKRETGHQTLMKRQGEKVL 642
Cdd:pfam15558 166 QKKVQENNLSELLNHQARKVL 186
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-781 |
3.11e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 550 AQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEK--DRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRE 627
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 628 TGHQTLMKRQGEKvlqpTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTlgSNPAYRRPEVRKKMDQVK 707
Cdd:PTZ00121 1520 EAKKADEAKKAEE----AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED--KNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488310544 708 QVTQVDVPQTHSTPQRVQPKVNEPitrmNRHNTPIIKKEKRTKQSPVVRRERKKPGTQKITNKPKGVRQPRARK 781
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-781 |
4.76e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQaqEERKAAI-------KKRQEEARKH---GKAETGLKQRPLNKEQEKRSAlrrELKPRP 539
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKA--EEAKKADeakkaeeAKKADEAKKAeekKKADELKKAEELKKAEEKKKA---EEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 540 QHKAPNAIEKAQEgLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKdrlKKQESLKKINDQSDESTNLTALRNQNRRT 619
Cdd:PTZ00121 1573 EEDKNMALRKAEE-AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK---IKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 620 GQRSKKRETGHQTLMKRQGEKVLQPTNKPKDMKKqvvARSPRRTGQPTTRQNIQPKVAAQTVKRsggtlgsnpayRRPEV 699
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK---AEEDEKKAAEALKKEAEEAKKAEELKK-----------KEAEE 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 700 RKKMDQVK---QVTQVDVPQTHSTPQRVQPKVNEPITRMNRHNTPIIKKEKRTKQSPVVRRERKKPGTQKITNKPKGVRQ 776
Cdd:PTZ00121 1715 KKKAEELKkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....*
gi 488310544 777 PRARK 781
Cdd:PTZ00121 1795 EVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
474-708 |
1.21e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQEN----KERRKQAQEERKAAIKKRQEEARKHGKAETGLKQR--PLNKEQEKRSAlrRELKPRPQHKAPNAI 547
Cdd:PTZ00121 1218 RKAEDAKKAEAvkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqAAIKAEEARKA--DELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 548 EKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKdrlKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRE 627
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 628 TGHQTLMKRQGEKVLQPTNKPKDMKKQvvARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVK 707
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
.
gi 488310544 708 Q 708
Cdd:PTZ00121 1451 K 1451
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
474-594 |
1.38e-08 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 54.66 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQK-QENKERRKQAQEERKAA--IKKRQEEARKHGKAETglkQRPlnKEQEKRSALRRELKPRPqhkapnaiEKA 550
Cdd:pfam05672 20 RRQAREQReREEQERLEKEEEERLRKeeLRRRAEEERARREEEA---RRL--EEERRREEEERQRKAEE--------EAE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488310544 551 QEGLRQAHEKGRMQEQKSEEQlkRQQHESARQKEYEKDRLKKQE 594
Cdd:pfam05672 87 EREQREQEEQERLQKQKEEAE--AKAREEAERQRQEREKIMQQE 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-708 |
3.87e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENK-ERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIE 548
Cdd:PTZ00121 1198 DARKAEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 549 KAQEGLRQAHEKGRMQEQKSEEQLKRQqhESARQKEYEKDrlKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRET 628
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 629 GHQTLMKRQGEKVLQPTNKPKDMKKQV-----VARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKM 703
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAdaakkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
....*
gi 488310544 704 DQVKQ 708
Cdd:PTZ00121 1434 DEAKK 1438
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
478-597 |
8.86e-08 |
|
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: 55.34 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 478 REQKQENKERRKQAQEE-------RKAAI---KKRQEEARKHGKAETGLKQRPLNKEQEK----RSALRRELKPRPQHKA 543
Cdd:pfam15709 361 RRLQQEQLERAEKMREEleleqqrRFEEIrlrKQRLEEERQRQEEEERKQRLQLQAAQERarqqQEEFRRKLQELQRKKQ 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488310544 544 PNAIEKAQEG--------LRQAHEKGRMQEQKSEEQL----KRQQHESARQKEYEKDRLKKQESLK 597
Cdd:pfam15709 441 QEEAERAEAEkqrqkeleMQLAEEQKRLMEMAEEERLeyqrQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
470-605 |
2.03e-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: 53.70 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETglkqrplNKEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-------AKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488310544 550 AQEglrQAHEKGRMQEQKSEEQLKRQQHESARQKEyEKDRLKKQESLKKINDQSDE 605
Cdd:TIGR02794 152 AEE---EAKAKAAAEAKKKAEEAKKKAEAEAKAKA-EAEAKAKAEEAKAKAEAAKA 203
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
475-596 |
2.61e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.19 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 475 RAAR-EQKQENKERRKQAQEERKAAIKKRQEEARKHgKAETGLKQRP------LNKEQEKRSALRRELKPRPQHKAPNAi 547
Cdd:pfam15709 339 RAERaEMRRLEVERKRREQEEQRRLQQEQLERAEKM-REELELEQQRrfeeirLRKQRLEEERQRQEEEERKQRLQLQA- 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488310544 548 ekAQEGLRQAHEKGR-----MQEQKSEEQLKRQQHESARQKEYEKDRLKKQESL 596
Cdd:pfam15709 417 --AQERARQQQEEFRrklqeLQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRL 468
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
479-708 |
3.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 479 EQKQENKERRKQAQEERKAAIKKRQEEARK---HGKAETGLKQRPLNKEQEKRSA--LRRELKPRPQHKAPNAIE--KAQ 551
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKaeeARKAEDAKRVEIARKAEDARKAeeARKAEDAKKAEAARKAEEvrKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 EgLRQAHEKGRMQEQKSEEQLKRQqhESARQKEYEK--DRLKKQESLKKINDQ---SDESTNLTALRNQNRRTGQRSKKR 626
Cdd:PTZ00121 1192 E-LRKAEDARKAEAARKAEEERKA--EEARKAEDAKkaEAVKKAEEAKKDAEEakkAEEERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 627 ETGHQTLMKRQGEKVLQPTNKPK--DMKKqvvARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMD 704
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKadEAKK---AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
....
gi 488310544 705 QVKQ 708
Cdd:PTZ00121 1346 EAAK 1349
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
471-594 |
3.65e-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: 53.42 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 471 ANMRRAAREQK---QENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEkrsalRRELKPRPQHKAPNAi 547
Cdd:pfam15709 343 AEMRRLEVERKrreQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ-----RQEEEERKQRLQLQA- 416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488310544 548 ekAQEGLRQAHEKGRMQEQksEEQLKRQQhESARQKEYEKDRLKKQE 594
Cdd:pfam15709 417 --AQERARQQQEEFRRKLQ--ELQRKKQQ-EEAERAEAEKQRQKELE 458
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-713 |
5.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 472 NMRRAAREQKQENKER---RKQAQEERKAAIKKRQEEARK---HGKAETGLKQRPLNKEQEKRSA--------LRR--EL 535
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRveiARKAEDARKAEEARKAEDAKKaeaARKAEEVRKAEELRKAEDARKAeaarkaeeERKaeEA 1217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 536 KPRPQHKAPNAIEKAQEGLRQAHEKGRMQEQKSEEQLK-----RQQHESARQKEYEKDRLKKQESLKKIND--QSDEstn 608
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRkfeeaRMAHFARRQAAIKAEEARKADELKKAEEkkKADE--- 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 609 ltALRNQNRRTGQRSKKR--ETGHQTLMKRQGE----KVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVK 682
Cdd:PTZ00121 1295 --AKKAEEKKKADEAKKKaeEAKKADEAKKKAEeakkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
250 260 270
....*....|....*....|....*....|.
gi 488310544 683 RSGGTLGSNPAYRRPEVRKKMDQVKQVTQVD 713
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
470-771 |
6.81e-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: 52.82 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQE---------------EARKhgKAETGLKQRPLNKEQEKRSALRRE 534
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQErmamererelerirqEERK--RELERIRQEEIAMEISRMRELERL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 535 LKPRPQ--HKAPNAIEKAQEGLRQAHEKGR-MQEQKSEEQLKRQQHESARQKE---YEKDRLKKQESLKKinDQSDESTN 608
Cdd:pfam17380 384 QMERQQknERVRQELEAARKVKILEEERQRkIQQQKVEMEQIRAEQEEARQREvrrLEEERAREMERVRL--EEQERQQQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 609 LTALRNQ--NRRTGQRSKKRETGHQTLMKRQGEKVLQptNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGg 686
Cdd:pfam17380 462 VERLRQQeeERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA- 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 687 tlgsnpayrrPEVRKKMDQVKQVTQVDVPQTHSTPQRVQPKVNEPITRMNRHntpIIKKEKRTKQSPVVrrerkkpgTQK 766
Cdd:pfam17380 539 ----------EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ---IVESEKARAEYEAT--------TPI 597
|
....*
gi 488310544 767 ITNKP 771
Cdd:pfam17380 598 TTIKP 602
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
470-605 |
1.19e-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: 51.88 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKaaikKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEK 549
Cdd:pfam15709 375 REELELEQQRRFEEIRLRKQRLEEERQ----RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAE 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488310544 550 AQ----EGLRQAHEKGRM-----------QEQKSEEQLKRQQH-ESARQKEYEKDRLKKQESLKKINDQSDE 605
Cdd:pfam15709 451 KQrqkeLEMQLAEEQKRLmemaeeerleyQRQKQEAEEKARLEaEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
473-598 |
1.98e-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: 50.61 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 473 MRRAAREQKQENKERRKQAQEERKAAIKKR-QEEARKhgkaeTGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQ 551
Cdd:TIGR02794 55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRaAEQARQ-----KELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488310544 552 EGLRQAHEKGRmqEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKK 598
Cdd:TIGR02794 130 AEAKAKAEAEA--ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKK 174
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
481-600 |
2.11e-06 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 49.32 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 481 KQENKERRKQAQEERKAaiKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAI-----EKAQEGLR 555
Cdd:pfam13904 64 KQRQRQKELQAQKEERE--KEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLakperKVSQEEAK 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488310544 556 QaHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKIN 600
Cdd:pfam13904 142 E-VLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQ 185
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
472-781 |
2.07e-05 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 47.75 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 472 NMRRAAREQKQENKerrkqaQEERKAAIKKRQEEARKHGKAETGLKQRPLN----KEQEKRSALRRELKPRPQHKAPNAI 547
Cdd:pfam04747 22 NLGRVAKSQRNQFR------QWLLTAVLPNSINDQRKEAFASLELTEQPQQvekvKKSEKKKAQKQIAKDHEAEQKVNAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 548 EKAQEGLRQAHEKGRMQEQKSEEQlkrqQHESARQKEYEKDRLKKQESLKKINDQSDEStnlTALRNQNRRTGQRSKKRE 627
Cdd:pfam04747 96 KAAEKEARRAEAEAKKRAAQEEEH----KQWKAEQERIQKEQEKKEADLKKLQAEKKKE---KAVKAEKAEKAEKTKKAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 628 TGhqtlmkrqgekvlQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVK 707
Cdd:pfam04747 169 TP-------------APVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 708 QVTQVDVPQTHSTPQRVQPKVNEPITRMNRHNTPIIKKEKRTKQSPVV-------------RRERKKPGTQKITNKPKGV 774
Cdd:pfam04747 236 QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVettppasenqkknKKDKKKSESEKVVEEPVQA 315
|
....*..
gi 488310544 775 RQPRARK 781
Cdd:pfam04747 316 EAPKSKK 322
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
474-723 |
2.15e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNK-EQEKRSALRRELKPRPQHKAPNAIEKAQE 552
Cdd:COG3064 12 AAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKaEAEQRAAELAAEAAKKLAEAEKAAAEAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 553 glRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKindQSDESTNLTALRNQNRRTGQRSKKRETGHQT 632
Cdd:COG3064 92 --KAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR---KAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 633 LMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVKQVTQV 712
Cdd:COG3064 167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALG 246
|
250
....*....|.
gi 488310544 713 DVPQTHSTPQR 723
Cdd:COG3064 247 GAEEAADLAAV 257
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
474-774 |
3.09e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSA--------LRRELKP---RPQHK 542
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAeaekaaaeAEKKAAAekaKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 543 APNAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQR 622
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 623 SKKRETGHQTLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTlgsNPAYRRPEVRKK 702
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGA---EEAADLAAVGVL 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488310544 703 MDQVKQVTQVDVPQTHSTPQRVQPKVNEPITRMNRHNTPIIKKEKRTKQSPVVRRERKKPGTQKITNKPKGV 774
Cdd:COG3064 261 GAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGG 332
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
483-602 |
3.70e-05 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 44.40 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 483 ENKERRKQAQEERKAAIKKRQEEARkhgkaetglKQRPLNKEQEKRsalrrelkprpqhkapnaiEKAQEGLRQAHEKGR 562
Cdd:pfam15236 45 EERERKRQKALEHQNAIKKQLEEKE---------RQKKLEEERRRQ-------------------EEQEEEERLRREREE 96
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488310544 563 MQEQKSEEQLKRQQHESARQKEYE--KDRLKKQESLKKINDQ 602
Cdd:pfam15236 97 EQKQFEEERRKQKEKEEAMTRKTQalLQAMQKAQELAQRLKQ 138
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
474-628 |
5.00e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQE------EARKHGKAEtgLKQRPLNKEQEKRSALRRELKPRPQHKApnAI 547
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEkeeerkEERKRYRQE--LEEQIEEREQKRQEEYEEKLQEREQMDE--IV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 548 EKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQEslKKINDQSDESTNLTALRNQNRRTGQRSKKRE 627
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED--ERILEYLKEKAEREEEREAEREEIEEEKERE 185
|
.
gi 488310544 628 T 628
Cdd:pfam13868 186 I 186
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
470-639 |
5.23e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQ---EERKAAIKKRQEEARKHgkAETGLKQRPLNKEQEKRSAL-RRELKPRPQHKAPN 545
Cdd:TIGR00618 271 ELRAQEAVLEETQERINRARKAAplaAHIKAVTQIEQQAQRIH--TELQSKMRSRAKLLMKRAAHvKQQSSIEEQRRLLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 546 AIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDrLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKK 625
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTL-TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
170
....*....|....
gi 488310544 626 RETGHQTLMKRQGE 639
Cdd:TIGR00618 428 HAKKQQELQQRYAE 441
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
470-636 |
5.52e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEAR--------KHGKAETGLKQRPLNKEQEKRSALRRELKPRPQH 541
Cdd:pfam02463 271 LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 542 KAPNAIEKAQEGLRQAHEKgRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLtALRNQNRRTGQ 621
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLE-QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL-EDLLKEEKKEE 428
|
170
....*....|....*
gi 488310544 622 RSKKRETGHQTLMKR 636
Cdd:pfam02463 429 LEILEEEEESIELKQ 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-627 |
8.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRpLNKEQEKRSALRRELkprpqHKAPNAIEK 549
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-LEELELELEEAQAEE-----YELLAELAR 299
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488310544 550 AQEGLRQAHEKgRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRE 627
Cdd:COG1196 300 LEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
470-598 |
1.01e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAI----KKRQEEARKhgKAETglKQRPLNKEQEKRSALRRELKPRPQHKAPN 545
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEaeaeRKAKEEAAK--QAEE--EAKAKAAAEAKKKAEEAKKKAEAEAKAKA 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 488310544 546 -AIEKAQEGLRQAhekgrmqeqKSEEQLKRQQHESARQKEYEKDRLKKQESLKK 598
Cdd:TIGR02794 184 eAEAKAKAEEAKA---------KAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| Activator_LAG-3 |
pfam11498 |
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ... |
472-583 |
1.03e-04 |
|
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.
Pssm-ID: 151935 [Multi-domain] Cd Length: 476 Bit Score: 45.72 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 472 NMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKaetglkQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQ 551
Cdd:pfam11498 318 NPQHIAQLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQH------QQQQQQEHQQQQMLLQQQQQMHQLQQHHQMNGGG 391
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488310544 552 EGLRQAHEKG---------RMQEQKSEEQLKRQQHESARQK 583
Cdd:pfam11498 392 QFATQAHQHAaylqqmqhmRLQEQIQHQQQQAQHHQQAQQQ 432
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
477-605 |
1.23e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 477 AREQKQENKER-----------RKQAQEERKAAIKKRQEEARKHGKaetgLKQRpLNKEQEKRSALRRELKprpqHKAPN 545
Cdd:PRK00409 507 AKKLIGEDKEKlneliasleelERELEQKAEEAEALLKEAEKLKEE----LEEK-KEKLQEEEDKLLEEAE----KEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 546 AIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARqKEYEKDRLKKQESLKKINDQSDE 605
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
474-635 |
1.77e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGkaETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQEG 553
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSE--ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 554 LRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQR---SKKRETGH 630
Cdd:pfam07888 153 ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttAHRKEAEN 232
|
....*
gi 488310544 631 QTLMK 635
Cdd:pfam07888 233 EALLE 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
474-643 |
2.79e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQEN--KERRKQAQEERKAAIKKRQEEARKHGKAETGLKQrpLNKEQEKRSALRRELKPRPQHKApnAIEKAQ 551
Cdd:COG1196 295 AELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEE--LEEELEEAEEELEEAEAELAEAE--EALLEA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 EGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEY----EKDRLKKQESLKK-INDQSDESTNLTALRNQNRRTGQRSKKR 626
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEeLEELEEALAELEEEEEEEEEALEEAAEE 450
|
170
....*....|....*..
gi 488310544 627 ETGHQTLMKRQGEKVLQ 643
Cdd:COG1196 451 EAELEEEEEALLELLAE 467
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
474-731 |
3.74e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERK--AAIKKRQEEARKhgKAETGLKQRplnKEQEKRSALRRElkprpQHKAPNAIEKAQ 551
Cdd:COG3064 91 KKAAAEKAKAAKEAEAAAAAEKAaaAAEKEKAEEAKR--KAEEEAKRK---AEEERKAAEAEA-----AAKAEAEAARAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 EGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRETGHQ 631
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 632 TLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVKQVTQ 711
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
250 260
....*....|....*....|
gi 488310544 712 VDVPQTHSTPQRVQPKVNEP 731
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAA 340
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
474-621 |
3.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKE--RRKQAQEERKAAIKKRQEEAR-KHGKAETGLKQRPLNKEQEKRSALRRELKPRPQH--------- 541
Cdd:COG4717 80 LKEAEEKEEEYAElqEELEELEEELEELEAELEELReELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleelr 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 542 -------KAPNAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQ-QHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALR 613
Cdd:COG4717 160 eleeeleELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
....*...
gi 488310544 614 NQNRRTGQ 621
Cdd:COG4717 240 ALEERLKE 247
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
470-598 |
4.14e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKER-RKQAQEERKAAIKKRQEEARKHGKAEtglkqrplnkEQEKRSALRRELKPRPQHKAPNAIE 548
Cdd:PRK09510 91 ELQQKQAAEQERLKQLEKeRLAAQEQKKQAEEAAKQAALKQKQAE----------EAAAKAAAAAKAKAEAEAKRAAAAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488310544 549 KAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKK 598
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK 210
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
470-583 |
4.32e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.38 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQ-AQEERKAAIKKRQEEARKhgKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIE 548
Cdd:pfam13904 71 ELQAQKEEREKEEQEAELRKRlAKEKYQEWLQRKARQQTK--KREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWE 148
|
90 100 110
....*....|....*....|....*....|....*...
gi 488310544 549 ---KAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQK 583
Cdd:pfam13904 149 rkkLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
478-598 |
4.68e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 478 REQKQENKERRKQAQEERKAAiKKRQEEARKHGKAETGLKQ----RPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQEG 553
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQ-QQAEELQQKQAAEQERLKQlekeRLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488310544 554 LRQAHEkgrmQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKK 598
Cdd:PRK09510 145 AKAKAE----AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKK 185
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
475-622 |
5.16e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 475 RAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRplnkeQEKRSALRRELKPRPQHKAPNAIEKAQ--- 551
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQsek 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 -------EGLRQAHEKGRMQEQKsEEQLKRQQHE-----SARQKEYEKDRLKKQESLKKINDQSDesTNLTALRNQNRRT 619
Cdd:TIGR00618 690 eqltywkEMLAQCQTLLRELETH-IEEYDREFNEienasSSLGSDLAAREDALNQSLKELMHQAR--TVLKARTEAHFNN 766
|
...
gi 488310544 620 GQR 622
Cdd:TIGR00618 767 NEE 769
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
470-627 |
5.52e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERR-----------KQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELkpr 538
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREederileylkeKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL--- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 539 pqhkapnAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESL--KKINDQSDESTNLTALRNQN 616
Cdd:pfam13868 211 -------YQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEefERMLRKQAEDEEIEQEEAEK 283
|
170
....*....|.
gi 488310544 617 RRTGQRSKKRE 627
Cdd:pfam13868 284 RRMKRLEHRRE 294
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-582 |
5.82e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 476 AAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRplnkeQEKRSALRRELkprpqhkapNAIEKAQEGLR 555
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALARRI---------RALEQELAALE 82
|
90 100
....*....|....*....|....*..
gi 488310544 556 QAHEKGRMQEQKSEEQLKRQQHESARQ 582
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAEL 109
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
470-595 |
5.82e-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: 41.21 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAEtglKQRPLNKEQEKRSALRRELKPRPQHkapnaiEK 549
Cdd:pfam11600 12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEE---ARRKKEEEKELKEKERREKKEKDEK------EK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488310544 550 AqEGLRQAHEKGRMQEQKSEEQL--KRQQHESARQKEyEKDRLKKQES 595
Cdd:pfam11600 83 A-EKLRLKEEKRKEKQEALEAKLeeKRKKEEEKRLKE-EEKRIKAEKA 128
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
474-678 |
6.50e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKER--RKQAQEERKAAIKKRQEEARKHGKAETGL---KQRPLNKEQEKRSALRRELKPRPQHKAPNAIE 548
Cdd:PRK07735 12 KEAARRAKEEARKRlvAKHGAEISKLEEENREKEKALPKNDDMTIeeaKRRAAAAAKAKAAALAKQKREGTEEVTEEEKA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 549 KAQeglrqahekgrmqeQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTGQRSKKRET 628
Cdd:PRK07735 92 KAK--------------AKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488310544 629 GHQTLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAA 678
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
456-622 |
8.39e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 456 LSDGVGFIGNPFGTEAnmRRAAREQKQENKERRKQAQEERKaaiKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRREL 535
Cdd:PRK10811 569 LSRFFGALKALFSGGE--ETKPQEQPAPKAEAKPERQQDRR---KPRQNNRRDRNERRDTRDNRTRREGRENREENRRNR 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 536 KPRPQHKAPNAIEKAQEGLRQAHEKGRMQ-EQKSEEQLKRQqhESARQKEYEKDRLKKQESLKKINDQSDESTNLTAlRN 614
Cdd:PRK10811 644 RQAQQQTAETRESQQAEVTEKARTQDEQQqAPRRERQRRRN--DEKRQAQQEAKALNVEEQSVQETEQEERVQQVQP-RR 720
|
....*...
gi 488310544 615 QNRRTGQR 622
Cdd:PRK10811 721 KQRQLNQK 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-684 |
8.87e-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: 43.12 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKhgkaetglKQRplNKEQEKRSALRRELKPRPQH-------- 541
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK--------ELE--ELEEELEQLRKELEELSRQIsalrkdla 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 542 KAPNAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQ-SDESTNLTALRNQNRRTG 620
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREALDELRAELTLLN 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488310544 621 ---QRSKKRETGHQTLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQTVKRS 684
Cdd:TIGR02168 817 eeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
470-662 |
1.12e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREqKQENKERRKQAQEERKA-------------AIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELK 536
Cdd:PRK05035 456 EARQARLERE-KAAREARHKKAAEARAAkdkdavaaalarvKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 537 PRPQHKAPNAIEKA--QEGLRQAHEKGRMQEQKSEEQLKRQQHESAR-QKEYEKDRLKKQESLKKINDQSDESTNLTALR 613
Cdd:PRK05035 535 AEKQAAAAADPKKAavAAAIARAKAKKAAQQAANAEAEEEVDPKKAAvAAAIARAKAKKAAQQAASAEPEEQVAEVDPKK 614
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488310544 614 NQNRRTGQRSKKRETGHQTLMkrqgekvlqPTNKPKDMKKQVVARSPRR 662
Cdd:PRK05035 615 AAVAAAIARAKAKKAEQQANA---------EPEEPVDPRKAAVAAAIAR 654
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
465-712 |
1.26e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 465 NPFGTEANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKhgkaetglKQRPLNKEQEKRSA--LRRELKPRPQHK 542
Cdd:PTZ00121 1073 KPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARK--------AEEAKKKAEDARKAeeARKAEDARKAEE 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 543 APNAIE-KAQEGLRQAHEKGRMQEQKSEEQLKRQqhESARQKE--YEKDRLKKQESLKKINDqsdestnltALRNQNRRT 619
Cdd:PTZ00121 1145 ARKAEDaKRVEIARKAEDARKAEEARKAEDAKKA--EAARKAEevRKAEELRKAEDARKAEA---------ARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 620 GQRSKKRETGHQTLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQPKVAAQT-VKRSGGTLGSNPAYRRPE 698
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAeEARKADELKKAEEKKKAD 1293
|
250
....*....|....
gi 488310544 699 VRKKMDQVKQVTQV 712
Cdd:PTZ00121 1294 EAKKAEEKKKADEA 1307
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
490-601 |
1.87e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 39.71 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 490 QAQEERKAAIKKRQEEARKHGKaetglkqrpLNKEQEKRSALRRELKPRPQHKAPNA-IEKAQEGLRQAHEKGRMQEQKS 568
Cdd:smart01071 39 QARVERMEEIKNLKYELIMNDH---------LNKRIDKLLKGLREEELSPETPTYNEmLAELQDQLKKELEEANGDSEGL 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 488310544 569 EEQLKRQQHE-SARQKEYEK--DRLKKQESLKKIND 601
Cdd:smart01071 110 LEELKKHRDKlKKEQKELRKklDELEKEEKKKIWSV 145
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
477-667 |
2.10e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.57 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 477 AREQKQENKERR---KQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKR--SALRRELKPRPQHKAPNAIEKAQ 551
Cdd:PTZ00108 1146 EVEEKEIAKEQRlksKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRvdSDEKRKLDDKPDNKKSNSSGSDQ 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 EGLRQAHEKG------RMQEQKSEEQLKRQQHESARQKEYEKDRLKK---------QESLKKINDQSDESTNLTALRNQN 616
Cdd:PTZ00108 1226 EDDEEQKTKPkkssvkRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKnapkrvsavQYSPPPPSKRPDGESNGGSKPSSP 1305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488310544 617 RRTGQRSKKRETGHQTLMKRQGEKVLQPTNKPKDMKKQVVARSPRRTGQPT 667
Cdd:PTZ00108 1306 TKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRP 1356
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
479-599 |
2.14e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 479 EQKQENKERRKQAQEERkaAIKKRQEEARKHGKAEtglKQRPLNKEQEKRSALRRELKPRPQHKAPNAIekaqeglrqah 558
Cdd:pfam15709 326 EKREQEKASRDRLRAER--AEMRRLEVERKRREQE---EQRRLQQEQLERAEKMREELELEQQRRFEEI----------- 389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488310544 559 ekgRMQEQKSEEQLKRQQHESARQK-----EYEKDRLKKQESLKKI 599
Cdd:pfam15709 390 ---RLRKQRLEEERQRQEEEERKQRlqlqaAQERARQQQEEFRRKL 432
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
476-644 |
2.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 476 AAREQKQENKERRKQAQeeRKAAIKKRQEEARK----HGKAETGLKQrpLNKEQEKRSALRRELkPRPQHKAPNAIEKAQ 551
Cdd:COG3096 496 TARELLRRYRSQQALAQ--RLQQLRAQLAELEQrlrqQQNAERLLEE--FCQRIGQQLDAAEEL-EELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 552 EGLRQAHEKgRMQEQKSEEQLKRQQHESARQkeyEKDRLKKQESLKKINDQSDE----STNLTALRNQ---NRRTGQRSK 624
Cdd:COG3096 571 EQAAEAVEQ-RSELRQQLEQLRARIKELAAR---APAWLAAQDALERLREQSGEaladSQEVTAAMQQlleREREATVER 646
|
170 180
....*....|....*....|
gi 488310544 625 KRETGHQTLMKRQGEKVLQP 644
Cdd:COG3096 647 DELAARKQALESQIERLSQP 666
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
545-602 |
2.21e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 2.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488310544 545 NAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQ-HESARQKEYEKDRLKKQESLKKINDQ 602
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAEEA 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
469-627 |
2.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 469 TEANMRRAAREQkqenkerRKQAQEERKAAIKKRQEEARKHGKAETGLKQRpLNKEQEKRSALRR---ELKPRPQHKApN 545
Cdd:COG1196 260 AELAELEAELEE-------LRLELEELELELEEAQAEEYELLAELARLEQD-IARLEERRRELEErleELEEELAELE-E 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 546 AIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKIN-DQSDESTNLTALRNQNRRTGQRSK 624
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeELLEALRAAAELAAQLEELEEAEE 410
|
...
gi 488310544 625 KRE 627
Cdd:COG1196 411 ALL 413
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
481-598 |
2.52e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 481 KQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELkprpQHKAPNAIEKAQEGLRQAHEK 560
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488310544 561 GRMQEQ----KSEEQLKRQQhESARQKEYEKDRLKKQESLKK 598
Cdd:PRK09510 138 AAKAAAaakaKAEAEAKRAA-AAAKKAAAEAKKKAEAEAAKK 178
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
474-636 |
3.23e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENK-----------ERRKQAQEERKAAIKKRQEEARKhgKAETGLKqrplNKEQekrsalrrelkprpqhk 542
Cdd:pfam05262 247 RDEVRQKQQEAKnlpkpadtsspKEDKQVAENQKREIEKAQIEIKK--NDEEALK----AKDH----------------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 543 apnaieKAQEGLRQAHEKGRMQEQKSEE-QLKRQQHESARQKEYEKDRLKK----QESLKKIN-----DQSDESTNLTAL 612
Cdd:pfam05262 304 ------KAFDLKQESKASEKEAEDKELEaQKKREPVAEDLQKTKPQVEAQPtslnEDAIDSSNpvyglKVVDPITNLSEL 377
|
170 180
....*....|....*....|....
gi 488310544 613 RNQNRRTGQRskKRETGHQTLMKR 636
Cdd:pfam05262 378 VLIDLKTEVR--LRESAQQTIRRR 399
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
480-627 |
3.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 480 QKQENKERRKQAQEERKAAIKKRQEE--------ARKHGKAETGLKQrpLNKEQEKRSALRRELKPRPQHKApnAIEKAQ 551
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEisselpelREELEKLEKEVKE--LEELKEEIEELEKELESLEGSKR--KLEEKI 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488310544 552 EGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQ-NRRTGQRSKKRE 627
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGiEERIKELEEKEE 338
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
477-602 |
3.97e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.37 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 477 AREQKQENKERRKQAQEERKAAIKK--RQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQEGL 554
Cdd:pfam05262 211 DAKRAQQLKEELDKKQIDADKAQQKadFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEI 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488310544 555 RQ-AHEKGRMQEQKSEE--QLKRQQHESARQKEYE--KDRLKKQESLKKINDQ 602
Cdd:pfam05262 291 KKnDEEALKAKDHKAFDlkQESKASEKEAEDKELEaqKKREPVAEDLQKTKPQ 343
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-597 |
4.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAAREQKQENKERRKQAQEERKAA-IKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKprpqhkapNAIE 548
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE--------LEEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488310544 549 KAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLK 597
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
474-727 |
4.31e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.38 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSA---LRRELKPRPQHKAPNAIEKA 550
Cdd:NF033838 230 REKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSdssVGEETLPSPSLKPEKKVAEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 551 QEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDESTNLTALRNQNRRTgqRSKKRETgh 630
Cdd:NF033838 310 EKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKV--ESKKAEA-- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 631 qTLMkrqgEKVLQPTNKPKDMKKQVVARSPRRTGQPTTRQNIQP-----KVAAQTVKRSGGTLGSNPAYRRPEV---RKK 702
Cdd:NF033838 386 -TRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPapqpeKPAPKPEKPAEQPKAEKPADQQAEEdyaRRS 460
|
250 260
....*....|....*....|....*
gi 488310544 703 MDQVKQVTQVDVPQTHSTPQRVQPK 727
Cdd:NF033838 461 EEEYNRLTQQQPPKTEKPAQPSTPK 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
475-578 |
4.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 475 RAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQ---RPLNKEQEKRSALRRELKPR-PQHKAPNAIEKA 550
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERfAAALGDAVEREL 767
|
90 100
....*....|....*....|....*...
gi 488310544 551 QEGLRQAHEKGRMQEQKSEEQLKRQQHE 578
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
474-615 |
4.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHgkaETGLKQRPLNKEQEKRSALRRELKPRPQHKApnAIEKAQEG 553
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGDRLEQLEREIERLERELE--ERERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488310544 554 LRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQEslkkiNDQSDESTNLTALRNQ 615
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE-----EALAEAEAALRDLRRE 420
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
472-661 |
5.14e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.24 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 472 NMR-RAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKaetglkqrplNKEQEKRSAlRRELK---PRPQHKApNAI 547
Cdd:PRK00106 46 NLRgKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYRE----------EIEQEFKSE-RQELKqieSRLTERA-TSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 548 EKAQEGLRQaheKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQS----------DESTNLTA-----L 612
Cdd:PRK00106 114 DRKDENLSS---KEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSqaeareiilaETENKLTHeiatrI 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488310544 613 RNQNRRTGQRSKK--RETGHQTLMKRQGEKVLQPTNK----PKD-MKKQVVARSPR 661
Cdd:PRK00106 191 REAEREVKDRSDKmaKDLLAQAMQRLAGEYVTEQTITtvhlPDDnMKGRIIGREGR 246
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
474-593 |
5.61e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.59 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEErkaaIKKRQEEARKHGKAETGLKQRpLNKEQEKRSALRRElkprpQHKAPNAIEKAQE- 552
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEE----TKKAQEELEESEETAEELEEE-RRQAEEEAERLEQK-----RQEAEEEKERLEEs 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488310544 553 GLRQAHEKGRMQEQKSEEQLKRQQHESARQ-KEYEKDRLKKQ 593
Cdd:pfam20492 71 AEMEAEEKEQLEAELAEAQEEIARLEEEVErKEEEARRLQEE 112
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
521-781 |
5.76e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 521 LNKEQEKRSALRRELKprpqHKAP--------NAIEKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKK 592
Cdd:PTZ00108 1107 LNAELEKKEKELEKLK----NTTPkdmwledlDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKK 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 593 QESLKKINDQSDESTNLTAlrNQNRRTGQRSKKRETGHQTLMKRQGEkvlQPTNKPKDMKKQVVARSPRRTGQPTTRQNI 672
Cdd:PTZ00108 1183 KSSADKSKKASVVGNSKRV--DSDEKRKLDDKPDNKKSNSSGSDQED---DEEQKTKPKKSSVKRLKSKKNNSSKSSEDN 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 673 QPKVAAQTVKRSGGTLGSNPAYRRPEVRKKMDQVKQVTQVDVPQTHSTPQRVQPKVNEPitrmnrhnTPIIKKEKRTKQS 752
Cdd:PTZ00108 1258 DEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEG--------SLAALKKKKKSEK 1329
|
250 260
....*....|....*....|....*....
gi 488310544 753 PVVRRERKKpgTQKITNKPKGVRQPRARK 781
Cdd:PTZ00108 1330 KTARKKKSK--TRVKQASASQSSRLLRRP 1356
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
469-612 |
5.80e-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: 40.43 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 469 TEANMRRAAREQKQENKERRKQAQE-ERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKapNAI 547
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL--AQL 927
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488310544 548 EKAQEGLRQahEKGRMQEQKSEEQLKRQQHESARQKEYEKDRLKKQESLKKINDQSDE--STNLTAL 612
Cdd:TIGR02168 928 ELRLEGLEV--RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAAI 992
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-643 |
6.20e-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: 40.04 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 480 QKQENKERRKQAQEERKAAIKKRQEEArkhgkaetglkQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQEGLRQAHE 559
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEEL-----------EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 560 KGRMQEQKSEEQLKRQQHESARQKEyekDRLKKQESL---------KKINDQSDESTNLTALRNQNRRTGQRSKKRETGH 630
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKV---AQLELQIASlnneierleARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
170
....*....|...
gi 488310544 631 QTLMKRQGEKVLQ 643
Cdd:TIGR02168 441 ELEELEEELEELQ 453
|
|
| NinG |
pfam05766 |
Bacteriophage Lambda NinG protein; NinG or Rap is involved in recombination. Rap ... |
464-523 |
6.39e-03 |
|
Bacteriophage Lambda NinG protein; NinG or Rap is involved in recombination. Rap (recombination adept with plasmid) increases lambda-by-plasmid recombination catalyzed by Escherichia coli's RecBCD pathway.
Pssm-ID: 428621 Cd Length: 195 Bit Score: 38.70 E-value: 6.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 464 GNPFGTEANMRRAAREQKQEnKERRKQAQEERkAAIKKRQEEARKHGKAEtGLKQRPLNK 523
Cdd:pfam05766 31 ASAVGKEQALKKRAAERKAE-KKRRKREQKER-AALRIRKLALKPRSEWE-KDLQKAVNK 87
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
474-599 |
6.45e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.85 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 474 RRAAREQKQENKERRKQAQEERKAAIKkrQEEARKHGKAETGLKQRPLNKEQEKR------SALRRELKPRPQHKAPNAI 547
Cdd:pfam02029 173 NFAKEEVKDEKIKKEKKVKYESKVFLD--QKRGHPEVKSQNGEEEVTKLKVTTKRrqgglsQSQEREEEAEVFLEAEQKL 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488310544 548 EKA----QEGLRQAHEKGRMQEQKSE---EQLKRQQHESARQKEYEKDRLKKQESLKKI 599
Cdd:pfam02029 251 EELrrrrQEKESEEFEKLRQKQQEAElelEELKKKREERRKLLEEEEQRRKQEEAERKL 309
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-575 |
8.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 467 FGTEANMRRAAREQKQENKERRKQAQEERKAAIKKRQEEARKHGKAETGLKQRPLNKEQEKRSALRRELKPRPQHKAPNA 546
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110
....*....|....*....|....*....|
gi 488310544 547 IEKAQEGLRQAHEKGRMQEQKSE-EQLKRQ 575
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERElERLERE 775
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-599 |
8.85e-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: 37.71 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 486 ERRKQAQEErkaaikKRQEEARKHGKAETG--LKQRPLNKEQEKRSALRRELKPRPQHKAPNAIEKAQEGLRQAHEKgRM 563
Cdd:pfam05672 18 EKRRQAREQ------REREEQERLEKEEEErlRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER-EQ 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 488310544 564 QEQKSEEQLKRQQHESAR--QKEYEKDRLKKQESLKKI 599
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAkaREEAERQRQEREKIMQQE 128
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
470-601 |
8.89e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.13 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 470 EANMRRAARE---QKQENKERRKQAQEERKAAIKKRQEEARKHGKAEtglKQRPLNK-----EQEKRSALRRELKpRPQH 541
Cdd:pfam13868 216 ERKERQKEREeaeKKARQRQELQQAREEQIELKERRLAEEAEREEEE---FERMLRKqaedeEIEQEEAEKRRMK-RLEH 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488310544 542 KapnaieKAQEGLRQAHEKGRMQEQKSEEQLKRQQHESARQkeyEKDRLkKQESLKKIND 601
Cdd:pfam13868 292 R------RELEKQIEEREEQRAAEREEELEEGERLREEEAE---RRERI-EEERQKKLKE 341
|
|
| |
