|
Name |
Accession |
Description |
Interval |
E-value |
| INCENP_N |
pfam12178 |
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ... |
6-41 |
8.37e-17 |
|
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.
Pssm-ID: 463484 [Multi-domain] Cd Length: 36 Bit Score: 74.66 E-value: 8.37e-17
10 20 30
....*....|....*....|....*....|....*.
gi 767968086 6 PGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEA 41
Cdd:pfam12178 1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
|
|
| INCENP_ARK-bind |
pfam03941 |
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ... |
838-892 |
3.50e-15 |
|
Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.
Pssm-ID: 461100 [Multi-domain] Cd Length: 53 Bit Score: 70.30 E-value: 3.50e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 767968086 838 NSDDSTDDEAHPRKPIPTWARGTPLSQAIIHQYyhPPNLLELFGTILPLDLEDIF 892
Cdd:pfam03941 1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-781 |
1.28e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRK-EEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK--------EEKKKQIEQKFAQ 601
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadeakkaEEAKKADEAKKAE 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 602 IDEKTE---KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARR---------LRWLQQVRAQEEEERRHQELLQK--- 666
Cdd:PTZ00121 1532 EAKKADeakKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKaee 1611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 667 -KKEEEQ----ERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQERE 741
Cdd:PTZ00121 1612 aKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767968086 742 KALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAK 781
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-788 |
2.33e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEK 608
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 609 AKEERlaeekakKKAAAKKMEEVEARRKQEEEARRLRwlqqvraqeeeerrhqellQKKKEEEQERlRKAAEAKRLAEQR 688
Cdd:PTZ00121 1649 AEELK-------KAEEENKIKAAEEAKKAEEDKKKAE-------------------EAKKAEEDEK-KAAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 689 EQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLA 768
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250 260
....*....|....*....|
gi 767968086 769 ERQLQEEQEKKAKEAAGASK 788
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
532-790 |
2.38e-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: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 532 EKERQrLENLRRkeEAEQLRR-QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 610
Cdd:COG1196 197 ELERQ-LEPLER--QAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 611 EERLAEEKAKKKAAAKKMEEVEA--------RRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAK 682
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAElarleqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 683 RLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKE 762
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260
....*....|....*....|....*...
gi 767968086 763 EQQRLAERQLQEEQEKKAKEAAGASKAL 790
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-789 |
2.67e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEqmkeEKKKQIEQKFAQIDEKTEKAK 610
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE----EAKKAAEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 611 EERLAEEKAKKKAAAKKMEEVEARRKQEEEarrlRWLQQVRAQEEEERRHQELLQKKKEEEqerlRKAAEAKRLAEQREQ 690
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAK----KKADEAKKKAEEKKK 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 691 ERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQK--EQLQRELEEKKKKEEQQRLA 768
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKA 1512
|
250 260
....*....|....*....|.
gi 767968086 769 ERQLQEEQEKKAKEAAGASKA 789
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEA 1533
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
531-787 |
3.18e-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: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfaQIDEKTEKAK 610
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 611 EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQ 690
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 691 ERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAER 770
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250
....*....|....*..
gi 767968086 771 QLQEEQEKKAKEAAGAS 787
Cdd:COG1196 482 LLEELAEAAARLLLLLE 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-790 |
3.78e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQIEQKFAQ 601
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 602 IDEKTEKAKEERLAEEKAKKKAAA----KKME----EVEARRKQEEEARRLRWLQQVRAQEEEERRhqellQKKKEEEQE 673
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-----ELKKAEEEN 1659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 674 RLRKAAEAKRlAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAErELQEREKALRLQKEQLQR 753
Cdd:PTZ00121 1660 KIKAAEEAKK-AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKK 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767968086 754 ELEEKKKKEEQQRLAE------RQLQEEQEKKAKEAAGASKAL 790
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-683 |
4.88e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 521 KRNTPLRMDPKEKERQRLENLRRKEE----AEQLRRqkvEEDKRRRLEEVKLKREERLRKVLQARERVEQMK----EEKK 592
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKK---AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaEEAK 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 593 KQIEQKfaQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLrwlQQVRAQEEEERRHQELLQKKKEEEQ 672
Cdd:PTZ00121 1669 KAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA---EELKKAEEENKIKAEEAKKEAEEDK 1743
|
170
....*....|.
gi 767968086 673 erlRKAAEAKR 683
Cdd:PTZ00121 1744 ---KKAEEAKK 1751
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-789 |
6.02e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 532 EKERQRLENLRRKEEAEQLRRQ-KVEEDKRRRLEEVKLKREERlRKVLQARERVEQMK--EEKKKQIEQKfAQIDEKTEK 608
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKkaEEAKKKAEEA-KKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 609 AKEERlAEEKAKKKAAAKKMEEVEARRKQE-----------EEARRLRWLQQVRAQEEEERRHQELLQKKKEE--EQERL 675
Cdd:PTZ00121 1479 AEEAK-KADEAKKKAEEAKKKADEAKKAAEakkkadeakkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 676 RKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQerlQAERELQEREKALRLQKEQLQREL 755
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKKAEEAKIKAEELKKAEEEKKK 1634
|
250 260 270
....*....|....*....|....*....|....*.
gi 767968086 756 EEKKKKEEQQ--RLAERQLQEEQEKKAKEAAGASKA 789
Cdd:PTZ00121 1635 VEQLKKKEAEekKKAEELKKAEEENKIKAAEEAKKA 1670
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-789 |
5.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVK----LKREERLRKVLQAR--------ERVEQMKEEKKK 593
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKkaeaaRKAEEVRkaeeLRKAEDARKAEAARkaeeerkaEEARKAEDAKKA 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 594 QIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEeeerrhqellQKKKEEE-- 671
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE----------EKKKADEak 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 672 -QERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERElQEREKALRLQKEQ 750
Cdd:PTZ00121 1297 kAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA-EEKAEAAEKKKEE 1375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767968086 751 LQRELEEKKKKEEQQRLAE--RQLQEEQEKKAKEAAGASKA 789
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADeaKKKAEEDKKKADELKKAAAA 1416
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
527-791 |
6.00e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 606
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 607 EKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAE 686
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 687 QREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKE-QLQRELEEKKKKEEQQ 765
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEA 542
|
250 260
....*....|....*....|....*...
gi 767968086 766 RLAER--QLQEEQEKKAKEAAGASKALN 791
Cdd:COG1196 543 ALAAAlqNIVVEDDEVAAAAIEYLKAAK 570
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-789 |
6.83e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREER----------LRKVLQARERVEQMKEEKKKQIEQKFA 600
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERnneeirkfeeARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 601 QIDEKTEKAKE-ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAA 679
Cdd:PTZ00121 1287 EEKKKADEAKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 680 EAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAErELQEREKALRLQKEQLQRELEEKK 759
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKK 1445
|
250 260 270
....*....|....*....|....*....|
gi 767968086 760 KKEEQQRLAERQLQEEQEKKAKEAAGASKA 789
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
520-682 |
7.31e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 520 IKRNTPLRMDPKEKERQRLENLRRKEEAEQLR----RQKVEEDKR-----RRLEEVKLKREERLRKVLQARERVEQMKee 590
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaaeeAKKAEEDKKkaeeaKKAEEDEKKAAEALKKEAEEAKKAEELK-- 1708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 591 KKKQIEQKFAqidEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWL--QQVRAQEEEERRHQELLQKKK 668
Cdd:PTZ00121 1709 KKEAEEKKKA---EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkkEEEKKAEEIRKEKEAVIEEEL 1785
|
170
....*....|....
gi 767968086 669 EEEQERLRKAAEAK 682
Cdd:PTZ00121 1786 DEEDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-782 |
1.32e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEE----AEQLRRqKVEEDKRRRlEEVKlKREERLRKVLQARERVEQMK--EEKKKQIEQKfAQIDE 604
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEekkkADEAKK-KAEEDKKKA-DELK-KAAAAKKKADEAKKKAEEKKkaDEAKKKAEEA-KKADE 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 605 KTEKAKEERlaeEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQV--RAQEEEERRHQELLQKKKEEE---QERLRKAA 679
Cdd:PTZ00121 1449 AKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEakkAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 680 EAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKK 759
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
250 260
....*....|....*....|....*
gi 767968086 760 KKEEQQ--RLAERQLQEEQEKKAKE 782
Cdd:PTZ00121 1606 KMKAEEakKAEEAKIKAEELKKAEE 1630
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-783 |
1.84e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVklKREERLRKVLQARERVEQMKEEKKKQIEQkfAQIDEK 605
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDARkaeeaRKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEA--ARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 606 TEKAKEERlaeeKAKKKAAAKKMEEVEARRKQEEEARR---LRWLQQVRAQEEEERRHQELLQKKKEEEQErlRKAAEAK 682
Cdd:PTZ00121 1211 ERKAEEAR----KAEDAKKAEAVKKAEEAKKDAEEAKKaeeERNNEEIRKFEEARMAHFARRQAAIKAEEA--RKADELK 1284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 683 RlAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKE 762
Cdd:PTZ00121 1285 K-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
250 260
....*....|....*....|.
gi 767968086 763 EQQRLAERQlQEEQEKKAKEA 783
Cdd:PTZ00121 1364 EKAEAAEKK-KEEAKKKADAA 1383
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
522-784 |
3.17e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 522 RNTPLRMDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQ 601
Cdd:pfam02463 196 KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 602 IDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEA 681
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 682 KRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKK 761
Cdd:pfam02463 356 EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260
....*....|....*....|...
gi 767968086 762 EEQQRLAERQLQEEQEKKAKEAA 784
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQEL 458
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
531-790 |
3.99e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEE--AEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEK 608
Cdd:pfam02463 168 KRKKKEALKKLIEETEnlAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 609 AKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRL---------RWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAA 679
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 680 EAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERElqEREKALRLQKEQLQRELEEKK 759
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE--RLSSAAKLKEEELELKSEEEK 405
|
250 260 270
....*....|....*....|....*....|.
gi 767968086 760 KKEEQQRLAERQLQEEQEKKAKEAAGASKAL 790
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
539-790 |
1.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 539 ENLRRKEEAEQLRRQKVEEDkrRRLEEVKlKREERLRKVLQARERVEQMK-EEKKKQIEQKFAQIDEKTEKAKEERLAEE 617
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEA--RKAEEAK-KKAEDARKAEEARKAEDARKaEEARKAEDAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 618 KAKKKAAAKKMEEVEARRKQEeearrLRWLQQVRAQEEEerrhqellqKKKEEEQ--ERLRKAAEAKRL-AEQREQERRE 694
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEE-----LRKAEDARKAEAA---------RKAEEERkaEEARKAEDAKKAeAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 695 QERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQK-EQLQRELEEKKKKEEQQRLAERQLQ 773
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKaDEAKKAEEKKKADEAKKKAEEAKKA 1317
|
250
....*....|....*..
gi 767968086 774 EEQEKKAKEAAGASKAL 790
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAA 1334
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
530-685 |
6.28e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.42 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 530 PKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERlrkvLQARERVEQMKEEKKKQIEQKFAQIDektekA 609
Cdd:PRK09510 81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA----KQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968086 610 KEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLA 685
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
531-782 |
6.69e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQK--VEEDKRRRLEEVKLKRE---ERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEK 605
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEiaMEISRMRELERLQMERQqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 606 TEKAKEERlaeekakkkaaakkmeEVEARRKQEEEARRlrwLQQVRAQEEEERRHQELLqkkKEEEQERLRKAAEAKRLA 685
Cdd:pfam17380 426 RAEQEEAR----------------QREVRRLEEERARE---MERVRLEEQERQQQVERL---RQQEEERKRKKLELEKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 686 EQREQERREQERREQERREQERREQERREQERQLaeqerrreqerlqAERELQEREKALRLQKEQLQREleekKKKEEQQ 765
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-------------LEKEMEERQKAIYEEERRREAE----EERRKQQ 546
|
250
....*....|....*..
gi 767968086 766 RLAERQLQEEQEKKAKE 782
Cdd:pfam17380 547 EMEERRRIQEQMRKATE 563
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-789 |
1.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAeqlrRQKVEEDKR----------RRLEEVKLKREERLRKVLQARE--RVEQMK--EEKKKQIE 596
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEA----KKDAEEAKKaeeernneeiRKFEEARMAHFARRQAAIKAEEarKADELKkaEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 597 QKFAQ----IDEKTEKAKEERlaEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQE-----EEERRHQELLQKK 667
Cdd:PTZ00121 1295 AKKAEekkkADEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadeaEAAEEKAEAAEKK 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 668 KEEEQ---ERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREqerqlAEQERRREQERLQAERELQEREKAL 744
Cdd:PTZ00121 1373 KEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-----AKKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767968086 745 RLQKEQLQREleekKKKEEQQRLAERQLQEEQEKKAKEAAGASKA 789
Cdd:PTZ00121 1448 EAKKKAEEAK----KAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
531-611 |
1.50e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQ-RLENLRRKEEAEQLRRQKveEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 609
Cdd:PRK12704 56 KEALLEaKEEIHKLRNEFEKELRER--RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
..
gi 767968086 610 KE 611
Cdd:PRK12704 134 EE 135
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
531-790 |
2.86e-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: 47.22 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQK------------ 598
Cdd:pfam13868 59 EEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRqlreeidefnee 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 599 ---FAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERL 675
Cdd:pfam13868 139 qaeWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 676 RKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREkalRLQKEQLQREL 755
Cdd:pfam13868 219 ERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR---RMKRLEHRREL 295
|
250 260 270
....*....|....*....|....*....|....*
gi 767968086 756 EEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKAL 790
Cdd:pfam13868 296 EKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
542-790 |
5.85e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 542 RRKEEAEQLRRQKVEEDKRRRLEEvklKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKK 621
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 622 KAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERREQE 701
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 702 RREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAK 781
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
....*....
gi 767968086 782 EAAGASKAL 790
Cdd:pfam02463 391 KLKEEELEL 399
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
538-684 |
6.06e-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: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 538 LENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEE 617
Cdd:pfam15709 325 LEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQE 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968086 618 KAKKKAAAKKMEEVE-ARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEE-----EQERLRKAAEAKRL 684
Cdd:pfam15709 405 EEERKQRLQLQAAQErARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEmqlaeEQKRLMEMAEEERL 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
531-788 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEvklKREERLRKVLQARERVEQMKEEKKKQIEQkfAQIDEKTEKAK 610
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA---KRVEIARKAEDARKAEEARKAEDAKKAEA--ARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 611 EERLAE--EKAKKKAAAKKMEEVEARRKQEEEAR--RLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAE 686
Cdd:PTZ00121 1192 ELRKAEdaRKAEAARKAEEERKAEEARKAEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 687 QREQERREQERREQERREQERREQERREQERQLAeqerrreqerlQAERELQEREKALRLQK--EQLQRELEEKKKKEEQ 764
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-----------EAKKKAEEAKKADEAKKkaEEAKKKADAAKKKAEE 1340
|
250 260
....*....|....*....|....
gi 767968086 765 QRLAERQLQEEQEKKAKEAAGASK 788
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEE 1364
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
531-798 |
1.24e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 610
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 611 EERLaeekakkkaaakkmEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQ 690
Cdd:COG1196 453 ELEE--------------EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 691 ERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAER 770
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
250 260
....*....|....*....|....*...
gi 767968086 771 QLQEEQEKKAKEAAGASKALNVTVDVQV 798
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRT 626
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
542-685 |
1.45e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 542 RRKEEaeqlRRQKVEEDKRRRLEEVKLKREERLRKVLQARErveQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKK 621
Cdd:PRK09510 75 KRAEE----QRKKKEQQQAEELQQKQAAEQERLKQLEKERL---AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968086 622 KAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLA 685
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA 211
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
526-644 |
1.67e-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: 45.33 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 526 LRMDPKEKERQRLENLRRKEeaeQLRRQKVEEDKRRRLEEVKLKREERLRKVLQ-ARERVEQMKEEKKKQIEQKFAQIDE 604
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQELQRKKQQeEAERAEAEKQRQKELEMQLAEEQKR 467
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767968086 605 KTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRL 644
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
521-685 |
1.97e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 521 KRNTPLRMDPKEKERQRLENLRRkeEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERveqmKEEKKKQIEQKFA 600
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ--QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ----AEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 601 QiDEKTEKAKEErlaeekakkkAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAE 680
Cdd:TIGR02794 127 K-QAAEAKAKAE----------AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
....*
gi 767968086 681 AKRLA 685
Cdd:TIGR02794 196 AKAEA 200
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
429-682 |
3.81e-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: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 429 QQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQhLEDEELQPPRSKTPSSPCPASKVVRPLRTFLHTVQRNQMLMTP 508
Cdd:pfam17380 319 EEAEKARQAEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 509 TSAPRSVMKSFIKRNTPLRMDPKEKERQRLEnlrrKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVlqarERVEQMK 588
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAE----QEEARQREVRRLEEERAREMERVRLEEQERQQQV----ERLRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 589 EEKKKQIEQKFAQiDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRK---QEEEARRLRWLQQVRAQEEEERRHQELLQ 665
Cdd:pfam17380 470 EERKRKKLELEKE-KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlleKEMEERQKAIYEEERRREAEEERRKQQEM 548
|
250
....*....|....*..
gi 767968086 666 KKKEEEQERLRKAAEAK 682
Cdd:pfam17380 549 EERRRIQEQMRKATEER 565
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
543-789 |
4.12e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 543 RKEEAEQLRRQKVE-EDKRRRLEEVKLKREERLRK------------VLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 609
Cdd:PRK05035 441 IEQEKKKAEEAKARfEARQARLEREKAAREARHKKaaearaakdkdaVAAALARVKAKKAAATQPIVIKAGARPDNSAVI 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 610 KEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERrhqellqkkKEEEQERLRKAAEAKRLAEQRE 689
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---------EAEEEVDPKKAAVAAAIARAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 690 QERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKalrlqKEQLQRELEEKK-KKEEQQRLA 768
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPR-----KAAVAAAIARAKaRKAAQQQAN 666
|
250 260
....*....|....*....|.
gi 767968086 769 ERQLQEEQEKKAKEAAGASKA 789
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARA 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
531-784 |
5.30e-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: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK------EEKKKQIEQKFAQIDE 604
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkeltelEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 605 KTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLR--------WLQQVRAQEEEERRHQELLQKKKEEEQERLR 676
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 677 KAAEA-KRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKAL---RLQKEQLQ 752
Cdd:TIGR02168 856 SLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLE 935
|
250 260 270
....*....|....*....|....*....|..
gi 767968086 753 RELeekkkKEEQQRLAERQLQEEQEKKAKEAA 784
Cdd:TIGR02168 936 VRI-----DNLQERLSEEYSLTLEEAEALENK 962
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
531-652 |
6.46e-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: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLEN-LRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLR--KVLQARERVEQMKEEKKKQIEQKFA-----QI 602
Cdd:pfam13868 220 RQKEREEAEKkARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRrelekQI 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767968086 603 DEKTEKAKEERLAEEKakkkaaakkmeevEARRKQEEEARRLRWLQQVRA 652
Cdd:pfam13868 300 EEREEQRAAEREEELE-------------EGERLREEEAERRERIEEERQ 336
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
526-781 |
7.91e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 526 LRMDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEV---KLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQI 602
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREkteKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 603 DEK---TEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKK--KEEEQERLRK 677
Cdd:pfam02463 821 QLLieqEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELesKEEKEKEEKK 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 678 AAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLqaeRELQEREKALRLQKEQLQRE--- 754
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---KEEEEERNKRLLLAKEELGKvnl 977
|
250 260
....*....|....*....|....*....
gi 767968086 755 --LEEKKKKEEQQRLAERQLQEEQEKKAK 781
Cdd:pfam02463 978 maIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
532-680 |
8.80e-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: 43.13 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 532 EKERQRLENLRRKEEAEQLRR----------QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQ 601
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRdklteeyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 602 IDEKTEkaKEERLAEEKAKKKAAAKKMEEVEARRKQ-EEEARRLRW-LQQVRAQEEEERRHQELLQKKKEEEQERLRKAA 679
Cdd:TIGR02169 412 QEELQR--LSEELADLNAAIAGIEAKINELEEEKEDkALEIKKQEWkLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
.
gi 767968086 680 E 680
Cdd:TIGR02169 490 R 490
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
536-643 |
9.99e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 536 QRLENLRRkeEAEQlrrqkveedKRRRLEEvKLKREERLRKVLQAR-ERVEQMKEEKKKQIEQKFAQIdekTEKAKEERL 614
Cdd:PRK00409 523 ASLEELER--ELEQ---------KAEEAEA-LLKEAEKLKEELEEKkEKLQEEEDKLLEEAEKEAQQA---IKEAKKEAD 587
|
90 100
....*....|....*....|....*....
gi 767968086 615 AEEKAKKKAAAKKMEEVeaRRKQEEEARR 643
Cdd:PRK00409 588 EIIKELRQLQKGGYASV--KAHELIEARK 614
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
544-611 |
1.35e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.02 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968086 544 KEEAEQLRRQKVEEDKRRR-----LEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 611
Cdd:pfam12072 59 KEEIHKLRAEAERELKERRnelqrQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEE 131
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
531-612 |
1.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQ---RLENLRRKEEAEQLRRQKVE------EDKRRRLEEVKLKREERLRKVL-----QARERV-EQMKEEKKKQI 595
Cdd:PRK12704 92 LQKEENldrKLELLEKREEELEKKEKELEqkqqelEKKEEELEELIEEQLQELERISgltaeEAKEILlEKVEEEARHEA 171
|
90
....*....|....*..
gi 767968086 596 eqkFAQIDEKTEKAKEE 612
Cdd:PRK12704 172 ---AVLIKEIEEEAKEE 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
545-682 |
1.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 545 EEAEQLRRQKVEEDKRrrleEVKLKREErlrKVLQARERVEQMKEEKKKQIEQKFAQID--EKTEKAKEERLAEEKakkk 622
Cdd:PRK12704 34 KEAEEEAKRILEEAKK----EAEAIKKE---ALLEAKEEIHKLRNEFEKELRERRNELQklEKRLLQKEENLDRKL---- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968086 623 aaakkmeevEARRKQEEEARRLRwlQQVRAQEEEERRHQELLQKKKEEEQERLRKAA-----EAK 682
Cdd:PRK12704 103 ---------ELLEKREEELEKKE--KELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAK 156
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
537-645 |
1.93e-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: 39.13 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 537 RLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVKLKREERLRKVLQARERVEQmkeeKKKQIEQKFAQIDEKTEKAKE 611
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKaqeelEESEETAEELEEERRQAEEEAERLEQ----KRQEAEEEKERLEESAEMEAE 76
|
90 100 110
....*....|....*....|....*....|....
gi 767968086 612 ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLR 645
Cdd:pfam20492 77 EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
527-684 |
2.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLENLRRKEEAEQLRRQKVEEdKRRRLEEVKLKREERLRKVLQARERVEQMKEekKKQIEQKFAQIDEKT 606
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERL 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968086 607 EKAkEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRL 684
Cdd:COG4717 149 EEL-EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
141-287 |
2.04e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 42.00 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 141 PSSPTPESPTMLTK---KPEDNHTQCQLVPVVEIGISERQNAEQHVTQLMSTEPLPRTLSPTPASATAPTSQ----GIPT 213
Cdd:PRK08691 380 PSAQTAEKETAAKKpqpRPEAETAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWEDAPDEAQTAAGTAQtsakSIQT 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968086 214 SDEESTPKK---SKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPG-PRDSPAFPDSPWRERVLAPILP 287
Cdd:PRK08691 460 ASEAETPPEnqvSKNKAADNETDAPLSEVPSENPIQATPNDEAVETETFAHEAPAePFYGYGFPDNDCPPEDGAEIPP 537
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
448-783 |
2.11e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 448 RRKRSYKQAVSELDEEQHLEDEELqpprsktpsspcpaskvVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLR 527
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLEL-----------------EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 528 MDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTE 607
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 608 KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAEAKRLaEQ 687
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL-ED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 688 REQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKAlRLQKEQLQRELEEKKKKEEQQRL 767
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK-ETQLVKLQEQLELLLSRQKLEER 498
|
330
....*....|....*.
gi 767968086 768 AERQLQEEQEKKAKEA 783
Cdd:pfam02463 499 SQKESKARSGLKVLLA 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
527-782 |
2.24e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 606
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 607 EKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKE--EEQERLRKAAEAKRL 684
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEllEEEQLLIEQEEKIKE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 685 AEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQ 764
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
250
....*....|....*...
gi 767968086 765 QRLAERQLQEEQEKKAKE 782
Cdd:pfam02463 913 EEKENEIEERIKEEAEIL 930
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
527-683 |
2.40e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLENLRRKEEAEQlRRQKVEEDKRrrlEEVKLKREERLRKVLQarervEQMKEEKKKQIEQkfaqidEKT 606
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEER-KRKKLELEKE---KRDRKRAEEQRRKILE-----KELEERKQAMIEE------ERK 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968086 607 EKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELlqkkkEEEQERLRKAAEAKR 683
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM-----EREREMMRQIVESEK 586
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
531-795 |
2.59e-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: 41.58 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEAEQLRRQKVE-EDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 609
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 610 KEERlaeEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEERRHQELLQKKKE---EEQERLRKAAEAKRLAE 686
Cdd:TIGR02168 361 EELE---AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqQEIEELLKKLEEAELKE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 687 QREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQaERELQEREKALRLQKEQLQRE--------LEEK 758
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE-LAQLQARLDSLERLQENLEGFsegvkallKNQS 516
|
250 260 270
....*....|....*....|....*....|....*..
gi 767968086 759 KKKEEQQRLAERQLQEEQEKKAKEAAGASKALNVTVD 795
Cdd:TIGR02168 517 GLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVE 553
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
527-614 |
2.75e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 41.65 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLE--NLRRKE-EAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQID 603
Cdd:PTZ00266 429 RVDKDHAERARIEkeNAHRKAlEMKILEKKRIERLEREERERLERERMERIERERLERERLERERLERDRLERDRLDRLE 508
|
90
....*....|..
gi 767968086 604 -EKTEKAKEERL 614
Cdd:PTZ00266 509 rERVDRLERDRL 520
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
527-613 |
2.83e-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: 39.25 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 527 RMDPKEKERQRLENLRRKEEAEQLRR----QKVEEDKRRRLEEVKLKREERLRKVLQaRERVEQMKEEKKKQIEQKFAQi 602
Cdd:pfam05672 34 RLEKEEEERLRKEELRRRAEEERARReeeaRRLEEERRREEEERQRKAEEEAEEREQ-REQEEQERLQKQKEEAEAKAR- 111
|
90
....*....|.
gi 767968086 603 dEKTEKAKEER 613
Cdd:pfam05672 112 -EEAERQRQER 121
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-791 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 531 KEKERQRLENLRRKEEaeqlRRQKVEEDKRRRLEEVKLKREER-----LRKVLQARERVEQMKEEKK--KQIEQKFAQID 603
Cdd:TIGR02169 172 KEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAeryqaLLKEKREYEGYELLKEKEAleRQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 604 EKtEKAKEERlaeekaKKKAAAKKMEEVEARRKQEEEARRLRWL-----QQVRAQEEEERRHQELLQKKKEEEQERLRKA 678
Cdd:TIGR02169 248 SL-EEELEKL------TEEISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 679 AEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAE----RELQEREKALRLQKEQLQRE 754
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefAETRDELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|....*..
gi 767968086 755 LEEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKALN 791
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
532-784 |
6.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 532 EKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKE---EKKKQIEQKFAQIDEKTEK 608
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaELLEEAALLEAALAELLEE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 609 AKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARR--------LRWLQQVRAQEEEERRHQELLQKKKEEEQERLRKAAE 680
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 681 AKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQER-------EKALRLQKEQLQR 753
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaarlEAALRRAVTLAGR 645
|
250 260 270
....*....|....*....|....*....|.
gi 767968086 754 ELEEKKKKEEQQRLAERQLQEEQEKKAKEAA 784
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
142-513 |
6.34e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 40.28 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 142 SSPTPE------SPTMLTKKPEDNHTqcqlvpvveigisERQNAEQHVTQLMSTEPLPRTLSPTPAsATAPTSQGIPTSD 215
Cdd:pfam05109 474 TSPTPAgttsgaSPVTPSPSPRDNGT-------------ESKAPDMTSPTSAVTTPTPNATSPTPA-VTTPTPNATSPTL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 216 EESTPKKSKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPGPrDSPAFPDSPWRERVLAPILPDNFSTPTG 295
Cdd:pfam05109 540 GKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNA-TSPTVGETSPQANTTNHTLGGTSSTPVV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 296 SrtdsQSVRHSPIAPSSPSPQVLAQKYSLVAKQESVVrraSRRLAKKTAEEPAASGRIICHSYLERLLNVEVPQKVGSEQ 375
Cdd:pfam05109 619 T----SPPKNATSAVTTGQHNITSSSTSSMSLRPSSI---SETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTST 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 376 KEPPEEAEPVAAAEPEVPENNGNNSWPHNDTEIANSTPNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQ 455
Cdd:pfam05109 692 HHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHG 771
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968086 456 AVSELDEEQHLEDEElQPPRSK---TPSSPCPASKVVRPLRTFLH---TVQRNQMLMTPTSAPR 513
Cdd:pfam05109 772 ARTSTEPTTDYGGDS-TTPRTRynaTTYLPPSTSSKLRPRWTFTSppvTTAQATVPVPPTSQPR 834
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
525-682 |
6.87e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 38.92 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 525 PLRMDPKEKERQRLENLRRKEEAE-QLRRQKVEEDKRRRLEEVKL--------------KREERLRKVL---QARERVEQ 586
Cdd:pfam13904 5 WEDMYGGEKQPEEESSKHRVPSLSlDSSSQSSSLTYARKLEGLKLerqpleayenwlaaKQRQRQKELQaqkEEREKEEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 587 MKEEKKKQIEQKFAQ-IDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRL--RWLQQVRAqeeeerrhqeL 663
Cdd:pfam13904 85 EAELRKRLAKEKYQEwLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVlqEWERKKLE----------Q 154
|
170
....*....|....*....
gi 767968086 664 LQKKKEEEQERLRKAAEAK 682
Cdd:pfam13904 155 QQRKREEEQREQLKKEEEE 173
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
544-685 |
7.03e-03 |
|
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: 39.83 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 544 KEEAEQLRRQKVEEDKRRRLEEVKLKREERlrkvlQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKA 623
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQ-----QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968086 624 AAKKMEEVEARRKQEEEARRLRWLQQVRAQEEEErrhqellQKKKEEEQERLRKAAEAKRLA 685
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEE-------EAKAKAAAEAKKKAEEAKKKA 175
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
534-671 |
9.22e-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: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 534 ERQRLENLRRKEEaEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEER 613
Cdd:pfam05672 18 EKRRQAREQRERE-EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767968086 614 LAEEKAKKkaaakkmeevEARRKQEEEARRLRwlqQVRAQEEEERRHQELLQKKKEEE 671
Cdd:pfam05672 97 ERLQKQKE----------EAEAKAREEAERQR---QEREKIMQQEEQERLERKKRIEE 141
|
|
| PRK12585 |
PRK12585 |
putative monovalent cation/H+ antiporter subunit G; Reviewed |
520-613 |
9.34e-03 |
|
putative monovalent cation/H+ antiporter subunit G; Reviewed
Pssm-ID: 183610 Cd Length: 197 Bit Score: 38.51 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968086 520 IKRNTPLRMDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKF 599
Cdd:PRK12585 101 IRIRDQLRSVKKDDIKKKKSLIIRQEQIEKARQEREELEERMEWERREEKIDEREDQEEQEREREEQTIEEQSDDSEHEI 180
|
90
....*....|....
gi 767968086 600 AQIDEKTEKAKEER 613
Cdd:PRK12585 181 IEQDESETESDDDK 194
|
|
| |
