|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-1971 |
0e+00 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 2582.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1 MTLYSFLALVAFYCICKAKRIANPQEAFMDRFDIAKNHINIKWSTNGRLGEGDYKYDIDDGENTDFELSTESMTGTCPDN 80
Cdd:PTZ00121 1 MGLLKFFAFLAFLCICKAKAIANPQEAFMDRFDIAKNHINIKWSNNGIHGEGDFKYDIDDGDNLDFEGNEEEKSGICPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 81 GAQEMYKGSCPDYGKTFVMDLNVDEYNEEFLDEMSFGLLNKKLNLSIEIPVEKSGMAMYQGLFKRCPLDENHSSLIRKEH 160
Cdd:PTZ00121 81 GAEEMYKGGCPDYGKTFLMDFEDDEYNEEFLDEISFGFLNKKLKLPIEIPLEKSGLAMYQGLFKRCPLDEKHSSLIKKEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 161 VYDMCFERIYNRMELTDRNKKRTLRN-NYLHFGWHGLGGRFGSNIDYPLHDYNPSESHVTRKMGFSGLIRNLSDCSIYSY 239
Cdd:PTZ00121 161 EYDMCFEKFYNNMEISDRIKKRGKQNrKYIHFGSHGLGGRFGANIDEPLHDYKNDEHHVTKKMGFPEKIKNLFDCSIYSH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 240 CMGPCFGKDFNNECFRSLPVVFNHRTKECVILGTHEASRRRNCLSQNS-YGFERCFVPMKKEAGKEWTYASSFLRPDYET 318
Cdd:PTZ00121 241 CIGPCFGKDFNNECFLNLPILFNHQTKECVIIGTHEAKRIHNCLSGNSdQGFERCFLPMKKEAGKEWTYASSFIRPDYET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 319 KCPPRFPLNDTVFGYYNHRTGECKSAVKNNRGNYKSTFKNCIEGLFNHPEGDRGNGRNNFLWGVWFLEGSSEK---LSSM 395
Cdd:PTZ00121 321 KCPPRFPLNDTMFGYFNHRTGECESAVKNHEGNYKLSFKKCIEGLFNHIEGDDDNGNNNFLWGVWFIEGNAEEktnLASM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 396 NDIGMCSILREKPNCVLKKEKHYSFTNLTANSFDFAQSVTYPQVEEMHDQENGVSNLGETAWEGREERIDLSEVDGKREE 475
Cdd:PTZ00121 401 DDIGMCSFLKEKPNCVLKKEKHFSFTILTANSFDFAQNIIYPELEEMHDKENGSSLIGEKAPEGREERIDLEENDGKKEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 476 AGSEDKEIKETETYQNLQKNRKTEINEH--MGLSKENLNYMLPVQMRHESTHSN-RNDSIFRRKDEPISQMLELNQPSKS 552
Cdd:PTZ00121 481 AGSEDKEIKEFEIPQNLNKNEKEEINEHevKGLPKENINYILKVHMRFENNHFNiHNDSIFKRKDEPIHKMIELNIPSDN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 553 YLHNLGARGWGRYNISHWNSRRINNGSVSQNEGNMSSKLSKNPQSKFMERFDIPKNHIFINWKKDGEFGEGNLKYDILSN 632
Cdd:PTZ00121 561 KLHNLGAQGIGDSNISHWNSNNINGGSVSQNEGNIGEKLNGNPQQKFMERFDIPKNHIFIEWKKDGEFGEDEFKYDIISN 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 633 KTAGTAQSLLIDNYNDVCPNHSIPGRAQGSCPNYGKAIIVERPENKNEDSNFNYESLNEIHTGYLGRISINVVELPYDKS 712
Cdd:PTZ00121 641 KTAGTAQSLFHDNKDDTCPNHSIEGRAHGSCPNYGKAIIVENLEGEEEDKNFNLEFLNEIHTGYLGKIFIKDVEIPYDKS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 713 GIAMHHGFPASCPIDKQEERLLQRMNDYNYDMCKSRVFPSPLSMKELDYRNRTLKYYGLYGFGGRLGSTISINSRNVGRG 792
Cdd:PTZ00121 721 GIAMHHGFLASCPIDENEEKLFQRKNDYNYDMCKSKIFPNPFSMKELDPKNRLFKYYGLYGFGGRLGANISINKRDKGKE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 793 EKRTNNITLPMKNPGLINNLLDCSIYSYCLGPCMEGTYRNKCFRNLPAYYNHATNECVILGTHEQERNSNCRKETSDLSR 872
Cdd:PTZ00121 801 EKREDNITLPMKNPGLIKNLFDCSIYSYCLGPCLEGSFGNKCFRNLPAYYNHATNECVILGTHEQERNNNCRKEKEDKKK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 873 PNCQKIRKTLDSKDWTYVTSFIRPDYEEKCPPRFPLNSKSFGIYDERTGKCRSLIGEDNYVGIQNFGGCLEYLFINSPKD 952
Cdd:PTZ00121 881 PNCQIIRKTLDSKDWTYVSSFIRPDYEEKCPPRFPLKSKSFGIFDEKTGKCKSLIDEANEVGINKFGGCLEYLFINSPKD 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 953 LYNSDRKKYWGVWIGKEPVNDYNMFRVTGECYHILQKPTCVIHKENHFSFTSLTTNYIDFYQNFNIEPVEELVE------ 1026
Cdd:PTZ00121 961 LYNSDRKKYWGIWAADEPVNDNNIEIANGECYHILQKPTCVIDKENHFSFTALTANTIDFNQNFNIEKIEELTEygnndd 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1027 ---RRDIIDLDKEGNHYGRAEARAQVGQDRGLNPS--DFDFTAKKDSRATEATEEA----KKKAEEAKKKAEEARKAEEA 1097
Cdd:PTZ00121 1041 vlkEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSykDFDFDAKEDNRADEATEEAfgkaEEAKKTETGKAEEARKAEEA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1098 KKKAEEVRKAEEVRKAEEVRKAEEARKAEEDKRKAEEARKA-----EEARKAEEARKAEEARKAEEVRKAEEVRKAEEVR 1172
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1173 KAEEARKAEEVRKAEEVRKAEEARKAEEVRKVEEAKKKAEEARKAEEVR-----------------------KAEEARKA 1229
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERnneeirkfeearmahfarrqaaiKAEEARKA 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1230 EEVRKAEEVRKAEEARKAEEVRKVEEAKKKAEEARKAEEAKKKAEEAKKKAEAAKKKAEEAKKKAEAAKKKAEAAKKKAE 1309
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1310 AAKKKAEAAKKKTEEAKKKAEAAKKKAEEVRKAEEAKKKAEEDKKKAEEVKKAEAAKKKAEEAKKKAEEVRKAEEAKKKA 1389
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1390 EEARKAEEAKKKAEEARKAEEAKKKAEEARKAEEAKKKAEEARKAEEAKKKAEEAKkkaeearkaeeakkkaeearkaee 1469
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK------------------------ 1496
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1470 arkaeearkaeearkaeearkaeevRKAEEVRKAEEV-RKAEEVRKAEEARKAEEdkrkaeearkaeearkaeeARKAEE 1548
Cdd:PTZ00121 1497 -------------------------KKADEAKKAAEAkKKADEAKKAEEAKKADE-------------------AKKAEE 1532
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1549 ARKAEEVRKAEEVRKAEEVRKAEEVRKAEEVRKAEEARKAEEDK----RKAEEARKAEEDKRKAEEARKAE--------- 1615
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmalRKAEEAKKAEEARIEEVMKLYEEekkmkaeea 1612
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1616 --------------------------EARKAEEVRKAEEVRK-------------------------------------- 1631
Cdd:PTZ00121 1613 kkaeeakikaeelkkaeeekkkveqlKKKEAEEKKKAEELKKaeeenkikaaeeakkaeedkkkaeeakkaeedekkaae 1692
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1632 -------------------AEEVRKAEEVRKAEE--------AKRKAEEDKRKAEEARVDEGEKNKIAH----------- 1673
Cdd:PTZ00121 1693 alkkeaeeakkaeelkkkeAEEKKKAEELKKAEEenkikaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkeeekkaee 1772
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1674 -------VIKEGVDEKD-------DRTTKDIFSNSAVIIEGGKEGNLVVNDSKETEVSATKEVADSSNSVREESKEVQQH 1739
Cdd:PTZ00121 1773 irkekeaVIEEELDEEDekrrmevDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1740 KFNKNNISGEDGNSESNSNSETYNKEDFEEEVEEAKMIKQLDNNDMESEIPNSNYAPKNYESTDDKLDKDEYIKRNAEKT 1819
Cdd:PTZ00121 1853 KFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEET 1932
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1820 RQEIINLSKKDPCIVDVSSKFCDYMKENISSGNCSDVERKELCCSISNYCLKYFSYSSNEYYNCMNEEFGHKDYKCFQKS 1899
Cdd:PTZ00121 1933 REEIIKISKKDMCINDFSSKFCDYMKDNISSGNCSDEERKELCCSISDFCLKYFDHNSNEYYDCMKEEFADKDYKCFKKK 2012
|
2090 2100 2110 2120 2130 2140 2150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056678 1900 KVSNTAYFAGAGIVLILLLVIVSKAILGKWFNEATFDEFDENYEKVYTLAMINREQIQEAGSLDFSGYMSDK 1971
Cdd:PTZ00121 2013 EFSNMAYFAGAGIVLILLFVIGSKAIIGKWFEEATFDEFDENYDKIYTLAMINNEEIQEAGPLDFSEEMIDK 2084
|
|
| EBA-175_VI |
pfam11556 |
Erythrocyte binding antigen 175; EBA-175 is involved in the formation of a tight junction, a ... |
1817-1896 |
5.89e-33 |
|
Erythrocyte binding antigen 175; EBA-175 is involved in the formation of a tight junction, a necessary step in invasion. This family represents the region VI which is a cysteine rich domain essential for EBA-175 trafficking. The structure is a homodimer that contains a five-alpha-helical core stabilized by four disulphide bridges.
Pssm-ID: 431933 Cd Length: 81 Bit Score: 122.98 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1817 EKTRQEIINLSKKDPCIVDVSSKFCDYM-KENISSGNCSDVERKELCCSISNYCLKYFSYSSNEYYNCMNEEFGHKDYKC 1895
Cdd:pfam11556 1 SKTREEIIKLSKKNKCNNEISLKYCDYMiEDNISLGTCSREKRKNLCCSISDYCLKYFDYYSIEYYDCTKKEFDDPSYKC 80
|
.
gi 221056678 1896 F 1896
Cdd:pfam11556 81 F 81
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1495-1672 |
2.13e-14 |
|
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: 76.81 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAEEVRKAEEVRKA---EEVRKAEEARKAEEDKRkaeearkaeearkaeearkaeearkaeevRKAEEVR-KAEEVRKA 1570
Cdd:TIGR02794 84 RAAEQARQKELEQRAaaeKAAKQAEQAAKQAEEKQ-----------------------------KQAEEAKaKQAAEAKA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1571 EEVRKAEEVRKAEEARKAEED---KRKAEEARKAEEDKrkaeearkaeearkaeevRKAEEVRKAEEVrkAEEVRKAEEA 1647
Cdd:TIGR02794 135 KAEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAK------------------KKAEAEAKAKAE--AEAKAKAEEA 194
|
170 180
....*....|....*....|....*..
gi 221056678 1648 KRKAEEDKRKA--EEARVDEGEKNKIA 1672
Cdd:TIGR02794 195 KAKAEAAKAKAaaEAAAKAEAEAAAAA 221
|
|
| PTZ00045 |
PTZ00045 |
apical membrane antigen 1; Provisional |
594-1037 |
3.50e-14 |
|
apical membrane antigen 1; Provisional
Pssm-ID: 240241 [Multi-domain] Cd Length: 595 Bit Score: 78.11 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 594 NPQSKFMERFDIPKNH---IFINWKKDGEFGegNLKYdilsnktagtaqsllidnyndvcpnhSIPGraqGSCPNYGKAI 670
Cdd:PTZ00045 94 NPWKKFMEKFDIPRVHgsgIYVDLGEDAEVG--GKKY--------------------------REPA---GKCPVFGKAI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 671 IVERPENknedsNFnyesLNEIHTGYlgrisinvvelPYDKSGiamhhGFPascpidkqeerLLQRMNDYNYDMCKSRVf 750
Cdd:PTZ00045 143 ILENPDN-----DF----LDPVPTGN-----------PYPKEG-----GFA-----------FPATKVASNSSPTGQLI- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 751 pSPLSMKELDYRNRTLKYyglygfggrlgstisinsrnvgrgekrtnnitlpmknpglINNLLDCSIYSYCLGPCMEGTY 830
Cdd:PTZ00045 186 -SPISAELLRERYYDNGH----------------------------------------CKALNDLALCAEYASNFVPANN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 831 RNKCFRnLPAYYNHATNECVILGTHEQERNSN--CRKetsDLSRPN----CQKIRKTLDSKDWTYVTSFIRPDYEEKCpP 904
Cdd:PTZ00045 225 KNSKYR-YPFVYDEKKKLCYILYLSMQENQGPkyCSV---DGEEGTltwaCFKPDKSKEDNHLLYGSKNVPDDWESKC-P 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 905 RFPLNSKSFGIYDErtGKCRSlIGEDNYVGIQNFGGCLEYLFINSPKD-------------------------------- 952
Cdd:PTZ00045 300 RKPLRNAIFGLWVD--GNCVP-IPPVFEVEAESLEECAKIVFENSPVAsdqptqyeeltdyekikegfknnnlsmiksaf 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 953 --LYNSDRKKYWGVWIGKepvNDYNMFRVTGECYHILQKPTCVIHKENHFSFTSLtTNYIDFYQNFNIEPVEELVERRDI 1030
Cdd:PTZ00045 377 lpLGSFDSDNYKSKGVGY---NWANYDKESGKCEIFDVVPTCLISDSGYYALTAL-SSPNEVDANFPCSIKEKIVLPRIF 452
|
....*..
gi 221056678 1031 IDLDKEG 1037
Cdd:PTZ00045 453 ISTDKDS 459
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1495-1662 |
1.65e-13 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 74.11 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAEEVRKAEEVRKAEEvrkAEEARKAEEdkrkaeeARKAeearkaeearkaeearkaeevRKAEEVRKAEEVRKAEEVR 1574
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEE---AEKQRAAEQ-------ARQK---------------------ELEQRAAAEKAAKQAEQAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1575 K--AEEVRKAEEAR-KAEEDKRKAEEA---RKAEEDKRkaeearkaeearkaeevRKAEEVRKAEEvrKAEEVRKAEEAK 1648
Cdd:TIGR02794 112 KqaEEKQKQAEEAKaKQAAEAKAKAEAeaeRKAKEEAA-----------------KQAEEEAKAKA--AAEAKKKAEEAK 172
|
170
....*....|....
gi 221056678 1649 RKAEEDKRKAEEAR 1662
Cdd:TIGR02794 173 KKAEAEAKAKAEAE 186
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1495-1662 |
2.28e-13 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 73.73 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAEEVRKAEEVRKAEEVRKAEEARKAeedkrkaeearkaeearkaeearkaeearkaeevRKAEEVRKAEEVRKAEEvr 1574
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQ----------------------------------RAAEQARQKELEQRAAA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1575 kAEEVRKAEEARKAEEDKRKAEEARKAeedkrkaeearkaeearkaeevRKAEEVRKAEEvrKAEEVRKAEEAKRKAEED 1654
Cdd:TIGR02794 101 -EKAAKQAEQAAKQAEEKQKQAEEAKA----------------------KQAAEAKAKAE--AEAERKAKEEAAKQAEEE 155
|
170
....*....|....*..
gi 221056678 1655 ---------KRKAEEAR 1662
Cdd:TIGR02794 156 akakaaaeaKKKAEEAK 172
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1512-1743 |
2.74e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 65.06 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1512 VRKAEEARKAEEDKRKAEEARKAEEArkaeearkaeearkaeevRKAEEVRKAEEVRKAEEVRKAEEVRKAEEA---RKA 1588
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKR------------------AAAEAEQKAKEEAEEERLAELEAKRQAEEEareAKA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1589 EEDKRK----AEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRKAEEVRKAEEVRKAEEAKRKAEED-KRKAEEARV 1663
Cdd:COG3064 63 EAEQRAaelaAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEaKRKAEEERK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1664 DEGeknkiahviKEGVDEKDDRTTKDIFSNSAVIIEGGKEGNLVVNDSKETEVSATKEVADSSNSVREESKEVQQHKFNK 1743
Cdd:COG3064 143 AAE---------AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1492-1682 |
3.25e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 64.10 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1492 EEVRK-AEEVRKAEEVRKAeevRKAEEARKAEEdkrkaeearkaeearkaeearkaeearkaeevRKAEEVRKAEEVRKA 1570
Cdd:TIGR02794 108 EQAAKqAEEKQKQAEEAKA---KQAAEAKAKAE--------------------------------AEAERKAKEEAAKQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1571 EEVRKAEEvrKAEEARKAEEDKRKAEEARKAEEDkrkaeearkaeearkaeevrkAEEVRKAEEVR-KAEEVRK--AEEA 1647
Cdd:TIGR02794 153 EEEAKAKA--AAEAKKKAEEAKKKAEAEAKAKAE---------------------AEAKAKAEEAKaKAEAAKAkaAAEA 209
|
170 180 190
....*....|....*....|....*....|....*....
gi 221056678 1648 KRKAEEDK----RKAEEARVDEGEKNKIAHVIKEGVDEK 1682
Cdd:TIGR02794 210 AAKAEAEAaaaaAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| AMA-1 |
pfam02430 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
810-1040 |
4.31e-10 |
|
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual blood-stage antigen. It has been suggested that positive selection operates on the AMA-1 gene in regions coding for antigenic sites.
Pssm-ID: 396824 Cd Length: 432 Bit Score: 64.16 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 810 NNLLDCSIYSYCLGPcmeGTYRNKCFRNlPAYYNHATNECVILGTHEQERNSN--CRKETSD--LSRPNCQKIRKTLDSK 885
Cdd:pfam02430 107 NDLANCSEYASNLIP---ASDKNSKYRY-PFVYDEKEKMCYILYSAAQYNQGPryCDNDSSEegTSSLFCMKPDKSAEDA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 886 DWTYVTSFIRPDYEEKCpPRFPLNSKSFGIYDErtGKCRSlIGEDNYVGIQNFGGCLEYLFINSPKDL------------ 953
Cdd:pfam02430 183 HLYYGSKNVDPDWEKVC-PRKPLRDAIFGLWVD--GNCVA-IPPVFEEEAEDLEECAKIVFENSASDLdieqyneeltdy 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 954 -------------------------YNSDRKKYWGVWIgkepvNDYNMFRVTGECYHILQKPTCVIHKENHFSFTSLTT- 1007
Cdd:pfam02430 259 kkikegfknlnlsmiksaiflplgaFAGDRRISKGVGM-----NWATYDKESKKCAIFNVKPTCLINNAGSIALTALSSp 333
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056678 1008 ------NY-IDFYQNFNIEPVEELVERRDIIDLDKEGNHY 1040
Cdd:pfam02430 334 levdavNYpCSIYKDEIKKEIGYVSPRAKLKSEDKETNKY 373
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1496-1739 |
1.09e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 60.05 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1496 KAEEVRKAEEVRKAEEVRKAEEARKAEEDKRKAEEARKAEEARKAEEARKAeearkaeeVRKAEE----VRKAEEVRKAE 1571
Cdd:COG3064 28 AAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK--------LAEAEKaaaeAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1572 EVRKAEEVRKAEEARKAEEDKRKAEEARKAEEDKRkaeearkaeearkaeevRKAEEVRK---AEEVRKAEEVRKAEEAK 1648
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAK-----------------RKAEEERKaaeAEAAAKAEAEAARAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1649 RKAEEDKRKAEEARVDEGEKNKIAHVIKEGVDEKDDRTTKDIFSNSAVIIEGGKEGNLVVNDSKETEVSATKEVADSSNS 1728
Cdd:COG3064 163 AAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEE 242
|
250
....*....|.
gi 221056678 1729 VREESKEVQQH 1739
Cdd:COG3064 243 AALGGAEEAAD 253
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1105-1252 |
1.54e-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: 55.62 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1105 RKAEEVRKAEEVRKAEEARKAEEdkrkaeearkaeearkaeearkAEEARKAeevRKAEEVRKAEEVRKAEEARK-AEEV 1183
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRA----------------------AEQARQK---ELEQRAAAEKAAKQAEQAAKqAEEK 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056678 1184 RKAEEVRKA----EEARKAEEVRKVEeakkkaeearkaeevRKAEEARKAEEVRKAEEvrKAEEARKAEEVRK 1252
Cdd:TIGR02794 118 QKQAEEAKAkqaaEAKAKAEAEAERK---------------AKEEAAKQAEEEAKAKA--AAEAKKKAEEAKK 173
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1495-1754 |
2.44e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 55.43 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAEEVRKAEEVRkAEEVRKAEEARKAEEDK--RKAEEarkaeearkaeearkaeearkaeevrKAEEVRKAEEVRKAEE 1572
Cdd:COG3064 60 AKAEAEQRAAELA-AEAAKKLAEAEKAAAEAekKAAAE--------------------------KAKAAKEAEAAAAAEK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1573 VRKAEEVRKAEEA-RKAEED-KRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRKAEEVRKAEEVRKAEEAKRK 1650
Cdd:COG3064 113 AAAAAEKEKAEEAkRKAEEEaKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1651 AEEDKRKAEEARVDEGEKNKIAHVIKEGVDEKDDRTTKDIFSNSAVIIEGGKEGNLVVNDSKETEVSATKEVADSSNSVR 1730
Cdd:COG3064 193 ADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAA 272
|
250 260
....*....|....*....|....
gi 221056678 1731 EESKEVQQHKFNKNNISGEDGNSE 1754
Cdd:COG3064 273 ALSSGLVVVAAALAGLAAAAAGLV 296
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1105-1252 |
4.58e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1105 RKAEEVRK-AEEVRKAEEARKAEEdkrkaeearkaeearkaeearkaeearkaeevrKAEEVRKAE---EVRKAEEA-RK 1179
Cdd:TIGR02794 105 KQAEQAAKqAEEKQKQAEEAKAKQ---------------------------------AAEAKAKAEaeaERKAKEEAaKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056678 1180 AEEVRKAEEvrKAEEARKAEEVRKveeakkkaeearkaeevrKAEEARKAEEVrkAEEVRKAEEAR-KAEEVRK 1252
Cdd:TIGR02794 152 AEEEAKAKA--AAEAKKKAEEAKK------------------KAEAEAKAKAE--AEAKAKAEEAKaKAEAAKA 203
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1495-1696 |
5.83e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAEEVRKAEEVRKAEEVR--KAEEARKAEEDKRKAEearkaeearkaeearkaeearkaeevrKAEEVRK-AEEVRK-- 1569
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQqkQAAEQERLKQLEKERL---------------------------AAQEQKKqAEEAAKqa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1570 AEEVRKAEEVR-KAEEARKA---EEDKRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRK---AEEVRKAEEVR 1642
Cdd:PRK09510 128 ALKQKQAEEAAaKAAAAAKAkaeAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAkaaAEAKKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056678 1643 K---AEEAKRKAE-EDKRKAEEARVD---EGEKNKIAHVIKEGVDEKDDRTTKDIFSNSAV 1696
Cdd:PRK09510 208 KkkaAAEAKKKAAaEAKAAAAKAAAEakaAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDS 268
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1160-1264 |
9.86e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1160 RKAEEVRKAEEVRKAEEA---RKAEEVRKAEEVRKA---EEARKAEEVRKVEEAKKKAEEARKAeevRKAEEARKAEEVr 1233
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAekqRAAEQARQKELEQRAaaeKAAKQAEQAAKQAEEKQKQAEEAKA---KQAAEAKAKAEA- 138
|
90 100 110
....*....|....*....|....*....|.
gi 221056678 1234 KAEEVRKAEEARKAEEVRKVEEAKKKAEEAR 1264
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAE 169
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1105-1249 |
1.30e-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: 52.93 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1105 RKAEEVRKAEEVRKA---EEARKAEEDKRKAEEARKAEEARKAEEARKAEEARKAEEVRKAEE--VRKAEEVRKAEEA-- 1177
Cdd:TIGR02794 84 RAAEQARQKELEQRAaaeKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEeaAKQAEEEAKAKAAae 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1178 --RKAEEVRK-----------AEEVRKAEEAR-KAEEVRKveeakkkaeearkaeeVRKAEEARKAEEVRKAEEvrKAEE 1243
Cdd:TIGR02794 164 akKKAEEAKKkaeaeakakaeAEAKAKAEEAKaKAEAAKA----------------KAAAEAAAKAEAEAAAAA--AAEA 225
|
....*.
gi 221056678 1244 ARKAEE 1249
Cdd:TIGR02794 226 ERKADE 231
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1556-1664 |
1.16e-05 |
|
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: 47.34 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1556 RKAEEVRKAEEvRKAEEVRKAEEVRKAEEARKAEEDK-RKAEEARKAEEdkrkaeEARKAEEARKAEEVRKAEEVRKAEE 1634
Cdd:pfam05672 21 RQAREQREREE-QERLEKEEEERLRKEELRRRAEEERaRREEEARRLEE------ERRREEEERQRKAEEEAEEREQREQ 93
|
90 100 110
....*....|....*....|....*....|
gi 221056678 1635 VRKAEEVRKAEEAKRKAEEDkrkAEEARVD 1664
Cdd:pfam05672 94 EEQERLQKQKEEAEAKAREE---AERQRQE 120
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1105-1252 |
1.17e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1105 RKAEEVRKAEEVRKAEEARKAEEDKRKAEEARKAEEARKAEEARkaeearkaeevRKAEEvrKAEEvRKAEEARKAEEVR 1184
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAK-----------RQAEE--EARE-AKAEAEQRAAELA 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056678 1185 kAEEVRKAEEARKAEEVRKVEEAKKKAEEArkaeevRKAEEARKAEEVRKAEEVRKAEEA-RKAEEVRK 1252
Cdd:COG3064 73 -AEAAKKLAEAEKAAAEAEKKAAAEKAKAA------KEAEAAAAAEKAAAAAEKEKAEEAkRKAEEEAK 134
|
|
| AMA-1 |
smart00815 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
810-916 |
2.10e-05 |
|
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual blood-stage antigen. It has been suggested that positive selection operates on the AMA-1 gene in regions coding for antigenic sites.
Pssm-ID: 214831 [Multi-domain] Cd Length: 239 Bit Score: 48.21 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 810 NNLLDCSIYSYCLGPcmeGTYRNKCFRnLPAYYNHATNECVILGTHEQERNSN--CRKETSDLSRPNCQKIRKTLDSKDW 887
Cdd:smart00815 100 NDLSLCAEHASNTVP---GNNKNSKYR-YPFVYDSDDKLCYILYVAAQENQGPryCSNDEEGTSSLFCFKPDKSKEDHHL 175
|
90 100
....*....|....*....|....*....
gi 221056678 888 TYVTSFIRPDYEEKCpPRFPLNSKSFGIY 916
Cdd:smart00815 176 IYGSANVGDDWEEVC-PNKPLRNAKFGLW 203
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1105-1249 |
4.04e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1105 RKAEEVRKAEEVRKAEEARKAEEDKRKaeearkaeearkaeearkaeearkaeevRKAEEVRK-----AEEVRKAEEARK 1179
Cdd:COG3064 33 QKAKEEAEEERLAELEAKRQAEEEARE----------------------------AKAEAEQRaaelaAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056678 1180 A-EEVRKAEEVRKAEEARKAEEVRKveeakkkaeearKAEEVRKAEEARKAEEVRKAEEV--RKAEEARKAEE 1249
Cdd:COG3064 85 AaAEAEKKAAAEKAKAAKEAEAAAA------------AEKAAAAAEKEKAEEAKRKAEEEakRKAEEERKAAE 145
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1104-1252 |
1.45e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1104 VRKAEEVRKAEEVRKAEEARKAEEDkrkaeearkaeearkaeearkaeearkaeeVRKAEEVRKAEEVRKAEEARKAEEV 1183
Cdd:COG3064 64 AEQRAAELAAEAAKKLAEAEKAAAE------------------------------AEKKAAAEKAKAAKEAEAAAAAEKA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1184 RKAEEVRKAEEA-RKAEEVRKVEEAKKKAEEARKAEEVRKAEEARKAEEVRKAEEVRKAEEARKAEEVRK 1252
Cdd:COG3064 114 AAAAEKEKAEEAkRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
|
| AMA-1 |
pfam02430 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
230-424 |
3.08e-04 |
|
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual blood-stage antigen. It has been suggested that positive selection operates on the AMA-1 gene in regions coding for antigenic sites.
Pssm-ID: 396824 Cd Length: 432 Bit Score: 45.29 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 230 NLSDCSIYSYCMGPCFGKDFNnecFRsLPVVFNHRTKECVIL--GTHEASRRRNC---LSQNSYGFERCFVPMKKEAGKE 304
Cdd:pfam02430 108 DLANCSEYASNLIPASDKNSK---YR-YPFVYDEKEKMCYILysAAQYNQGPRYCdndSSEEGTSSLFCMKPDKSAEDAH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 305 WTYASSFLRPDYETKCpPRFPLNDTVFGYYNhrTGECKsAVKNNRGNYKSTFKNCIEGLFNHPEGDR------------- 371
Cdd:pfam02430 184 LYYGSKNVDPDWEKVC-PRKPLRDAIFGLWV--DGNCV-AIPPVFEEEAEDLEECAKIVFENSASDLdieqyneeltdyk 259
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056678 372 ------GNGRNNFLWGVWFLEGSSEKLSS-------MN------DIGMCSILREKPNCVLKKEKHYSFTNLT 424
Cdd:pfam02430 260 kikegfKNLNLSMIKSAIFLPLGAFAGDRriskgvgMNwatydkESKKCAIFNVKPTCLINNAGSIALTALS 331
|
|
| AMA-1 |
smart00815 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
212-334 |
3.44e-04 |
|
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual blood-stage antigen. It has been suggested that positive selection operates on the AMA-1 gene in regions coding for antigenic sites.
Pssm-ID: 214831 [Multi-domain] Cd Length: 239 Bit Score: 44.35 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 212 NPSESHVT----RKMGFSGLIRNLSDCSIYSYCMGPcfGKDFNNEcFRsLPVVFNHRTKECVIL--GTHEASRRRNC-LS 284
Cdd:smart00815 79 NVLLSPISadelKLMYKNHNLNDLSLCAEHASNTVP--GNNKNSK-YR-YPFVYDSDDKLCYILyvAAQENQGPRYCsND 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 221056678 285 QNSYGFERCFVPMKKEAGKEWTYASSFLRPDYETKCpPRFPLNDTVFGYY 334
Cdd:smart00815 155 EEGTSSLFCFKPDKSKEDHHLIYGSANVGDDWEEVC-PNKPLRNAKFGLW 203
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1106-1251 |
5.41e-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: 45.11 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1106 KAEEVRKAEEVRKAEEARKAEEdkrkaEEARKAEEARKAEEARKAEEARKAEEVRKAEEVRKAEEVRKAEEARKAEEVR- 1184
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQ-----AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRe 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056678 1185 ----------KAEEVRKAEEARKAEEVRKVEEAKKKAEEARKAEEVRKAEEARKAEEVRKAEEvrkaEEARKAEEVR 1251
Cdd:pfam17380 380 lerlqmerqqKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE----ERAREMERVR 452
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1556-1671 |
6.29e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 42.37 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1556 RKAEEVRKAEEVRKAEEVRKAEEVRKAEEARKAEEDKRKAEEARKAEEDKRKAeearkaeearkaeevRKAEEVRKAEEV 1635
Cdd:pfam11600 28 QLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEK---------------EKAEKLRLKEEK 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 221056678 1636 R--KAEEVRKAEEAKRKAEEDKRKAEEARVDEGEKNKI 1671
Cdd:pfam11600 93 RkeKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEI 130
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1495-1672 |
7.13e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1495 RKAE-EVRKAEEVRKAEEVRKAEEARKAEEdkrkaeearkaeearkaeearkaeearkaeevRKAEEVRKAEEvRKAEEV 1573
Cdd:COG2268 202 RIAEaEAERETEIAIAQANREAEEAELEQE--------------------------------REIETARIAEA-EAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1574 RKAEEVRKAEEAR-KAEEDKRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRKAEEVRKAEEVRKAEEAKRKAE 1652
Cdd:COG2268 249 KKAEERREAETARaEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
170 180
....*....|....*....|
gi 221056678 1653 EDKRKAEEARVDEGEKNKIA 1672
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAE 348
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1582-1670 |
7.20e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.95 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1582 AEEARKA-EEDKRKAEEARKAEEdkrkaeeaRKAEEARKAEEVRKAEEVRKAEEVR--KAEEVRKAEEAKRKAEED-KRK 1657
Cdd:pfam05672 9 AEEAARIlAEKRRQAREQREREE--------QERLEKEEEERLRKEELRRRAEEERarREEEARRLEEERRREEEErQRK 80
|
90
....*....|...
gi 221056678 1658 AEEARVDEGEKNK 1670
Cdd:pfam05672 81 AEEEAEEREQREQ 93
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1167-1252 |
1.05e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 43.33 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1167 KAEEVRKAEEARKAEEvrkaEEVRKAEEARKAEEVRKveeakkkaeearkaeevrKAEEARKAEEVRK-----AEEVRKA 1241
Cdd:pfam07946 255 RPEALKKAKKTREEEI----EKIKKAAEEERAEEAQE------------------KKEEAKKKEREEKlaklsPEEQRKY 312
|
90
....*....|.
gi 221056678 1242 EEARKAEEVRK 1252
Cdd:pfam07946 313 EEKERKKEQRK 323
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1106-1251 |
1.68e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1106 KAEEVRKAEEVRKAEEarKAEEDKRKAEEARKAEEARKAEEARKAEEARKAEEVRKAEEVRKAEE----VRKAEEARKAE 1181
Cdd:COG3064 22 EAEKRAAAEAEQKAKE--EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKaaaeAEKKAAAEKAK 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056678 1182 EVRKAEEVRKAEEARKAEEVRKVEEAKkkaeearkaeevRKAEE--ARKAEEVRKAEEVRKAEEARKAEEVR 1251
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAK------------RKAEEeaKRKAEEERKAAEAEAAAKAEAEAARA 159
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1444-1763 |
2.53e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1444 AKkkaeearkaeeakkkaeearkaeearkaeearkaeearkaeearkaeevRKAEEVRKAEEVRKAEEVRKAEEA---RK 1520
Cdd:COG3064 31 AE-------------------------------------------------QKAKEEAEEERLAELEAKRQAEEEareAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1521 AEEdkrkaeearkaeearkaeearkaeearkaeevRKAEEVRKAEEVRKAEEVRKAEEVRKAEEARKAEEDKRKAEEARK 1600
Cdd:COG3064 62 AEA--------------------------------EQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1601 AEEDKrkaeearkaeearkaeevRKAEEVRKAEEVRKAEEV--RKAEEAKRKAEEDKRKAEEARVDEGEKNKIAHVIKEG 1678
Cdd:COG3064 110 AEKAA------------------AAAEKEKAEEAKRKAEEEakRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1679 VDEKDDRTTKDIFSNSAVIIEGGKEGNLVVNDSKETEVSATKEvadSSNSVREESKEVQQHKFNKNNISGEDGNSESNSN 1758
Cdd:COG3064 172 ARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA---ALLALAVAARAAAASREAALAAVEATEEAALGGA 248
|
....*
gi 221056678 1759 SETYN 1763
Cdd:COG3064 249 EEAAD 253
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1624-1665 |
2.74e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 42.17 E-value: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 221056678 1624 RKAEEVRK--AEEVRKAEEVRKAEEAKRKAEEDKRKAEEARVDE 1665
Cdd:pfam07946 260 KKAKKTREeeIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLAK 303
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1556-1664 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1556 RKAEEVRKAEEVRKA---EEVRKAEEVR-----KAEEARKAEEDKRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAE 1627
Cdd:pfam15709 363 LQQEQLERAEKMREElelEQQRRFEEIRlrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE 442
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 221056678 1628 EVRKAEevrkAEEVRKAEEAKRKAEEDKR---KAEEARVD 1664
Cdd:pfam15709 443 EAERAE----AEKQRQKELEMQLAEEQKRlmeMAEEERLE 478
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1496-1734 |
7.38e-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: 41.26 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1496 KAEEVRKAEEvrKAEEVRKAEEARKAEEdkrkaeearkaeeARKAEEAR--------KAEEARKAEEVRKAEEVRKAEEV 1567
Cdd:pfam17380 295 KMEQERLRQE--KEEKAREVERRRKLEE-------------AEKARQAEmdrqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1568 RKAEEVRKAEEVRKAEEARKAE----EDKRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRKAEEVRKAEEVRK 1643
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1644 AEEAK-RKAE-------EDKRKAEEARVDEGEKNKiahviKEGVDEKDDRTTKDIFSNSAVIIEGG-KEGNLVVNDSKET 1714
Cdd:pfam17380 440 LEEERaREMErvrleeqERQQQVERLRQQEEERKR-----KKLELEKEKRDRKRAEEQRRKILEKElEERKQAMIEEERK 514
|
250 260
....*....|....*....|
gi 221056678 1715 EVSATKEVADSSNSVREESK 1734
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEER 534
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1104-1252 |
7.90e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1104 VRKAEEVRKAEEVRKAEEARKAEedkrkaeearkaeearkaeearkaeearkaeeVRKAE-----EVRKAEEVRKAEEAR 1178
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETE--------------------------------IAIAQanreaEEAELEQEREIETAR 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056678 1179 KAEEvRKAEEVRKAEEARKAEEVRKVEEAKKKAEEARKAEEV-RKAEEARKAEEVRKAEEVRKAEEARKAEEVRK 1252
Cdd:COG2268 239 IAEA-EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELEADVRK 312
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
1557-1734 |
8.57e-03 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 40.75 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1557 KAEEVRKAEEVRKAEEVRKA-----EEVRKAEEARKAEEDKRKAEEARKAEEDKRKAEEARKAEEARKAEEVRKAEEVRK 1631
Cdd:PRK05901 11 AAEEEAKKKLKKLAAKSKSKgfitkEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKAAAAKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1632 AEEVRKAEEVRKAEEAKRKAEEDKRKAEEARVDEGEKNKIAHVIKEGVDEKDDRTTKDIFSNSAVIIEGGKEGNLVVNDS 1711
Cdd:PRK05901 91 PAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDDVDDEDE 170
|
170 180
....*....|....*....|...
gi 221056678 1712 KETEVSATKEVADSSNSVREESK 1734
Cdd:PRK05901 171 EKKEAKELEKLSDDDDFVWDEDD 193
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1559-1665 |
9.44e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 37.98 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1559 EEVRKA-EEVRKAEEvrKAEEVrkAEEARKAEEDKRKAEEARKAEEDKRKAEEARKAEEarkaeevrKAEEVRKAEEVRK 1637
Cdd:pfam20492 20 EETKKAqEELEESEE--TAEEL--EEERRQAEEEAERLEQKRQEAEEEKERLEESAEME--------AEEKEQLEAELAE 87
|
90 100 110
....*....|....*....|....*....|...
gi 221056678 1638 AEEV--RKAEEAKRKAEEDKR---KAEEARVDE 1665
Cdd:pfam20492 88 AQEEiaRLEEEVERKEEEARRlqeELEEAREEE 120
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
1556-1726 |
9.95e-03 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 40.40 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1556 RKAEEVRKAEEVRKAEEVRKAEEVRKAEEAR--KAEEDKRKAEEARKAEEDKRKAEEARKAEEarkaeevRKAEEVRKAE 1633
Cdd:COG5269 201 AKNREKRAKLKNQDNARLKRLVQIAKKRDPRikSFKEQEKEMKKIRKWEREAGARLKALAALK-------GKAEAKNKAE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056678 1634 EVrkAEEVRKAEEAKRKAEEDKRKAEEArvdegEKNKIAHVIKEGVDEKDDRTTKDIFSNSAVIIEGGKEGNLV-VNDSK 1712
Cdd:COG5269 274 IE--AEALASATAVKKKAKEVMKKALKM-----EKKAIKNAAKDADYFGDADKAEHIDEDVDLIMDKLGDEELGqLAADI 346
|
170
....*....|....
gi 221056678 1713 ETEVSATKEVADSS 1726
Cdd:COG5269 347 KAEAAGAAAVFDEF 360
|
|
| |
