|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-2054 |
0e+00 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 2550.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1 MGVLKHFFFLLFLYVNNTSAINNPQEEFMDRFDINKNHVNIKWSNSGIHGKGKFKYEIEERDVLS-EGNESEKSTICPNH 79
Cdd:PTZ00121 1 MGLLKFFAFLAFLCICKAKAIANPQEAFMDRFDIAKNHINIKWSNNGIHGEGDFKYDIDDGDNLDfEGNEEEKSGICPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 80 VKEGTYKLGCPDYGKTFLMGFEDNKYSEEFLNEISFGFLNKKYKLPIEIPLNKSGLSMYQGLFKRCPYNKKHYSMIKNEN 159
Cdd:PTZ00121 81 GAEEMYKGGCPDYGKTFLMDFEDDEYNEEFLDEISFGFLNKKLKLPIEIPLEKSGLAMYQGLFKRCPLDEKHSSLIKKEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 160 EYDMCFRKFYNNSNISTRIYKRGKQNRKYIYFSSHGLGGRLGANIEEPLHKYKNDEHYVTKKMRYPEKIKNLFDCSIYSH 239
Cdd:PTZ00121 161 EYDMCFEKFYNNMEISDRIKKRGKQNRKYIHFGSHGLGGRFGANIDEPLHDYKNDEHHVTKKMGFPEKIKNLFDCSIYSH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 240 CIGPCLYKDFNNSCFLNLPILFNHQTKECVIIGTHEEKRIHNCQSGSTDQNIQRCFLPVKKEKGNQWTYASSFIRTDYMT 319
Cdd:PTZ00121 241 CIGPCFGKDFNNECFLNLPILFNHQTKECVIIGTHEAKRIHNCLSGNSDQGFERCFLPMKKEAGKEWTYASSFIRPDYET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 320 KCPPRFPLNHTMFGYFNYSTGKCETYYMNHEKR-TLSFSKCIETLFNNIKKQDDVNNSSFLWGVWTIENNANEKTNLASM 398
Cdd:PTZ00121 321 KCPPRFPLNDTMFGYFNHRTGECESAVKNHEGNyKLSFKKCIEGLFNHIEGDDDNGNNNFLWGVWFIEGNAEEKTNLASM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 399 DNTGSCYFLKKKPTCVLKKENHFSFTILTANSFNLNQNIIYPELKNNSSKE-GSSLIHFKDPKQTNKRVLYENNKKSKRN 477
Cdd:PTZ00121 401 DDIGMCSFLKEKPNCVLKKEKHFSFTILTANSFDFAQNIIYPELEEMHDKEnGSSLIGEKAPEGREERIDLEENDGKKEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 478 VRTKINSVNPFTIPSTLNTNEKEEYNKNEVKNYPNNNISYIQKVHSSFVNNRFNIHSDSSFK----PIHKMIQMNIYTDN 553
Cdd:PTZ00121 481 AGSEDKEIKEFEIPQNLNKNEKEEINEHEVKGLPKENINYILKVHMRFENNHFNIHNDSIFKrkdePIHKMIELNIPSDN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 554 KLYNNNNQKIKDSN------NNMNGMSVTQRSPSIGENQNGNPQQKYMERFDIPNNHIFIEWQKEGEYGNDEFKYNIISN 627
Cdd:PTZ00121 561 KLHNLGAQGIGDSNishwnsNNINGGSVSQNEGNIGEKLNGNPQQKFMERFDIPKNHIFIEWKKDGEFGEDEFKYDIISN 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 628 KTAGTSQSLFHNYKDKTCPNHVYEGRAHGSCPNYGKAIIVQNLLGEEYDKNFNLNFLNEIRTGYLNKYFKKDVEISYENS 707
Cdd:PTZ00121 641 KTAGTAQSLFHDNKDDTCPNHSIEGRAHGSCPNYGKAIIVENLEGEEEDKNFNLEFLNEIHTGYLGKIFIKDVEIPYDKS 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 708 GIAMHNNMLRSCPVHENEEKLFSVKTDYNYKMCKSKIFSNRFTMKEYDPKTRLFMYYGLYGLGGRLGANI---KRDKQKE 784
Cdd:PTZ00121 721 GIAMHHGFLASCPIDENEEKLFQRKNDYNYDMCKSKIFPNPFSMKELDPKNRLFKYYGLYGFGGRLGANIsinKRDKGKE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 785 KKYEDNITLPMKNPSLIKNLFDCSIYSYCLGPCLENSFGNKCFRNLPAYYNHLTNECVILGTHEQERTNSCRRTKEEKKK 864
Cdd:PTZ00121 801 EKREDNITLPMKNPGLIKNLFDCSIYSYCLGPCLEGSFGNKCFRNLPAYYNHATNECVILGTHEQERNNNCRKEKEDKKK 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 865 PNCQILRKTTDSKDWTYVSSFIRPDYETKCPPRYPLKSKVFGTFDQKTGKCKSLMDKAYEVGINKFSVCLEYLFLVSPKD 944
Cdd:PTZ00121 881 PNCQIIRKTLDSKDWTYVSSFIRPDYEEKCPPRFPLKSKSFGIFDEKTGKCKSLIDEANEVGINKFGGCLEYLFINSPKD 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 945 LYNSGRNNYWGIWAADHSVNENNIEIANGKCYHLVVKPTCVIDKENHFSFTALTANTVDFNQSVNIRKIEELTEYGNNDD 1024
Cdd:PTZ00121 961 LYNSDRKKYWGIWAADEPVNDNNIEIANGECYHILQKPTCVIDKENHFSFTALTANTIDFNQNFNIEKIEELTEYGNNDD 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1025 VLKEKEINNEPIDNVNETKINRKSHVNSMERNKPSYKENEYDQMEKNVEDETYSEEFGLFEEARKTETGRIEEESKKKEA 1104
Cdd:PTZ00121 1041 VLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1105 MKRAEDARRIEEARRAEDARRIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRRA-ELRKAEDAR 1183
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAeELRKAEDAR 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1184 RIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1264 DELKKKAEEKKKAAELKKKAEEKKKADEVKKAEEKKKADELKKSEEKKKADELKKKAEEKKKADELKKKAEEKKKAENLK 1343
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1344 KAEEKKKAENLKKAEEKKKADELKKKAEEKKKADELKKKAEEKKK-----ADELKKKAEEKKKAENLKKAEEKKKAENLK 1418
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadelKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1419 KAEEKKKADELKKKAEEKKKADEVKKAEEKKKADELKKKAEEKKKADELKKKAEEKKKADELKKKAEEKKKADELKKAEE 1498
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1499 KKKADELKKAEEKKKADELKKAEEKKKADELEKAEELKKAEEKKKVEQKKREEERRNMALRRAEILKQIEKKRIEEVMKL 1578
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1579 YEEEKKMKAEQLKKEEEEKIKAEQLKKEEEEKKKVEQLKKKEEEEKKKAEQLKKEEEENKIKAEQLKKKEEEEKKKAEEL 1658
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1659 KKEEEEEKKKAEQLKKEEEEKKKVEQLKKKEEEEKKKAEQLKKEEEENKIKVEQLKKEEEEEKKKAEQLKKEEEEKKKVQ 1738
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1739 QLKKEEEKKAEEIRKEKEAVIEEELKKEDEKRRMEVEKKIKDTKDNFENIQEGNNKNTPYIN--KEMFDSEIKEVVITKN 1816
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINdsKEMEDSAIKEVADSKN 1840
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1817 MQLNEADAFEKH----NSENSKSSNKNADFSKEKDLLEDDIENILETDENEKINKDDIER--SNNNMKGNNNDIIYTKLD 1890
Cdd:PTZ00121 1841 MQLEEADAFEKHkfnkNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEReiPNNNMAGKNNDIIDDKLD 1920
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1891 VEEYKKRDVNETREKIIKISKKNMCNNDFSSKYCDYMKDNISSGTCSNEERKSLCCSISDFCLKYFDHNSNKYYDCTKIE 1970
Cdd:PTZ00121 1921 KDEYIKRDAEETREEIIKISKKDMCINDFSSKFCDYMKDNISSGNCSDEERKELCCSISDFCLKYFDHNSNEYYDCMKEE 2000
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1971 FADPLYRCFKKKEFSNMVYFAGAGIVLILLFVIGSKMIIGKWFEEATFDEMDLNYDKIYTLAMINNEETQVSNPLSYSEE 2050
Cdd:PTZ00121 2001 FADKDYKCFKKKEFSNMAYFAGAGIVLILLFVIGSKAIIGKWFEEATFDEFDENYDKIYTLAMINNEEIQEAGPLDFSEE 2080
|
....
gi 914546577 2051 NIIK 2054
Cdd:PTZ00121 2081 MIDK 2084
|
|
| EBA-175_VI |
pfam11556 |
Erythrocyte binding antigen 175; EBA-175 is involved in the formation of a tight junction, a ... |
1900-1979 |
5.75e-37 |
|
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: 134.54 E-value: 5.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1900 NETREKIIKISKKNMCNNDFSSKYCDYM-KDNISSGTCSNEERKSLCCSISDFCLKYFDHNSNKYYDCTKIEFADPLYRC 1978
Cdd:pfam11556 1 SKTREEIIKLSKKNKCNNEISLKYCDYMiEDNISLGTCSREKRKNLCCSISDYCLKYFDYYSIEYYDCTKKEFDDPSYKC 80
|
.
gi 914546577 1979 F 1979
Cdd:pfam11556 81 F 81
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
989-1262 |
1.50e-12 |
|
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: 72.85 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 989 ENHFSFTALtaNTVDFNQSVNIRKIEELTEYGNNDDVLKEKEINNEPIDNVNETKINRKSHVNSMERNKPSYKENEYDQM 1068
Cdd:pfam17380 267 ENEFLNQLL--HIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1069 EKNVE-------------DETYSEEFGL------------FEEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDA 1123
Cdd:pfam17380 345 ERERElerirqeerkrelERIRQEEIAMeisrmrelerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1124 RRIEEarraEDARRVEIaRRVEDARRIEISRraedaKRIEAARRAIEVRRaeLRKAEDARR---IEAARRYENERRIEEA 1200
Cdd:pfam17380 425 IRAEQ----EEARQREV-RRLEEERAREMER-----VRLEEQERQQQVER--LRQQEEERKrkkLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914546577 1201 RRYEDEKRIEAVKRA--EEVRKdeeeakraekernneeiRKFEEARMAHfarRQAAIKAEEKRK 1262
Cdd:pfam17380 493 RRKILEKELEERKQAmiEEERK-----------------RKLLEKEMEE---RQKAIYEEERRR 536
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1085-1263 |
1.42e-11 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 69.30 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESK-KKEAMKRAEDARRIEEARRAEDARRIEEARRAedaRRVEIARRVEDarrieisRRAEDAKRIE 1163
Cdd:COG3064 11 EAAAQERLEQAEAEKRaAAEAEQKAKEEAEEERLAELEAKRQAEEEARE---AKAEAEQRAAE-------LAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1164 AARRAIEV--RRAELRKAEDARRIEAARRYENERRIEEARRYEDEKR---IEAVKRAEEVRKDEEEAKRAEKERNNEEIR 1238
Cdd:COG3064 81 EAEKAAAEaeKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkaeEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180
....*....|....*....|....*
gi 914546577 1239 KFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAA 185
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1100-1263 |
3.05e-11 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 68.14 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1100 KKKEAMKRAEDARRiEEARRAEDARRieeaRRAEDARRVEIARRVEDARRIEISRRAEdakriEAARRAievrRAELRKA 1179
Cdd:COG3064 2 QEALEEKAAEAAAQ-ERLEQAEAEKR----AAAEAEQKAKEEAEEERLAELEAKRQAE-----EEAREA----KAEAEQR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1180 EDARRIEAARRYEN-ERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKraekernNEEIRKFEEARMAhfARRQAAIKAE 1258
Cdd:COG3064 68 AAELAAEAAKKLAEaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAA-------AAEKEKAEEAKRK--AEEEAKRKAE 138
|
....*
gi 914546577 1259 EKRKA 1263
Cdd:COG3064 139 EERKA 143
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1085-1264 |
3.53e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 67.18 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMK--RAEDARRIEEARraEDARRIEEARRAEDARRVEIARRVEDARRIEIsRRAEDAKRI 1162
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAEkqRAAEQARQKELE--QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-QAAEAKAKA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1163 EAARRAIEVRRAElRKAEDARRIEAARryENERRIEEARRyedeKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEE 1242
Cdd:TIGR02794 137 EAEAERKAKEEAA-KQAEEEAKAKAAA--EAKKKAEEAKK----KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEA 209
|
170 180
....*....|....*....|..
gi 914546577 1243 ARMAHfARRQAAIKAEEKRKAD 1264
Cdd:TIGR02794 210 AAKAE-AEAAAAAAAEAERKAD 230
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1082-1263 |
7.94e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1082 GLFEEA--------RKtetgrieEESKKK-EAMK----RAED-----ARRIEE-ARRAEDARR-------IEEARRAEDA 1135
Cdd:COG1196 159 AIIEEAagiskykeRK-------EEAERKlEATEenleRLEDilgelERQLEPlERQAEKAERyrelkeeLKELEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1136 RRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRRAELRKA--EDARRIEAARRYENE-----RRIEEARRYEDEKR 1208
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleELELELEEAQAEEYEllaelARLEQDIARLEERR 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 914546577 1209 IEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| PTZ00045 |
PTZ00045 |
apical membrane antigen 1; Provisional |
584-1024 |
9.52e-11 |
|
apical membrane antigen 1; Provisional
Pssm-ID: 240241 [Multi-domain] Cd Length: 595 Bit Score: 66.94 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 584 ENQNGNPQQKYMERFDIPNNH---IFIEWQKEGEYGNdeFKYNIISnktagtsqslfhnykdktcpnhvyegrahGSCPN 660
Cdd:PTZ00045 89 SNRKQNPWKKFMEKFDIPRVHgsgIYVDLGEDAEVGG--KKYREPA-----------------------------GKCPV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 661 YGKAIIVQNLlgeeydknfNLNFLNEIRTGylNKYFKKdveisyenSGIAMhnNMLRSCPVHENEEKLFSVKTDYNykmc 740
Cdd:PTZ00045 138 FGKAIILENP---------DNDFLDPVPTG--NPYPKE--------GGFAF--PATKVASNSSPTGQLISPISAEL---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 741 kskifsnrftMKEYdpktrlfmyyglyglggrlganikRDKQKEKKYEDNITLpmknpsliknlfdCSIYSYCLGPcleN 820
Cdd:PTZ00045 193 ----------LRER------------------------YYDNGHCKALNDLAL-------------CAEYASNFVP---A 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 821 SFGNKCFRnLPAYYNHLTNECVILGTHEQERTNS--CRRTKEEKK------KPncqilRKTTDSKDWTYVSSFIRPDYET 892
Cdd:PTZ00045 223 NNKNSKYR-YPFVYDEKKKLCYILYLSMQENQGPkyCSVDGEEGTltwacfKP-----DKSKEDNHLLYGSKNVPDDWES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 893 KCPpRYPLKSKVFGTFDQktGKCKSlMDKAYEVGINKFSVCLEYLFLVSPKD--------------LYNSGRNN-----Y 953
Cdd:PTZ00045 297 KCP-RKPLRNAIFGLWVD--GNCVP-IPPVFEVEAESLEECAKIVFENSPVAsdqptqyeeltdyeKIKEGFKNnnlsmI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 954 WGIWAADHSV------------NENNIEIANGKCYHLVVKPTCVIDKENHFSFTALTA-NTVDFNQSVNIRKIEELTEYG 1020
Cdd:PTZ00045 373 KSAFLPLGSFdsdnykskgvgyNWANYDKESGKCEIFDVVPTCLISDSGYYALTALSSpNEVDANFPCSIKEKIVLPRIF 452
|
....
gi 914546577 1021 NNDD 1024
Cdd:PTZ00045 453 ISTD 456
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1070-1259 |
4.64e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.04 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1070 KNVEDET-YSEEFGLFEEARKTETGRIEE-ESKKKEAMKRAEDARRIEEARrAEDARRIEEARRAEDARrvEIARRVEDA 1147
Cdd:COG2268 177 TDLEDENnYLDALGRRKIAEIIRDARIAEaEAERETEIAIAQANREAEEAE-LEQEREIETARIAEAEA--ELAKKKAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1148 RRieisrrAEDAKRIEAARrAIEVRRAELRKaEDARRIEAARRyenERRIEEARryedekrIEAVKRAEEVRKDeeeakr 1227
Cdd:COG2268 254 RR------EAETARAEAEA-AYEIAEANAER-EVQRQLEIAER---EREIELQE-------KEAEREEAELEAD------ 309
|
170 180 190
....*....|....*....|....*....|..
gi 914546577 1228 aekernneeIRKFEEarmahfARRQAAIKAEE 1259
Cdd:COG2268 310 ---------VRKPAE------AEKQAAEAEAE 326
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1065-1261 |
2.78e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1065 YDQM--EKNVED--ETYSEEFGLFEEARKtetgRIEEESKKKEAMKRA-EDARRIEEARRaedarRIEEARRAEDARRVE 1139
Cdd:COG4913 214 REYMleEPDTFEaaDALVEHFDDLERAHE----ALEDAREQIELLEPIrELAERYAAARE-----RLAELEYLRAALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1140 IARRVEDARRIEISRRAEDAKRIEAARRAIEVRRAELRkaEDARRIEAARRYENERRIEEARRyEDEKRIEAVKRAEEVR 1219
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALR--EELDELEAQIRGNGGDRLEQLER-EIERLERELEERERRR 361
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 914546577 1220 KDEEEAKRAEKERNNEEIRKFEEARmAHFARRQAAIKAEEKR 1261
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALR-AEAAALLEALEEELEA 402
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1056-1263 |
4.17e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1056 NKPSYKENEY-DQMEKNVEDETYSEEFGLFEEARKTETGRIEEEskKKEAMKRAEDARRIEE---ARRAEDARRI----E 1127
Cdd:pfam17380 261 NGQTMTENEFlNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQE--KEEKAREVERRRKLEEaekARQAEMDRQAaiyaE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1128 EARRA-EDARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRRAELRKAEDARR-IEAARRY-----ENERRIEEA 1200
Cdd:pfam17380 339 QERMAmERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKVkileeERQRKIQQQ 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914546577 1201 RRYEDEKRIEAvkraEEVRKDEEEAKRAEKERNNEEIRKFEEARMAHFAR-RQAaiKAEEKRKA 1263
Cdd:pfam17380 419 KVEMEQIRAEQ----EEARQREVRRLEEERAREMERVRLEEQERQQQVERlRQQ--EEERKRKK 476
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1085-1214 |
4.98e-08 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 54.28 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEEskKKEAMKRAEDARRIEEARraedARRIEEARRAEDARRveiaRRVEDARRIEISRRAEDAK--RI 1162
Cdd:pfam05672 25 EQREREEQERLEKE--EEERLRKEELRRRAEEER----ARREEEARRLEEERR----REEEERQRKAEEEAEEREQreQE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 914546577 1163 EAARRAIEVRRAELRKAEDARRieaaRRYENERRI--EEARRYEDEKRIEAV-KR 1214
Cdd:pfam05672 95 EQERLQKQKEEAEAKAREEAER----QRQEREKIMqqEEQERLERKKRIEEImKR 145
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1027-1262 |
6.57e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.57 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1027 KEKEINNEPI-DNVNETKINrkshvNSMERNKPSYKENEYDQME-KNVEDETYSEEFGLFEEARKTETGRIEEESKKKEa 1104
Cdd:pfam02029 87 KEFDPTIADEkESVAERKEN-----NEEEENSSWEKEEKRDSRLgRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1105 mKRAEDARRIEEARRAEDARRIEEARraEDARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRRAELRKAEDARR 1184
Cdd:pfam02029 161 -DKSEEAEEVPTENFAKEEVKDEKIK--KEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1185 IEAARRYENERRIEEARRYEDEKRIEAVKRAEEvRKDEEEAKRAEKERNNEEIRKFEEA----RMAHFARRQAAiKAEEK 1260
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQ-KQQEAELELEELKKKREERRKLLEEeeqrRKQEEAERKLR-EEEEK 315
|
..
gi 914546577 1261 RK 1262
Cdd:pfam02029 316 RR 317
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1103-1265 |
2.59e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1103 EAMKRAEDARRIEEARRAEdARRIEEARRAEDARRVEIARrVEDARRIEISRRAEdakrieaARRAIEVRRAELRKAEDA 1182
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAE-AERETEIAIAQANREAEEAE-LEQEREIETARIAE-------AEAELAKKKAEERREAET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1183 RRIEAARRYENERriEEARRyEDEKRIEAVKRAEEVRkdeeeakraekernneeirkfeearmahfARRQAAIKAEEKRK 1262
Cdd:COG2268 260 ARAEAEAAYEIAE--ANAER-EVQRQLEIAEREREIE-----------------------------LQEKEAEREEAELE 307
|
...
gi 914546577 1263 ADE 1265
Cdd:COG2268 308 ADV 310
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
1094-1218 |
5.96e-07 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 51.21 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1094 RIEEESKKKEAMKRAEDARRIEEARRAedarrIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRIEAARraievrr 1173
Cdd:pfam15346 23 RVEEELEKRKDEIEAEVERRVEEARKI-----MEKQVLEELEREREAELEEERRKEEEERKKREELERILEEN------- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 914546577 1174 aeLRKAEDARRIEAARRY---ENERRIEEARRYEDEKRIEAVKRAEEV 1218
Cdd:pfam15346 91 --NRKIEEAQRKEAEERLamlEEQRRMKEERQRREKEEEEREKREQQK 136
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1064-1217 |
6.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1064 EYDQMEKNVED-ETYSEEFGLFEEARKTETGRiEEESKKKEAMKRAEDARRIEEARRA---EDARRIEEARRAEDARRVE 1139
Cdd:COG4913 263 RYAAARERLAElEYLRAALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDalrEELDELEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1140 -IARRVEDARRiEISRRAEDAKRIEAARRAIEVRRAELRKAEDARRIEAARR---YENERRIEEARRYEDEKRIEAVKRA 1215
Cdd:COG4913 342 qLEREIERLER-ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALleaLEEELEALEEALAEAEAALRDLRRE 420
|
..
gi 914546577 1216 EE 1217
Cdd:COG4913 421 LR 422
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
1086-1212 |
1.17e-06 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 50.52 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1086 EARKTETGRIEEE-SKKKEAMKRAEDAR--RIEEARRAEDARRIEEARRAE----------------DARRVEIARRVED 1146
Cdd:pfam09486 11 ERRTRRYQRLRAElEAARAALAQAEAALaaAQAQAEQARDRVRAHEERLDDlttggspfsaadylacRAYRDVLEGRVGA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914546577 1147 ARRIEisRRAEDAkrIEAARRAIEVRRAELRKAE---DA--RRIEAARRYEnERRIEEArryEDEKRIEAV 1212
Cdd:pfam09486 91 AEAAL--AAARQA--LDAAEDAVAATRRKIARNDaqlDVcrERIARLRRAA-ERAREDA---ADEEAEEAA 153
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1083-1218 |
1.41e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.68 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1083 LFEEARKT-ETGRIEEESKKKEAMKRAEDARriEEARRAEDARRiEEARRAEDARRVEIARRVE---------------- 1145
Cdd:NF041483 518 LRRQAEETlERTRAEAERLRAEAEEQAEEVR--AAAERAARELR-EETERAIAARQAEAAEELTrlhteaeerltaaeea 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1146 --DAR----RI------EISR-RAEDAKRIEAARRAIEVRRAELRK--AEDAR-------------RIEAARryENERRI 1197
Cdd:NF041483 595 laDARaeaeRIrreaaeETERlRTEAAERIRTLQAQAEQEAERLRTeaAADASaaraegenvavrlRSEAAA--EAERLK 672
|
170 180
....*....|....*....|.
gi 914546577 1198 EEARRYEDEKRIEAVKRAEEV 1218
Cdd:NF041483 673 SEAQESADRVRAEAAAAAERV 693
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
989-1217 |
1.50e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.03 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 989 ENHFSFTALTANTVDFNQSVNIRKIEELTEYGNNDDVLKEKEINNEPIDNVNETK-------INRKSHVNSMERNKPSYK 1061
Cdd:pfam15709 288 ESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERaemrrleVERKRREQEEQRRLQQEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1062 ENEYDQMEKNVEDE--TYSEEFGLFEEARKTETGRIEEESKKKEAMKRA--EDARRIEEARRaEDARRIEEARRAEDARR 1137
Cdd:pfam15709 368 LERAEKMREELELEqqRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAaqERARQQQEEFR-RKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1138 VEiarrVEDARRIEISRR-AEDAKRIeaARRAIEVRRAELRK---AEDARRIEAARRyenERRIEEARRYEDEkriEAVK 1213
Cdd:pfam15709 447 AE----AEKQRQKELEMQlAEEQKRL--MEMAEEERLEYQRQkqeAEEKARLEAEER---RQKEEEAARLALE---EAMK 514
|
....
gi 914546577 1214 RAEE 1217
Cdd:pfam15709 515 QAQE 518
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1153-1220 |
8.30e-06 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 46.28 E-value: 8.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914546577 1153 SRRAEDAKRIEAARRAIE--VRRAE------LRKAE-DARRIEAARRyenERRIEEARRYEDEKRIEAVKRAEEVRK 1220
Cdd:pfam16999 12 EREAALDQQIEAARKEAEreVEAAEaeaariLREAEaKAKALQAEYR---QELAAETARIREEARARAEAEAQAVRT 85
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1085-1251 |
8.63e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 51.06 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKkEAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRIEA 1164
Cdd:PRK12678 100 AKAEAAPAARAAAAAAA-EAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1165 ARRAIEVRRAEL----RKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKF 1240
Cdd:PRK12678 179 EDRQAEAERGERgrreERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGR 258
|
170
....*....|.
gi 914546577 1241 EEARMAHFARR 1251
Cdd:PRK12678 259 GGRRGRRFRDR 269
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1097-1263 |
9.27e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1097 EESKKKEAMKRaEDARRIEEARRAEDARR--IEEARRAEDARRVEIARRVEDARRIEIS-RRAEDAKRIEAARRAIEVR- 1172
Cdd:PRK07735 2 DPEKDLEDLKK-EAARRAKEEARKRLVAKhgAEISKLEEENREKEKALPKNDDMTIEEAkRRAAAAAKAKAAALAKQKRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1173 -----------RAELRKAEDARRIEAARRYENERRIEEARRYEDEK-----RIEAVKRAEEVRKDEEEAKRAEKERNNEE 1236
Cdd:PRK07735 81 gteevteeekaKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAakakaAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180
....*....|....*....|....*..
gi 914546577 1237 IRKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAE 187
|
|
| AMA-1 |
pfam02430 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
831-1034 |
1.17e-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: 396824 Cd Length: 432 Bit Score: 50.30 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 831 PAYYNHLTNECVILGTHEQERTNSCRRTKEEKKKPN----CQILRKTTDSKDWTYVSSFIRPDYETKCPpRYPLKSKVFG 906
Cdd:pfam02430 132 PFVYDEKEKMCYILYSAAQYNQGPRYCDNDSSEEGTsslfCMKPDKSAEDAHLYYGSKNVDPDWEKVCP-RKPLRDAIFG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 907 TFDQktGKCKSLmDKAYEVGINKFSVCLEYLFLVSPKDL----YNSGRNNY----------------------WGIWAAD 960
Cdd:pfam02430 211 LWVD--GNCVAI-PPVFEEEAEDLEECAKIVFENSASDLdieqYNEELTDYkkikegfknlnlsmiksaiflpLGAFAGD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 961 H------SVNENNIEIANGKCYHLVVKPTCVIDKENHFSFTALTA-NTVD-FNQSVNIRKIEELTEYGNNDDVLKEKEIN 1032
Cdd:pfam02430 288 RriskgvGMNWATYDKESKKCAIFNVKPTCLINNAGSIALTALSSpLEVDaVNYPCSIYKDEIKKEIGYVSPRAKLKSED 367
|
..
gi 914546577 1033 NE 1034
Cdd:pfam02430 368 KE 369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
999-1264 |
1.27e-05 |
|
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: 50.44 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 999 ANTVDFNQSVNIRKIEELTEYGNNDDVLKEKEINN--EPIDNVNETKINRKSHVNSMERnKPSYKENEYDQMEKNVEDET 1076
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAElrKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1077 Y-----SEEFGLFEEARKTETGRIEEESKKKEAM--KRAEDARRIEEARRAEDA--RRIEEARRAEDARRVEIARRVEDA 1147
Cdd:TIGR02168 747 EriaqlSKELTELEAEIEELEERLEEAEEELAEAeaEIEELEAQIEQLKEELKAlrEALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1148 RRIEiSRRAEDAKRIEAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARRyEDEKRIEAVKRAEEVRKDEEEAKR 1227
Cdd:TIGR02168 827 ESLE-RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN-ERASLEEALALLRSELEELSEELR 904
|
250 260 270
....*....|....*....|....*....|....*....
gi 914546577 1228 AEKERNNEEIRKFEEAR--MAHFARRQAAIKAEEKRKAD 1264
Cdd:TIGR02168 905 ELESKRSELRRELEELRekLAQLELRLEGLEVRIDNLQE 943
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1086-1190 |
1.45e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 47.09 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1086 EARKTE-TGRIEE-ESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAEDArrvEIARRVEDARRiEISRRAEDAK-RI 1162
Cdd:COG0711 30 DERQEKiADGLAEaERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA---IAEEAKAEAEA-EAERIIAQAEaEI 105
|
90 100 110
....*....|....*....|....*....|
gi 914546577 1163 EAARRAIevrRAELRK--AEDArrIEAARR 1190
Cdd:COG0711 106 EQERAKA---LAELRAevADLA--VAIAEK 130
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1123-1264 |
1.58e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1123 ARRIEEARRAEDARRveiarrvEDARRIEisrrAEDAKRIEAARRAIEvrRAELRKAEDARRIEAARRYENERRIEEARR 1202
Cdd:COG3064 1 AQEALEEKAAEAAAQ-------ERLEQAE----AEKRAAAEAEQKAKE--EAEEERLAELEAKRQAEEEAREAKAEAEQR 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914546577 1203 yEDEKRIEAVKRAEEVRKDEEEakrAEKERNNEEIRKFEEARMAHFARR-----QAAIKAEEKRKAD 1264
Cdd:COG3064 68 -AAELAAEAAKKLAEAEKAAAE---AEKKAAAEKAKAAKEAEAAAAAEKaaaaaEKEKAEEAKRKAE 130
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1085-1221 |
2.05e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.52 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIE--EARRAEDARRIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRI 1162
Cdd:PRK12678 73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEaaPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 914546577 1163 EAARRAievrrAELRKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKD 1221
Cdd:PRK12678 153 ATEARA-----DAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRR 206
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1085-1201 |
2.15e-05 |
|
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: 49.07 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKT--ETGRIEEESKKK---EAMKRAE---DARRIEEARR-AEDARRIEEArrAEDARRVEIARRVEDARRIEISRR 1155
Cdd:TIGR02794 108 EQAAKQaeEKQKQAEEAKAKqaaEAKAKAEaeaERKAKEEAAKqAEEEAKAKAA--AEAKKKAEEAKKKAEAEAKAKAEA 185
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 914546577 1156 AEDAKRIEAARRAIEVRraELRKAEDARRIEAAR----RYENERRIEEAR 1201
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAK--AKAAAEAAAKAEAEAaaaaAAEAERKADEAE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1252 |
2.36e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARR----------------AEDARRVEIARRVEDAR 1148
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplalllspedfLDAVRRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1149 RIEISRRAEDAKRIEAARRAIEVRRAELRKAEDARRiEAARRYENERRIEEARRYEDEKRIEAV-KRAEEVRKDEEEAKR 1227
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELE-EERAALEALKAERQKLLARLEKELAELaAELAELQQEAEELEA 227
|
170 180
....*....|....*....|....*
gi 914546577 1228 AEKERNNEEIRKFEEARMAHFARRQ 1252
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1026-1261 |
2.41e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1026 LKEKEINNEPIDNVNETKINRKSHVnSMERNKpsyKEnEYDQMEKNVEDETYSEEFGLFEEARKT-ETGRIEEESKKKEA 1104
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERL-RREREK---AE-RYQALLKEKREYEGYELLKEKEALERQkEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1105 MKRaedarrieEARRAEDARRIEEARRaedaRRVEIARRVED---ARRIEISRRAEDAK-RIEAARRAIEVRRAELRKAE 1180
Cdd:TIGR02169 254 EKL--------TEEISELEKRLEEIEQ----LLEELNKKIKDlgeEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1181 DARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEiRKFEEARMAHFARRQAAIKAEEK 1260
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREKLEKLKRE 400
|
.
gi 914546577 1261 R 1261
Cdd:TIGR02169 401 I 401
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1007-1200 |
3.01e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1007 SVNIRKIEELTEYgnnddvlkekeINNEPIDNVNETKINRKSHVNSMERN-KPSYKENEYDQMEKNVEDETYSEEFGLFE 1085
Cdd:COG2268 173 SVAITDLEDENNY-----------LDALGRRKIAEIIRDARIAEAEAEREtEIAIAQANREAEEAELEQEREIETARIAE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1086 EARKTETGRIEEESKKKEAMKRAEDARRIEEARRAED-ARRIEEARRaedARRVEIARrvedaRRIEISRRAEDA---KR 1161
Cdd:COG2268 242 AEAELAKKKAEERREAETARAEAEAAYEIAEANAEREvQRQLEIAER---EREIELQE-----KEAEREEAELEAdvrKP 313
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 914546577 1162 IEAARRAIEVR-RAELrkaeDARRIEAARRYENERRIEEA 1200
Cdd:COG2268 314 AEAEKQAAEAEaEAEA----EAIRAKGLAEAEGKRALAEA 349
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1104-1215 |
3.03e-05 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 44.74 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1104 AMKRAEDARRIEEARRaeDARRIEEARRAEDARrveIARRVEdarrieisrraEDAKRIEAARRaiEVRRAELRK-AEDA 1182
Cdd:pfam16999 11 AEREAALDQQIEAARK--EAEREVEAAEAEAAR---ILREAE-----------AKAKALQAEYR--QELAAETARiREEA 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 914546577 1183 R-RIEA---ARRYENERRIEEArryedekrIEAVKRA 1215
Cdd:pfam16999 73 RaRAEAeaqAVRTRAEGRLQQA--------VELILRA 101
|
|
| PTZ00045 |
PTZ00045 |
apical membrane antigen 1; Provisional |
294-485 |
3.64e-05 |
|
apical membrane antigen 1; Provisional
Pssm-ID: 240241 [Multi-domain] Cd Length: 595 Bit Score: 48.83 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 294 CFLPVKKEKGNQWTYASSFIRTDYMTKCpPRFPLNHTMFGyfNYSTGKCETYYMNHEKRTLSFSKCIETLFNN------- 366
Cdd:PTZ00045 271 CFKPDKSKEDNHLLYGSKNVPDDWESKC-PRKPLRNAIFG--LWVDGNCVPIPPVFEVEAESLEECAKIVFENspvasdq 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 367 ------------IKKQDDVNNSSFLWGVWT---IENNANEKT-----NLASMDNT-GSCYFLKKKPTCVLKKENHFSFTI 425
Cdd:PTZ00045 348 ptqyeeltdyekIKEGFKNNNLSMIKSAFLplgSFDSDNYKSkgvgyNWANYDKEsGKCEIFDVVPTCLISDSGYYALTA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914546577 426 L------TAN-SFNLNQNIIYPELKNNSSKEGSSLIHFKDPKQTNKRVLYENNKKSKRNVRTKINSV 485
Cdd:PTZ00045 428 LsspnevDANfPCSIKEKIVLPRIFISTDKDSPFCPATPLKVSNSTCSFYVCERVEKSCGVKENNEV 494
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1085-1255 |
4.89e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAED---ARRIEEARR---------AEDARRI--EEARRAEDARRVEIARRVEDARRI 1150
Cdd:COG3064 90 EKKAAAEKAKAAKEAEAAAAAEKAAAaaeKEKAEEAKRkaeeeakrkAEEERKAaeAEAAAKAEAEAARAAAAAAAAAAA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1151 EISRRAEDAKRIEAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEK 1230
Cdd:COG3064 170 AAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAE 249
|
170 180
....*....|....*....|....*
gi 914546577 1231 ERNNEEIRKFEEARMAHFARRQAAI 1255
Cdd:COG3064 250 EAADLAAVGVLGAALAAAAAGAAAL 274
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1091-1259 |
5.08e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1091 ETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVEIARRVEDARRIEISRRAEDakriEAARRAIE 1170
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQ----ERARQQQE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1171 VRRAELRKAEDARRIEAARRYENERRieeaRRYEDEKRI-EAVKR----AEEVR---KDEEEAKRAEKERNNEEIRKFEE 1242
Cdd:pfam15709 427 EFRRKLQELQRKKQQEEAERAEAEKQ----RQKELEMQLaEEQKRlmemAEEERleyQRQKQEAEEKARLEAEERRQKEE 502
|
170 180
....*....|....*....|
gi 914546577 1243 --ARMA-HFARRQAAIKAEE 1259
Cdd:pfam15709 503 eaARLAlEEAMKQAQEQARQ 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1062-1252 |
5.20e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1062 ENEYDQMEK--NVEDETYSEEFGLFEEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVE 1139
Cdd:COG4717 52 EKEADELFKpqGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1140 IARRVEDARRIEISRRAEDAKR----IEAARRAIEVRRAELRKAE-DARRIEAARRYENERRIEEARRyedekRIEAVKR 1214
Cdd:COG4717 132 QELEALEAELAELPERLEELEErleeLRELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAE-----ELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 914546577 1215 AEEVRKDEEEAKRAEKERNNEEIRKFEEARMAHFARRQ 1252
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1116-1202 |
5.86e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 45.16 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1116 EARRAEDARRIEEARRAE---DARRVEIARRVEDARRiEISRRAEDAKriEAARRAIEVRRAELRkAEDARRIEAArrye 1192
Cdd:COG0711 30 DERQEKIADGLAEAERAKeeaEAALAEYEEKLAEARA-EAAEIIAEAR--KEAEAIAEEAKAEAE-AEAERIIAQA---- 101
|
90
....*....|
gi 914546577 1193 nERRIEEARR 1202
Cdd:COG0711 102 -EAEIEQERA 110
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
1066-1190 |
6.35e-05 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 47.41 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1066 DQMEKNVEDE-TYSEEFGLFEEARKT--------ETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAE--- 1133
Cdd:pfam16021 25 LELRENVEDDsVWSESYSRAAELKHElqekllllEDPELLESLKRKLERRQKKRLRRKRRKEERKEEKKEEQERRAErea 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914546577 1134 --DARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRR--AELRKAEDARRI--EAARR 1190
Cdd:pfam16021 105 kiDKWRRKQIQEVEEKKRERELKLAADAVLSEVRKKQADAKRmlDILRSLEKLRKLrkEAARR 167
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1009-1190 |
7.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1009 NIRKIEELTEYgnnddvLKEKEINNEPIDNVNETKINRKSHVNSMERNKPSyKENEYDQMEKNVEDETYSEEFGLFEEAR 1088
Cdd:COG4717 69 NLKELKELEEE------LKEAEEKEEEYAELQEELEELEEELEELEAELEE-LREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1089 KTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARR----AEDARRVEIARRVEDA--RRIEISRRAEDAK-R 1161
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELqqRLAELEEELEEAQeE 221
|
170 180
....*....|....*....|....*....
gi 914546577 1162 IEAARRAIEVRRAELRKAEDARRIEAARR 1190
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARL 250
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
1106-1251 |
9.41e-05 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 44.74 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1106 KRAEDARRIEEARRAEDAR---RIEEARRAEDARRVEIARRVEDARRIEISRRAEDAK---------------------- 1160
Cdd:pfam09486 1 RRASAWRTLVERRTRRYQRlraELEAARAALAQAEAALAAAQAQAEQARDRVRAHEERlddlttggspfsaadylacray 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1161 ------RIEAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARRyedekRIEAVKRAEEVRKDeeeakraekerNN 1234
Cdd:pfam09486 81 rdvlegRVGAAEAALAAARQALDAAEDAVAATRRKIARNDAQLDVCRE-----RIARLRRAAERARE-----------DA 144
|
170
....*....|....*..
gi 914546577 1235 EEirkfEEARMAHFARR 1251
Cdd:pfam09486 145 AD----EEAEEAALARR 157
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1061-1262 |
1.22e-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: 46.45 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1061 KENEYDQMEKNVEDEtYSEEFglfEEARKtetgRIEEESKKKEAMKRA----EDARRIEEARRAEDARRIEEARRAEDAR 1136
Cdd:pfam13868 96 KLQEREQMDEIVERI-QEEDQ---AEAEE----KLEKQRQLREEIDEFneeqAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1137 RVEIA---RRVEDARRIEISRRAEDAKRIEAARRAIEVRRAElrkaedaRRIEAARRYENERRIEEARRYEDEKRIEAVK 1213
Cdd:pfam13868 168 EEEREaerEEIEEEKEREIARLRAQQEKAQDEKAERDELRAK-------LYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 914546577 1214 RAEEVRkdeeeakraekerNNEEIRKFEEARMAHFARRQAAIKAEEKRK 1262
Cdd:pfam13868 241 REEQIE-------------LKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1062-1175 |
1.57e-04 |
|
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: 43.37 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1062 ENEYDQMEKNVEDETYSEEfGLFEEARKTETGRIEEESKKKEAMkraEDARRIEEARRAEDARRIEEARRAEDARRvEIA 1141
Cdd:pfam20492 19 EEETKKAQEELEESEETAE-ELEEERRQAEEEAERLEQKRQEAE---EEKERLEESAEMEAEEKEQLEAELAEAQE-EIA 93
|
90 100 110
....*....|....*....|....*....|....
gi 914546577 1142 RRVEDARRieisrRAEDAKRIEAarRAIEVRRAE 1175
Cdd:pfam20492 94 RLEEEVER-----KEEEARRLQE--ELEEAREEE 120
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1079-1221 |
1.87e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1079 EEFGLFEEARKTETGRIEEESKKKEAMKRAEDARRIE-EARR-----AEDARR-IEEARRAE----------------DA 1135
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEaEGLRaalagAEMVRKnLEEGSQREleeiqrlhqeqlssltQA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1136 RRVEIARRVEDARRIEIS------RRAEDAKRIEAARRAIEVRRAELRKAEDARR-----IEAARRYENERRIEEARRY- 1203
Cdd:pfam07111 160 HEEALSSLTSKAEGLEKSlnsletKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvtlVESLRKYVGEQVPPEVHSQt 239
|
170 180
....*....|....*....|.
gi 914546577 1204 ---EDEKRIEAVKRAEEVRKD 1221
Cdd:pfam07111 240 welERQELLDTMQHLQEDRAD 260
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1085-1221 |
2.86e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEdaRRIEEAR------RAE-DARRVEIARRVEDARRIEISRRAE 1157
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLE--EQVERLEaeveelEAElEEKDERIERLERELSEARSEERRE 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914546577 1158 DAKRIEAARRAIEVRR--AELRKAEdaRRIEaarryENERRIEEARRYEDE---KRIEAVKRAEEVRKD 1221
Cdd:COG2433 461 IRKDREISRLDREIERleRELEEER--ERIE-----ELKRKLERLKELWKLehsGELVPVKVVEKFTKE 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1094-1263 |
2.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1094 RIEEESK---KKEAMKRAEDARRIEEARRaedarRIEEARRAEDARRVEIARRVEDARRIEisrraedakRIEAARRAIE 1170
Cdd:COG4717 50 RLEKEADelfKPQGRKPELNLKELKELEE-----ELKEAEEKEEEYAELQEELEELEEELE---------ELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1171 VRRAELRKAEDARRIEAARRYENERRIEEARRYED-EKRIEAVKRAE-----------EVRKDEEEAKRAEKERNNEEI- 1237
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEElEERLEELRELEeeleeleaelaELQEELEELLEQLSLATEEELq 195
|
170 180
....*....|....*....|....*....
gi 914546577 1238 ---RKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:COG4717 196 dlaEELEELQQRLAELEEELEEAQEELEE 224
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1066-1217 |
3.06e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1066 DQMEKNVEDETYSEEFGLFEEARKTETGRiEEESKKKEAMKRAEDARRIEEARRAEDARRIEEA-RRAEDARRVEiarRV 1144
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEE-EEIRRLEEQVERLEAEVEELEAELEEKDERIERLeRELSEARSEE---RR 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914546577 1145 EDARRIEISRRAEDAKR----IEAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARRyedekriEAVKRAEE 1217
Cdd:COG2433 460 EIRKDREISRLDREIERlereLEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTK-------EAIRRLEE 529
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1094-1266 |
3.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1094 RIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVEIARRVEDA-RRIEISRR--AEDAKRIEAARRAIE 1170
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeQELAALEAelAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1171 VRRAELRK-------------------AEDARriEAARRYENERRIEEARR------YEDEKRIEAVKRAEEVRKDEEEA 1225
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplalllsPEDFL--DAVRRLQYLKYLAPARReqaeelRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 914546577 1226 KRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEKRKADEL 1266
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1263 |
3.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1106 KRAEDARRIEEARR--AEDARRIEEARRAEDA--RRVEIARRVEDARRIEIsrraeDAKRIEAARRAIEVRRAELRKAED 1181
Cdd:COG4913 611 KLAALEAELAELEEelAEAEERLEALEAELDAlqERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1182 A-RRIEAaRRYENERRIEEARRyEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEK 1260
Cdd:COG4913 686 DlAALEE-QLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
...
gi 914546577 1261 RKA 1263
Cdd:COG4913 764 ERE 766
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1097-1264 |
3.86e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1097 EESKKKEAMKRAEDARRiEEARRAEDARRIEEARRAEDarrvEIARRVEDARRIEisrRAEDAKRIEAARRAIEVRRAEl 1176
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQ-KQAAEQERLKQLEKERLAAQ----EQKKQAEEAAKQA---ALKQKQAEEAAAKAAAAAKAK- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1177 RKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERnnEEIRKFEEARMAHFARRQAAIK 1256
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE--AEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|...
gi 914546577 1257 AEE-----KRKAD 1264
Cdd:PRK09510 227 AAKaaaeaKAAAE 239
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1085-1221 |
4.09e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAmKRAEDARRIEEARRAEDARRIEEARRAEDARRVEIARRV--EDARRIEISRRAEDAKRI 1162
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAA-AARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAaaEAASAPEAAQARERRERG 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1163 EAARRAIEVRRAELRKAEDAR-RIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVRKD 1221
Cdd:PRK12678 135 EAARRGAARKAGEGGEQPATEaRADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE 194
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1085-1221 |
5.79e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.89 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVE---IARRVEDARRIEISRRAE---- 1157
Cdd:PRK12678 135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGErgrREERGRDGDDRDRRDRREqgdr 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914546577 1158 ---DAKRIEAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARR-----YEDEKR----IEAVKRAEEVRKD 1221
Cdd:PRK12678 215 reeRGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRgrrfrDRDRRGrrggDGGNEREPELRED 290
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1095-1261 |
5.96e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1095 IEEESKKKEAMK--RAEDA--RRIEEARRaedaRRIEEARRAEDARRVEIARRVEDARRIEISRRAEdAKRIEAARRAIE 1170
Cdd:pfam15709 325 LEKREQEKASRDrlRAERAemRRLEVERK----RREQEEQRRLQQEQLERAEKMREELELEQQRRFE-EIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1171 VRRAELRKAEDARRIEAARryENERRIEEARR-----YEDEKRIEAVKRAEEvrkdeeeakraekernNEEIRKFEEARM 1245
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQ--ERARQQQEEFRrklqeLQRKKQQEEAERAEA----------------EKQRQKELEMQL 461
|
170
....*....|....*.
gi 914546577 1246 AHFARRQAAIkAEEKR 1261
Cdd:pfam15709 462 AEEQKRLMEM-AEEER 476
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1091-1201 |
6.11e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 44.86 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1091 ETGRIEEESKKKEAMKRAEDA------RRIEEARRAEDArRIEEARRAEDARRVEIAR-RVEDARRIEISRRAEDAKRIE 1163
Cdd:PRK12472 201 DAARAADEAKTAAAAAAREAAplkaslRKLERAKARADA-ELKRADKALAAAKTDEAKaRAEERQQKAAQQAAEAATQLD 279
|
90 100 110
....*....|....*....|....*....|....*...
gi 914546577 1164 AARRAIEVRRAELRKAEDARRIEAARRYENERRIEEAR 1201
Cdd:PRK12472 280 TAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAK 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1086-1264 |
6.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1086 EARKTETGRIEEEskKKEAMKRAEDARRIEEA--RRAEDARRIEEARRAE-DARRVEiaRRVEDARRiEISRRAEDAKRI 1162
Cdd:COG4913 613 AALEAELAELEEE--LAEAEERLEALEAELDAlqERREALQRLAEYSWDEiDVASAE--REIAELEA-ELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1163 EAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARryEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEE 1242
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE--EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
170 180
....*....|....*....|..
gi 914546577 1243 ARMAHFARRQAAIKAEEKRKAD 1264
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEE 787
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1085-1264 |
6.70e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEAR----------RAEDARRV---------------- 1138
Cdd:NF041483 233 EATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARaeaekvvaeaKEAAAKQLasaesaneqrtrtake 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1139 EIARRV-----------EDARRIEISRRAEDAKRI-EAARRAIEV-------------RRAE--LRKA-EDARRIEAARR 1190
Cdd:NF041483 313 EIARLVgeatkeaealkAEAEQALADARAEAEKLVaEAAEKARTVaaedtaaqlakaaRTAEevLTKAsEDAKATTRAAA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1191 YENERRIEEARRYEDEKRIEAVKRAEEVR---KDEEEAKRAEKERNNEEIRKF-------------EEARMAHFARRQA- 1253
Cdd:NF041483 393 EEAERIRREAEAEADRLRGEAADQAEQLKgaaKDDTKEYRAKTVELQEEARRLrgeaeqlraeavaEGERIRGEARREAv 472
|
250 260
....*....|....*....|
gi 914546577 1254 ------AIKAEE---KRKAD 1264
Cdd:NF041483 473 qqieeaARTAEElltKAKAD 492
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
1095-1220 |
7.00e-04 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 43.95 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1095 IEEESKKKEAMKRAEDARR--IEEARRAEDARRIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVR 1172
Cdd:pfam16021 31 VEDDSVWSESYSRAAELKHelQEKLLLLEDPELLESLKRKLERRQKKRLRRKRRKEERKEEKKEEQERRAEREAKIDKWR 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 914546577 1173 RAELRKAEDARRIEAARR------YENERRIEEARRYEDekRIEAVKRAEEVRK 1220
Cdd:pfam16021 111 RKQIQEVEEKKRERELKLaadavlSEVRKKQADAKRMLD--ILRSLEKLRKLRK 162
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
1102-1219 |
7.03e-04 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 44.34 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1102 KEAMKRAEDARRIEEARRAEDARRIEEARRA-----EDARRvEIARRVEDARrieisrraEDAKRIEAARRAIEVRRAEL 1176
Cdd:PRK13428 27 RRLMAARQDTVRQQLAESATAADRLAEADQAhtkavEDAKA-EAARVVEEAR--------EDAERIAEQLRAQADAEAER 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 914546577 1177 RKAEDARRIEAARRyenerriEEARRYEDEKRIEAVKRAEE-VR 1219
Cdd:PRK13428 98 IKVQGARQVQLLRA-------QLTRQLRLELGHESVRQAGElVR 134
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
1113-1219 |
8.27e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 43.67 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1113 RIEEARRAedARRIEEARR-----AEDARRVEIARR-VEDA---RRIEISRRAEDAKRIEAARRAIEVRRAELRKAE--- 1180
Cdd:COG0330 90 RITDPAKF--LYNVENAEEalrqlAESALREVIGKMtLDEVlstGRDEINAEIREELQEALDPYGIEVVDVEIKDIDppe 167
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 914546577 1181 ---DA-RRIEAARRyENERRIEEARRYEDEKRIEAVKRAEEVR 1219
Cdd:COG0330 168 evqDAmEDRMKAER-EREAAILEAEGYREAAIIRAEGEAQRAI 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1264 |
9.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKKKEAMKRAEDARRIE----EARRAEDARRIEEARRAEDARRVEIAR---RVEDARRIEISRRAE 1157
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQlaalERRIAALARRIRALEQELAALEAELAElekEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1158 DAKRIEAARRAIEVRRAEL----RKAEDARRIEAARRYENERRIEEARRYEDE-KRIEAVKRAEEVRKDEEEAKRAEKER 1232
Cdd:COG4942 106 LAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADlAELAALRAELEAERAELEALLAELEE 185
|
170 180 190
....*....|....*....|....*....|..
gi 914546577 1233 NNEEIRKFEEARMAHFARRQAAIKAEEKRKAD 1264
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1112-1263 |
9.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1112 RRIEEARRA--EDARRIEEARRAEDARRVEIARRVEDARRiEISRRAEDakrIEAARRAIEVRRAELRKAEDARRIEAAR 1189
Cdd:COG1579 20 DRLEHRLKElpAELAELEDELAALEARLEAAKTELEDLEK-EIKRLELE---IEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914546577 1190 R--YENERRIEEArryedEKRI-EAVKRAEEVRKDEeeakraekernnEEIRKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:COG1579 96 KeiESLKRRISDL-----EDEIlELMERIEELEEEL------------AELEAELAELEAELEEKKAELDEELAELE 155
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1046-1264 |
9.75e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1046 RKSHVNSMERNKPSYKENEYDQMEKNVEDEtyseefglfEEARKTETGRIEEESKKKEAMKRAEDARriEEARRAEDARr 1125
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQ---------ERLKQLEKERLAAQEQKKQAEEAAKQAA--LKQKQAEEAA- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1126 ieeARRAEDARrveiARRVEDARRIeisrrAEDAKRIEAARRAIEVRRAELRKAEDARRIEAArryenerriEEARRYED 1205
Cdd:PRK09510 139 ---AKAAAAAK----AKAEAEAKRA-----AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEA---------EAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 914546577 1206 EKRIEAVKRAEEVRKDEEeakraekernnEEIRKFEEARMAHFARRQAAIKAEEKRKAD 1264
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEA-----------KKKAAAEAKAAAAKAAAEAKAAAEKAAAAK 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1050-1227 |
1.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1050 VNSMERNKPSYKENEYDQMEKNVEDETYSEEFGLfEEARKTETGRIEE-ESKKKEAMKRAEDA---------RRIEEARR 1119
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGL-ESELAELDEEIERyEEQREQARETRDEAdevleeheeRREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1120 AEDARRIEEARRAEDARRVEIARRVEDARRI------EISRRAEDAKRIEAARRAIEVRRAELRKAEDarrieaarryEN 1193
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERleeleeERDDLLAEAGLDDADAEAVEARREELEDRDE----------EL 326
|
170 180 190
....*....|....*....|....*....|....
gi 914546577 1194 ERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKR 1227
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1096-1219 |
1.30e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1096 EEESKKKEAMKRAeDARRIEEARRAEdaRRIEEARRAEDARRVEIARRVEDARRIEISRRAEDAKRIEAARRAIEVRRAE 1175
Cdd:NF041483 667 EAERLKSEAQESA-DRVRAEAAAAAE--RVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLAS 743
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 914546577 1176 LRKAEDARRIEAARRYenerriEEARRYEDEKRIEAVKRAEEVR 1219
Cdd:NF041483 744 ARKRVEEAQAEAQRLV------EEADRRATELVSAAEQTAQQVR 781
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1108-1263 |
1.60e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1108 AEDARRIEE----ARRAEDARRIEEARRAEDARRvEIARRVEDARRIEISRRAEDAKR---IEAARRAievrRAELRKAE 1180
Cdd:PRK09510 61 VEQYNRQQQqqksAKRAEEQRKKKEQQQAEELQQ-KQAAEQERLKQLEKERLAAQEQKkqaEEAAKQA----ALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1181 DARRIEAAR-----RYENERRIEEARRYEDEKRIEAvkRAEEVRKDEeeakraekernnEEIRKFEEARMAHFARRQAAI 1255
Cdd:PRK09510 136 EAAAKAAAAakakaEAEAKRAAAAAKKAAAEAKKKA--EAEAAKKAA------------AEAKKKAEAEAAAKAAAEAKK 201
|
....*...
gi 914546577 1256 KAEEKRKA 1263
Cdd:PRK09510 202 KAEAEAKK 209
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1094-1202 |
1.97e-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: 39.90 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1094 RIEEESKK-KEAMKRAED-ARRIEE-ARRAEDARRIEEARRAEDARrvEIARRVEDARRIEISRRAEDAKRIEAARRAIE 1170
Cdd:pfam20492 17 QYEEETKKaQEELEESEEtAEELEEeRRQAEEEAERLEQKRQEAEE--EKERLEESAEMEAEEKEQLEAELAEAQEEIAR 94
|
90 100 110
....*....|....*....|....*....|..
gi 914546577 1171 VRRAELRKAEDARRIEAarryenerRIEEARR 1202
Cdd:pfam20492 95 LEEEVERKEEEARRLQE--------ELEEARE 118
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1085-1263 |
1.99e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1085 EEARKTETGRIEEESKK----KEAMKRAEDARRIEEARRAEDAR-------RIEEARRAEDARRVEIARRVEDARRIEIS 1153
Cdd:PRK05035 443 QEKKKAEEAKARFEARQarleREKAAREARHKKAAEARAAKDKDavaaalaRVKAKKAAATQPIVIKAGARPDNSAVIAA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1154 RRAEDAKRIEAARRAIE--------------VRRAELRKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKRAEEVR 1219
Cdd:PRK05035 523 REARKAQARARQAEKQAaaaadpkkaavaaaIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAE 602
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 914546577 1220 KDEEEAKRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:PRK05035 603 PEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1082-1190 |
2.00e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1082 GLFEEARKTETGRIEE-ESKKKEAMKRAEDAR-RIEEARrAEDARRIEEARRAEDARRVEIarrVEDARRiEISRRAEDA 1159
Cdd:cd06503 26 KALDEREEKIAESLEEaEKAKEEAEELLAEYEeKLAEAR-AEAQEIIEEARKEAEKIKEEI---LAEAKE-EAERILEQA 100
|
90 100 110
....*....|....*....|....*....|....
gi 914546577 1160 KR-IEAARRAIevrRAELRK--AEDArrIEAARR 1190
Cdd:cd06503 101 KAeIEQEKEKA---LAELRKevADLA--VEAAEK 129
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1088-1214 |
2.02e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1088 RKTETGRIEEESKKK-EAMKRAEDARRIEEARRAEDARRIEEARRAEDARRVE--IARRVE--DARRIEISRRAEDAKRI 1162
Cdd:PRK12705 31 LAKEAERILQEAQKEaEEKLEAALLEAKELLLRERNQQRQEARREREELQREEerLVQKEEqlDARAEKLDNLENQLEER 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 914546577 1163 EAARRAIEVRRAELRKAEDARRIEAARRYENERRIEEARRYEDEKRIEAVKR 1214
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQR 162
|
|
| Metal_resist |
pfam13801 |
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ... |
1108-1189 |
2.09e-03 |
|
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.
Pssm-ID: 433488 [Multi-domain] Cd Length: 119 Bit Score: 39.97 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1108 AEDARRIEEARRAEDARRIEEARRAEDARRveiarRVEDArrieISRRAEDAKRIEAARRAIEVRRAELRKAEDARRIEA 1187
Cdd:pfam13801 41 AEQRERLRAALRDHARELRALRRELRAARR-----ELAAL----LAAPPFDPAAIEAALAEARQARAALQAQIEEALLEF 111
|
..
gi 914546577 1188 AR 1189
Cdd:pfam13801 112 AA 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1084-1211 |
2.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1084 FEEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAEDARRIEEARRAE-DARRVEIArrvEDARRIEISRRAEDakRI 1162
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAAL---GDAVERELRENLEE--RI 775
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 914546577 1163 EAARRAIEVRRAELRKAedarRIEAARRYENERR-----IEEARRYEDE-KRIEA 1211
Cdd:COG4913 776 DALRARLNRAEEELERA----MRAFNREWPAETAdldadLESLPEYLALlDRLEE 826
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
1112-1221 |
2.74e-03 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 42.60 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1112 RRIEEARRAEDARRIEEARRAEDARRvEIARRVEDARRIEISRRaEDAKRIEAARRAIEVRRAELRKAEDARRIEAARRY 1191
Cdd:TIGR01622 2 YRDRERERLRDSSSAGDRDRRRDKGR-ERSRDRSRDRERSRSRR-RDRHRDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
|
90 100 110
....*....|....*....|....*....|.
gi 914546577 1192 ENERRIE-EARRYEDEKRIEAVKRAEEVRKD 1221
Cdd:TIGR01622 80 GDSYRRRrDDRRSRREKPRARDGTPEPLTED 110
|
|
| AMA-1 |
smart00815 |
Apical membrane antigen 1; Apical membrane antigen 1 (AMA-1) is a Plasmodium asexual ... |
803-906 |
3.00e-03 |
|
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: 41.66 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 803 NLFDCSIYSYCLGPcleNSFGNKCFRnLPAYYNHLTNECVILGTHEQERTNS--CRRTKEEKKKPNCQILRKTTDSKDWT 880
Cdd:smart00815 101 DLSLCAEHASNTVP---GNNKNSKYR-YPFVYDSDDKLCYILYVAAQENQGPryCSNDEEGTSSLFCFKPDKSKEDHHLI 176
|
90 100
....*....|....*....|....*.
gi 914546577 881 YVSSFIRPDYETKCpPRYPLKSKVFG 906
Cdd:smart00815 177 YGSANVGDDWEEVC-PNKPLRNAKFG 201
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1145-1261 |
3.46e-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: 40.02 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1145 EDARRIEISRRA---EDAKRIEAARRAIEvRRAELRKAEDARRI--EAARRYENERRIEEARR--YEDEKRIEAVKRAEE 1217
Cdd:pfam05672 10 EEAARILAEKRRqarEQREREEQERLEKE-EEERLRKEELRRRAeeERARREEEARRLEEERRreEEERQRKAEEEAEER 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 914546577 1218 VRKDEEEAKRAEKERNNEEIRKFEEARMAHFARRQAAIKAEEKR 1261
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQER 132
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1096-1208 |
3.57e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 42.72 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1096 EEESKKKEAMKRAEDARRIEEA--RRAEDARRIEEARRAEDARRVeiARrvEDARRieisRRAEDAKRIEAARRAIEVRR 1173
Cdd:PRK10811 590 EQPAPKAEAKPERQQDRRKPRQnnRRDRNERRDTRDNRTRREGRE--NR--EENRR----NRRQAQQQTAETRESQQAEV 661
|
90 100 110
....*....|....*....|....*....|....*
gi 914546577 1174 AELRKAEDARRieaarryeNERRIEEARRYEDEKR 1208
Cdd:PRK10811 662 TEKARTQDEQQ--------QAPRRERQRRRNDEKR 688
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1096-1190 |
4.76e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1096 EEESKKKEAMKRAEDAR-RIEEARrAEDARRIEEAR-RAEDARRVEIARRVEDARRIEISRRAEdakrIEAAR-RAievr 1172
Cdd:pfam00430 41 EAEERRKDAAAALAEAEqQLKEAR-AEAQEIIENAKkRAEKLKEEIVAAAEAEAERIIEQAAAE----IEQEKdRA---- 111
|
90
....*....|....*...
gi 914546577 1173 RAELRKAEDARRIEAARR 1190
Cdd:pfam00430 112 LAELRQQVVALAVQIAEK 129
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
1094-1212 |
4.82e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 38.74 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1094 RIEEESKKKEAMKRAEDarRIEEARRaEDARRIEEArraedarRVEIARRVEDARRiEISRRAEdaKRIEAARRAIEVRR 1173
Cdd:COG2811 3 RPEVLKEIKEAEEEADE--IIEEAKE-EREERIAEA-------REEAEEIIEQAEE-EAEEEAQ--ERLEEAREEAEAEA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 914546577 1174 AELRKAEDARRIEAARRYENerRIEEARRYEDEKRIEAV 1212
Cdd:COG2811 70 EEIIEEGEKEAEALKKKAED--KLDKAVELLVEEFEEAV 106
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1096-1263 |
5.33e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1096 EEESKKKEAMKRAEDARR-IEEARRaedARRIEEARRAEDARRV-EIARRVEDARRIEISRRAE-------DAKRIEAAR 1166
Cdd:pfam13868 63 KEEERKEERKRYRQELEEqIEEREQ---KRQEEYEEKLQEREQMdEIVERIQEEDQAEAEEKLEkqrqlreEIDEFNEEQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1167 RAIEVRRAELRKAEDARRIEAAR----RYENERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEE 1242
Cdd:pfam13868 140 AEWKELEKEEEREEDERILEYLKekaeREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKE 219
|
170 180
....*....|....*....|.
gi 914546577 1243 ARmahfARRQAAIKAEEKRKA 1263
Cdd:pfam13868 220 RQ----KEREEAEKKARQRQE 236
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1043-1178 |
6.10e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 39.67 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1043 KINRKSHVNSMERNKPSYKENEYDQmEKNVEDETYSEEFGLFEEARKTETGRIEEESKKKEAMKRAEDARRIEEARRAED 1122
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERL-RRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 914546577 1123 ARRIEEARRAEDARRVEIARRvedARRIEISRRAEDAKRIEAARRAIEVRRAELRK 1178
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEAL---EAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1062-1214 |
7.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1062 ENEYDQMEKNVED-----ETYSEEFGLF--EEARKTETGRIEE-ESKKKEA-MKRAEDARRIEEARRAEDARRIEEARRA 1132
Cdd:COG3206 181 EEQLPELRKELEEaeaalEEFRQKNGLVdlSEEAKLLLQQLSElESQLAEArAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1133 EDARRVEIARRVED--ARRIEISRR-AEDAKRIEAARRAIEVRRAELRKAEDARRIEAarryENERRIEEARRYEDEKRI 1209
Cdd:COG3206 261 QSPVIQQLRAQLAEleAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASL----EAELEALQAREASLQAQL 336
|
....*
gi 914546577 1210 EAVKR 1214
Cdd:COG3206 337 AQLEA 341
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1041-1254 |
8.98e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1041 ETKINR-KSHVNSMERNKPSYKENEYD----QMEKNVEDETYSEEFGLFEEARKTETGRIEEESKKKEAMKRAEDARRIE 1115
Cdd:TIGR02168 266 EEKLEElRLEVSELEEEIEELQKELYAlaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1116 EARRAEDARRIEEARRAEDARRVEIARRVEDARR-IEISRRAEDAKRIEAARRAIEVRRAELRK--AEDARRIEAARRYE 1192
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEqLETLRSKVAQLELQIASLNNEIERLEARLerLEDRRERLQQEIEE 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914546577 1193 NERRIEEARRYEDEKRIEAVKRAEEVRKDEEEAKRAEKERNNEEIRKFEEARMAhfARRQAA 1254
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELA 485
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1063-1263 |
9.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1063 NEYDQMEKNVEDETYSEEFGLFEEARKTETGRiEEESKKKEAMKRAEDARRI--EEARRAEDARRI--EEARRAEDARRV 1138
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQ-QKQAAEQERLKQLEKERLAaqEQKKQAEEAAKQaaLKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1139 --EIARRVEDArriEISRRAEDAKRIEAARRAIEVRRAELRKAEDARR---IEAARRYENERRIEEARRYEDEKRIEAVK 1213
Cdd:PRK09510 141 aaAAAKAKAEA---EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAAEAKKKAEAEAKKKAAAEAKK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 914546577 1214 RAEEVRKDEEEAkraekernneeirkfEEARMAHFARRQAAIKAEEKRKA 1263
Cdd:PRK09510 218 KAAAEAKAAAAK---------------AAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| YscO |
pfam07321 |
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ... |
1154-1261 |
9.09e-03 |
|
Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.
Pssm-ID: 399954 [Multi-domain] Cd Length: 148 Bit Score: 38.92 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914546577 1154 RRAEDAKRIEAARRAIEVRRAELRKAEDARRIEAAR----RYENERRIEEARRYE-------DEKRIEAVK------RAE 1216
Cdd:pfam07321 2 RRLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQaslqDYRAWRPQEEQRLYAeiqgklvLLKELEKVKqqvallREN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 914546577 1217 EVRKDEEEAKRAEKERNneEIRKFEEAR-MAHFARRQAAIKAEEKR 1261
Cdd:pfam07321 82 EADLEKQVAEARQQLEA--EREALRQARqALAEARRAVEKFAELVR 125
|
|
|