|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2233 |
0e+00 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 2420.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1 MAVSTQLGLLLWKNFTYRRRQTIQLLVEIIWPLFIFFILISVRLYYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNP 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 81 CFRYPTPGETPGVVGNFNDSIISRLFTDAKKILLYSQQDKS----FEGFKGLVRALRKLQRNTE-----GFKLKDFLHDN 151
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHlgqvWAELRTLSQFMDTLRTHPEriagrGIRIRDILKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 152 ETLSAFLEKNATLPKHAVRQIVEANVNLEKVLIKGFGVHLTDL-CNSTSLEEFVTIADKDVSQLTQNIICQSPADWLNNA 230
Cdd:TIGR01257 161 EALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDIaCSEALLERFIIFSQRRGAQTVRDALCSLSQGTLQWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 231 EQHFLSNLDFLKPIRkdvkSDPKIIKDVSIATDslLESLGALAVELA-SMKSW--RDMRNEILYLTGNSTQS--PNHMYQ 305
Cdd:TIGR01257 241 EDTLYANVDFFKLFH----VLPTLLDSRSQGIN--LRSWGGILSDMSpRIQEFihRPSVQDLLWVTRPLLQNggPETFTQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 306 ---AVSRIVCGHPEGGGLKIKSLNWFEDNNYKALFGNNGNDSDsePASVYDNSSTPYCNNLMKGLESSPISRMIWRALKP 382
Cdd:TIGR01257 315 lmgILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKD--PIYSYDKRTTSFCNALIQSLESNPLTKIAWRAAKP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 383 LLMGKILYTPDTPATQRIIHEVNKTFQELGVLRDLGGMWEEMRPKIWNFMENSEEMDLVRTLLQNNASARFFNAKLSGTE 462
Cdd:TIGR01257 393 LLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQLGEEG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 463 WRVEDVSRFLSKSSEDTRPHG-TAYTWREVFNETDQAIQTISRFMECVNLDKLEPVANEERLVNKSMRLLDDRKFWAGIV 541
Cdd:TIGR01257 473 ITAEAVLNFLYNGPREKQADDmTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 542 FPDMQSNTSDLPLNVNYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDLRYIWGGFTYLQDVIEHGIIRALTGSKEKTGV 621
Cdd:TIGR01257 553 FPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPVGI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 622 YIQQMPYPCYVDDIFLRVMSRSMPLFMTLAWMYSVAIIIKGVVYEKEARLKETMRIMGLDNGILWLSWFISSLIPLLISA 701
Cdd:TIGR01257 633 YLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSI 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 702 ALLVLILKMGNLLPYSDPGVIYLFLSSFAVVTIMQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQNYVGFGAKI 781
Cdd:TIGR01257 713 FLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKT 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 782 VVSLLSPVAFGFGCEYFALFEEQGVGIQWSNLLSSPMQEDSYNLTTSICLMLFDSVLYAVMTWYIEAVFPGQYGIPRPWY 861
Cdd:TIGR01257 793 AVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWY 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 862 FPFTKSYWCG-EKCgwttsvpSNRKENA----EAVCIE-EEPAHID---------------PGVYIENLMKIYS-NGKVA 919
Cdd:TIGR01257 873 FLLQESYWLGgEGC-------STREERAlektEPLTEEmEDPEHPEgindsfferelpglvPGVCVKNLVKIFEpSGRPA 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIW 999
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1000 FYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLL 1079
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1080 KYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKTQLGTGYYLTLVKKDFDLSASSCRTSSSTVSYSKGsl 1159
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGTCSCTSKG-- 1183
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1160 kkddsvSESSSDAGLGSDHESETTTIDISLISNVIFKHVPTARLVEDLGHEITYVLPYESAKDGAFVELFHEIDDRLTDL 1239
Cdd:TIGR01257 1184 ------FSTRCPARVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADL 1257
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1240 SISSYGISDTTLEEIFLKVAEDCGVDAETSDGTlparRNRRHAFGDHQSCLKPFTEDDFDFNDSEGDPESRETDWLDGA- 1318
Cdd:TIGR01257 1258 GLSSFGISDTPLEEIFLKVTEDADSGSLFAGGA----QQKRENANLRHPCSGPTEKAGQTPQASHTCSPGQPAAHPEGQp 1333
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1319 ----DGKGSYQVKGWSLKRQQFVALLWKRLLYARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLALEPSMYEEQ 1394
Cdd:TIGR01257 1334 ppepEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQ 1413
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1395 FTFISNDAPEDRHTNRLLDALKDSPAYTDQCTDGKNTASRSCpIKDGEWLVPEVTESIEAIFLNGNWSMENPSPLCECSC 1474
Cdd:TIGR01257 1414 YTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEEWLPEYPC-GNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCST 1492
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1475 EGRKKMLPECPPGAGGLPPPQIKVTHDETLQNLSGRNISDYLVKTYAQIIGKSLKNKLWVNEFRYGGFSLGARNTQALPP 1554
Cdd:TIGR01257 1493 REKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPIT 1572
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1555 GDELTDAISHIRSRFSLESGTAADRFLGSLSTFIRGLDTNNNVKIWFNNKGWHSIGSFLNVMNNAVLRANLPPGLDRSKF 1634
Cdd:TIGR01257 1573 GEALVGFLSDLGQMMNVSGGPVTREASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEY 1652
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1635 GINAFNHPLNLTKEQLSHVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVNKAKHMQFISGVQPFLYWLANFVWDM 1714
Cdd:TIGR01257 1653 GITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDI 1732
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1715 CNYIVPATLVIIIFVCFQQEAYVSSTNLPVLALLLLLYGWSITPLMYPASFFFKIPSTAYVVLTSVNILIGINGSVSTFV 1794
Cdd:TIGR01257 1733 MNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFV 1812
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1795 LELFGSNE-IGGINDILKNVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFRSPLAWDMVGKNLFAMAIEGVIFFSI 1873
Cdd:TIGR01257 1813 LELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLL 1892
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1874 TVLIQYRFCIKARSLSTKLKPIGEEDEDVARERQRILGGGGQTDILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLG 1953
Cdd:TIGR01257 1893 TLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLG 1972
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1954 VNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVAD 2033
Cdd:TIGR01257 1973 VNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVAN 2052
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2034 WGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEE 2113
Cdd:TIGR01257 2053 WSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2132
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2114 CEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGYTIILRVAGAD----PRLEPVMEFIERELPGSTLKEKHRNMLQYQLSS 2189
Cdd:TIGR01257 2133 CEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSS 2212
|
2250 2260 2270 2280
....*....|....*....|....*....|....*....|....
gi 827475625 2190 SltSLARIFNILSKNKEQLHIEDYSVSQTTLDQVFVNFAKDQSD 2233
Cdd:TIGR01257 2213 S--SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTE 2254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1919-2139 |
1.82e-114 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 362.21 E-value: 1.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSiIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2139
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
904-1122 |
2.03e-113 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 359.13 E-value: 2.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNG-KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVC 982
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1063 TAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLK 1122
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
906-1117 |
6.04e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 272.32 E-value: 6.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:COG1131 3 VRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:COG1131 82 PALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG1131 162 LDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1919-2142 |
4.78e-78 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 258.46 E-value: 4.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKF 2142
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
906-1112 |
1.01e-63 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 214.57 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:cd03230 3 VRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIwfyarlkglsaekvksemeqivmdlglphkrtsrsnQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03230 82 PSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03230 126 LDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
906-1112 |
1.14e-63 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 217.42 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG4555 163 LDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1919-2139 |
7.48e-62 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 211.46 E-value: 7.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03265 1 IEVENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2079 TTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2139
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
906-1122 |
1.40e-61 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 210.69 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:cd03265 3 VENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03265 82 LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1066 VDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLK 1122
Cdd:cd03265 162 LDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1934-2227 |
2.40e-61 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 213.02 E-value: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1934 PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYCPQFDAINDLLTGREH 2013
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2014 LEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNC 2093
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2094 ILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGYTIILRVAGADPRLEPVMEFIERELPGS 2173
Cdd:TIGR01188 167 IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIAELGETGL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2174 TLKEKHRNMLQYQLSSSLTS--LARIFNILSKNKeqLHIEDYSVSQTTLDQVFVNF 2227
Cdd:TIGR01188 247 GLLAVTVDSDRIKILVPDGDetVPEIVEAAIRNG--IRIRSISTERPSLDDVFLKL 300
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
911-1126 |
3.99e-58 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 203.78 E-value: 3.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 911 KIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFS 990
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 991 MLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYA 1070
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1071 RRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKTQLG 1126
Cdd:TIGR01188 160 RRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1919-2144 |
3.20e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 195.85 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGD 2144
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1919-2129 |
4.22e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 193.00 E-value: 4.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKqkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEfyailrgvpekevckvadwgirklglmkyvdkaagsYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
906-1112 |
4.66e-53 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 185.86 E-value: 4.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGqITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:cd03264 3 LENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1066 VDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
906-1111 |
4.22e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 183.39 E-value: 4.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNgKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDlnaIRQNLGVCPQH 985
Cdd:COG4152 4 LKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:COG4152 160 LDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
906-1117 |
1.15e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 179.45 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQ 984
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 H--NVLFsMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:COG1122 83 NpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1063 TAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
906-1111 |
2.27e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 174.96 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR-TDLNAIRQNLGVCP 983
Cdd:cd03225 2 LKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QH-NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1063 TAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1918-2133 |
7.34e-48 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 171.01 E-value: 7.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKP--AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNM 1995
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
904-1116 |
1.67e-47 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 170.24 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLG 980
Cdd:cd03266 2 ITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILD 1060
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1061 EPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1919-2130 |
1.24e-45 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 164.29 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGeCFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2079 TTGMDPKARRALWNcILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2130
Cdd:cd03264 158 TAGLDPEERIRFRN-LLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
904-1111 |
6.68e-45 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 162.45 E-value: 6.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNgKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTdlnAIRQNLGVCP 983
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1064 AGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd03269 157 SGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
920-1064 |
3.48e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.81 E-value: 3.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQHNVLFSMLTVEEHI 998
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 999 WFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSR----SNQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1064
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
906-1112 |
4.30e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 159.99 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQH 985
Cdd:cd03259 3 LKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1066 VDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03259 161 LDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1918-2233 |
1.39e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 161.81 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEIDEVH-QNMG 1996
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE----PLDPEDrRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLD 2076
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2077 EPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGdGYTIILRVAGAD 2156
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2157 PRLepvmefieRELPGSTLKEKHRNMLQYQLSSSlTSLARIFNILSknkEQLHIEDYSVSQTTLDQVFVNFAKDQSD 2233
Cdd:COG4152 234 GWL--------RALPGVTVVEEDGDGAELKLEDG-ADAQELLRALL---ARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
906-1117 |
1.40e-43 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 159.20 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSnGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQNLGV 981
Cdd:cd03261 3 LRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMLTVEEHIWFYARLKGlsaEKVKSEMEQIVMD----LGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLREHT---RLSEEEIREIVLEkleaVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
906-1117 |
1.59e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 159.39 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR-TDLNAIRQNLGVCPQ 984
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLP--HKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03295 83 QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1063 TAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
901-1117 |
2.96e-43 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 158.60 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIR 976
Cdd:COG1127 3 EPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 QNLGVCPQHNVLFSMLTVEEHIWFYAR-LKGLSaekvKSEMEQIVMD----LGLPHKRTSRSNQLSGGMQRKLSVALAFV 1051
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLReHTDLS----EAEIRELVLEklelVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1052 GGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
906-1112 |
3.00e-43 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 157.38 E-value: 3.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQH 985
Cdd:cd03268 3 TNDLTKTYGKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSaekvKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03268 157 LDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
906-1104 |
1.80e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 154.94 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:COG4133 5 AENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGL--SAEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:COG4133 84 DGLKPELTVRENLRFWAALYGLraDREAIDEALEA----VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 1064 AGVDPYARRGIWDLLLKYR-QGRTIILSTHhmDEADILGDRI 1104
Cdd:COG4133 160 TALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
904-1112 |
3.03e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 154.96 E-value: 3.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIR 976
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 -QNLGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADiLGDRIAIISHGKL 1112
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1919-2128 |
5.33e-42 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 153.91 E-value: 5.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIdEVHQNMGYC 1998
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVadwgIRKLGLMKYVDKAAGSYSGGnMR-KLSTAMALIGGPPVVFLDE 2077
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLG-MKqRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2078 PTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1912-2128 |
8.59e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 156.89 E-value: 8.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1912 GGGQTDILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEV 1991
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1992 HQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2072 VVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1919-2109 |
1.25e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.94 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVykRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:COG4133 3 LEAENLSCR--RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVcKVADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE-AIDEA-LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
906-1108 |
3.09e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 149.16 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG---KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrtdlNAIRQNLGVC 982
Cdd:cd03293 3 VRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1063 TAGVDPYARRGIWDLLLK--YRQGRTIILSTHHMDEADILGDRIAIIS 1108
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
906-1111 |
1.14e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.08 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQ 984
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 hnvlfsmltveehiwfyarlkglsaekvksemeqivmdlglphkrtsrsnqLSGGMQRKLSVALAFVGGSKVVILDEPTA 1064
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1065 GVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd00267 110 GLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
901-1112 |
1.38e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.50 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYSNGKV---AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLN 973
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIR-QNLGVCPQ-HNvLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFV 1051
Cdd:COG1136 82 RLRrRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1052 GGSKVVILDEPTAGVDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADIlGDRIAIISHGKL 1112
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
906-1111 |
1.72e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 149.96 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNgKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQH 985
Cdd:PRK13537 10 FRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:PRK13537 89 DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1066 VDPYARRGIWDLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK13537 169 LDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
901-1110 |
2.25e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 148.31 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIY---SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRtdlnAIRQ 977
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMLTVEEHIWFYARLKGLSaekvKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVP----KAERRERARELlelvGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHG 1110
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1919-2133 |
2.44e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 143.58 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlteIDEVHQNMGYC 1998
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
916-1111 |
2.53e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 147.67 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVE 995
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 1076 DLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK13536 213 ERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
906-1112 |
1.19e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 142.33 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQN 978
Cdd:cd03258 4 LKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1059 LDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1920-2128 |
6.90e-37 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 139.14 E-value: 6.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL-TEIDEVHQNMGYC 1998
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQF-DA--INDllTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03225 81 FQNpDDqfFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
906-1112 |
7.31e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.42 E-value: 7.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLNAIRQNLG 980
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQ-HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:COG2884 83 VVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1060 DEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
915-1117 |
1.05e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 140.18 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMLT 993
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEE--------HIWFYARLKGLSAEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:COG1120 92 VRElvalgrypHLGLFGRPSAEDREAVEEALER----TGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1066 VDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG1120 168 LDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
906-1117 |
1.14e-36 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 139.49 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCP-- 983
Cdd:cd03219 3 VRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEE------HIWFYARLKGLSAEKVKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:cd03219 82 QIPRLFPELTVLEnvmvaaQARTGSGLLLARARREEREARERAEELlervGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1919-2128 |
1.15e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.05 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:PRK13536 42 IDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
906-1118 |
1.55e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 146.97 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIY----SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLNAIRQ 977
Cdd:COG1123 263 VRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQH--NVLFSMLTVEEHIWFYARLKGLSAekvKSEMEQIVMDL----GLPHKRTSRS-NQLSGGMQRKLSVALAF 1050
Cdd:COG1123 343 RVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLS---RAERRERVAELlervGLPPDLADRYpHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1051 VGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
906-1111 |
1.92e-36 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 136.93 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQNLGVC 982
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIwfyarlkglsaekvksemeqivmdlGLPhkrtsrsnqLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03229 82 FQDFALFPHLTVLENI-------------------------ALG---------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1063 TAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd03229 128 TSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
906-1113 |
3.96e-36 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 137.28 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNgKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIrqnlGVCPQH 985
Cdd:cd03235 2 VEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----GYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 -NVLFSM-LTVEE--------HIWFYARLKGLSAEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:cd03235 77 rSIDRDFpISVRDvvlmglygHKGLFRRLSKADKAKVDEALER----VGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLC 1113
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
904-1117 |
6.68e-36 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 137.37 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCP 983
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEEHIWFYARLKGLS----AEKVKSEMEQIVMDlGLPHKRTSrsnQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPkaeiKERVAEALDLVQLE-GYANRKPS---QLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1060 DEPTAGVDPYARRgiwDLLLKYRQ-----GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:cd03300 155 DEPLGALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
881-1111 |
6.81e-36 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 149.12 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 881 PSNRKENAEAVCIEEEPAHIDPGVYIE--NL-MKIysnGK-VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP 956
Cdd:NF033858 242 PEEKRRGHQPVVIPPRPADDDDEPAIEarGLtMRF---GDfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 957 TSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQL 1036
Cdd:NF033858 319 SEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1037 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADiLGDRIAIISHGK 1111
Cdd:NF033858 399 PLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
906-1116 |
7.47e-36 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 137.08 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGfyEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQH 985
Cdd:cd03299 3 VENLSKDWKEFKLKNVSLEVE--RGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1066 VDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
904-1111 |
1.93e-35 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 133.66 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGV 981
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMlTVEEHIwfyarlkglsaekvksemeqivmdlglphkrtsrsnqLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1062 PTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGK 1111
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
906-1118 |
3.39e-35 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 134.98 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA-IRQNLGVC-- 982
Cdd:cd03218 3 AENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMhKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1063 TAGVDPYARRGIWDLLLKYRQgRTI-ILST-HHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKD-RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
906-1112 |
4.52e-35 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 134.56 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQN 978
Cdd:cd03257 4 VKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQhNVLFSM---LTVEEHIW--FYARLKGLSAEKVKSEMEQIVMDLGLPHKR-TSRSNQLSGGMQRKLSVALAFVG 1052
Cdd:cd03257 84 IQMVFQ-DPMSSLnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1053 GSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
906-1118 |
5.68e-35 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 134.71 E-value: 5.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA-IRQNLGV--C 982
Cdd:TIGR04406 4 AENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPMhERARLGIgyL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIwfYARL---KGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:TIGR04406 82 PQEASIFRKLTVEENI--MAVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1060 DEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
918-1112 |
6.81e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 135.17 E-value: 6.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAI-RQNLGVCP--QHNVLFSMLTV 994
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHrIARLGIARtfQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHI-----------WFYARLKGLSAEKVKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:COG0411 97 LENVlvaaharlgrgLLAALLRLPRARREEREARERAEELlervGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1060 DEPTAGVDPYARRGIWDLLLKYR--QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
901-1114 |
1.43e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIrqnlG 980
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI----G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQH-NVLFSM-LTVEE--------HIWFYARLKGLSAEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAF 1050
Cdd:COG1121 79 YVPQRaEVDWDFpITVRDvvlmgrygRRGLFRRPSRADREAVDEALER----VGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1051 VGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCC 1114
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
906-1118 |
1.95e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 133.23 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLN----AiRQNLGV 981
Cdd:COG1137 6 AENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPmhkrA-RLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1062 PTAGVDPYARRGIWDLLLKYRQgRTI-ILST-HHMDEadILG--DRIAIISHGKLCCVGSS 1118
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRE--TLGicDRAYIISEGKVLAEGTP 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1919-2128 |
2.37e-34 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 132.46 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYkRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE-IDEVHQNMGY 1997
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQfDAINDLL--TGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:COG1122 80 VFQ-NPDDQLFapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
906-1112 |
1.26e-33 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 130.38 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLmKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP-----PTSGTAYIQGKDIRT---DLNAIRQ 977
Cdd:cd03260 3 LRDL-NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldvDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMlTVEEHIWFYARLKGlsaEKVKSEMEQIVMDL----GLPH--KRTSRSNQLSGGMQRKLSVALAFV 1051
Cdd:cd03260 82 RVGMVFQKPNPFPG-SIYDNVAYGLRLHG---IKLKEELDERVEEAlrkaALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1052 GGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
919-1111 |
1.28e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.25 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA---IRQNLGVCPQHNVLFSMLTVE 995
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPherARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLkgLSAEKVKSEMEQIVmDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRG 1073
Cdd:cd03224 94 ENLLLGAYA--RRRAKRKARLERVY-ELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 827475625 1074 IWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd03224 171 IFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
907-1112 |
2.68e-33 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 129.06 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQNLGVC 982
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLS----AEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPpreiRKRVPAALEL----VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1059 LDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
906-1111 |
2.98e-33 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 130.00 E-value: 2.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLNAIRQNLGV 981
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQH-----------NVL-------------FSMLTVEEhiwfyaRLKGLSA-EKVksemeqivmdlGLPHKRTSRSNQL 1036
Cdd:cd03256 83 IFQQfnlierlsvleNVLsgrlgrrstwrslFGLFPKEE------KQRALAAlERV-----------GLLDKAYQRADQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1037 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1918-2223 |
3.95e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 132.13 E-value: 3.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKP-------------------AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAY 1978
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1979 LAG-------NSVLTEIDEVhqnMGycpQ-----FDaindlLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVD 2046
Cdd:COG4586 81 VLGyvpfkrrKEFARRIGVV---FG---QrsqlwWD-----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2047 KAAgsysggnmRKLS--------TAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEAL 2117
Cdd:COG4586 150 TPV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2118 CTRMAIMVNGRFRCLGSVQHLKNKFGDGYTIILRVAgadprlEPVMEFierELP-GSTLKEKHRNMLQYQLSSSlTSLAR 2196
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELA------EPVPPL---ELPrGGEVIEREGNRVRLEVDPR-ESLAE 291
|
330 340
....*....|....*....|....*..
gi 827475625 2197 IFNILSknkEQLHIEDYSVSQTTLDQV 2223
Cdd:COG4586 292 VLARLL---ARYPVRDLTIEEPPIEEV 315
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
913-1097 |
8.37e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.77 E-value: 8.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQNLGVCPQH--NV 987
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 988 LFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:TIGR01166 81 LFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 827475625 1068 PYARRGIWDLLLKYR-QGRTIILSTHHMDEA 1097
Cdd:TIGR01166 160 PAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1920-2128 |
1.30e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.05 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGYC 1998
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFdaindlltgrehlefyailrgvpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
894-1117 |
1.32e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 135.66 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 894 EEEPAHIDPGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DL 972
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 973 NAIRQNLGVCPQHNVLFSMlTVEEHIWFYARlkGLSAEKV-----KSEMEQIVMDL--GLPHKRTSRSNQLSGG-MQRkL 1044
Cdd:COG4988 407 ASWRRQIAWVPQNPYLFAG-TIRENLRLGRP--DASDEELeaaleAAGLDEFVAALpdGLDTPLGEGGRGLSGGqAQR-L 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1045 SVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGS 1117
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
906-1116 |
2.18e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.24 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQ 984
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 hnvlfsmltveehiwfyarlkglsaekvksemeqiVMD-LGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:cd03214 81 -----------------------------------ALElLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1064 AGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03214 126 SHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
918-1116 |
2.72e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 128.14 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQN-LGVCPQHNVLFSML 992
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARR 1072
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1073 GIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03294 198 EMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
904-1116 |
4.46e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 125.44 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNgKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCP 983
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1064 AGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03301 159 SNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
901-1112 |
5.14e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.10 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYSNGKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYIQGKDIRTDLNAIR 976
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 -QNLGVCPQH-NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGS 1054
Cdd:COG1123 82 gRRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
906-1117 |
1.06e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.00 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG----KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQN 978
Cdd:PRK13637 5 IENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVC---PQHNvLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKR-TSRSN-QLSGGMQRKLSVALAFVGG 1053
Cdd:PRK13637 85 VGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDyKDKSPfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
915-1112 |
1.09e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.46 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlT 993
Cdd:COG4619 11 GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPALWGG-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEEHI--WFYARLKGLSAEKVKSEMEQivmdLGLPH----KRTSRsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:COG4619 90 VRDNLpfPFQLRERKFDRERALELLER----LGLPPdildKPVER---LSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1068 PYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG4619 163 PENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1594-1876 |
1.11e-30 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 125.58 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1594 NNNVKIWFNNKGWHSIGSFLNVMNNAVLRANLPPGLDRSKFGINAFNHPLNLTKEQLShvalMTTSVDVLVSICVIFAMS 1673
Cdd:pfam12698 98 SATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNP----QSGYAYYLVGLILMIIIL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1674 FVPASFVVFLIQERVNKAKHMQFISGVQPFLYWLANFVWDMCNYIVPatLVIIIFVCFQqeAYVSSTNLPVLALLLLLYG 1753
Cdd:pfam12698 174 IGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ--LLIILLLLFG--IGIPFGNLGLLLLLFLLYG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1754 WSITPLMYPASFFFKIPSTAYVVLTSVNILIGINGSVSTFvlelfgsneIGGINDILKNVFLIFPHFCLGRGLIDMVKNQ 1833
Cdd:pfam12698 250 LAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFP---------LEDPPSFLQWIFSIIPFFSPIDGLLRLIYGD 320
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 827475625 1834 AMADalerfgenrfrsplawdmVGKNLFAMAIEGVIFFSITVL 1876
Cdd:pfam12698 321 SLWE------------------IAPSLIILLLFAVVLLLLALL 345
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
919-1131 |
1.24e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 129.89 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEH 997
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 998 IwfyaRL--KGLSAEKVKSEMEQI-----VMDL--GL-----PHKRtsrsnQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:COG4987 429 L----RLarPDATDEELWAALERVglgdwLAALpdGLdtwlgEGGR-----RLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1064 AGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKTQLGTGYYL 1131
Cdd:COG4987 500 EGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
901-1117 |
2.65e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYSNG-KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD-LNAIRQN 978
Cdd:PRK13632 5 SVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQH-NVLFSMLTVEEHIWFyarlkGLSAEKVK-SEMEQIVMDLGL-----------PHKrtsrsnqLSGGMQRKLS 1045
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDIAF-----GLENKKVPpKKMKDIIDDLAKkvgmedyldkePQN-------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1046 VALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGR--TIILSTHHMDEAdILGDRIAIISHGKLCCVGS 1117
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1919-2128 |
3.39e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 119.93 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEidEVHQ-NMGY 1997
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERrNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDE 2077
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2078 PTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
917-1112 |
3.74e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 120.90 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLG-VCPQHNVLFSMLTVE 995
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 827475625 1076 DLLLKYRQGR--TIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03267 194 NFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
903-1117 |
5.08e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.52 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 903 GVYIENLMKIYSNGkVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVC 982
Cdd:cd03296 2 SIEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1059 LDEPTAGVDPYARRGI--WDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:cd03296 160 LDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1919-2140 |
1.11e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 119.46 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVY---KrkqkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE-------- 1987
Cdd:cd03219 1 LEVRGLTKRFgglV-----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppheiarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 -IDEVHQNMGYCPQFDAINDLLTGREHLEFYAILRGVP---EKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTA 2063
Cdd:cd03219 76 gIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARArreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
916-1111 |
1.19e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.32 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA---IRQNLGVCPQHNVLFSM 991
Cdd:COG0410 14 GGIhVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPhriARLGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 LTVEEH--IWFYARlkgLSAEKVKSEMEQiVMDLgLPH---KRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:COG0410 93 LTVEENllLGAYAR---RDRAEVRADLER-VYEL-FPRlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1067 DPYARRGIWDLL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:COG0410 168 APLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
922-1112 |
1.82e-29 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 118.53 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYIQGKDIRTDLnaIRQNLGVCPQHNVLFSMLTVEEHI 998
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 999 WFYARLKG--LSAEKVKSEMEQIVM--DLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:cd03234 103 TYTAILRLprKSSDAIRKKRVEDVLlrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 1075 WDLLLKY-RQGRTIILSTHHmDEADI--LGDRIAIISHGKL 1112
Cdd:cd03234 183 VSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1919-2140 |
2.45e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 118.41 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTeiDEVHQ----N 1994
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--LPMHKrarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
906-1112 |
2.54e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.60 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKvAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNAIRqnLGVcp 983
Cdd:cd03216 3 LRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARR--AGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 qhnvlfsmltveehiwfyarlkglsaekvksemeQIVMdlglphkrtsrsnQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:cd03216 78 ----------------------------------AMVY-------------QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1064 AGVDPYARRGIWDLL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03216 111 AALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
901-1117 |
2.69e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNAIRQN 978
Cdd:COG3845 3 PPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQHNVLFSMLTVEEHIWFYA---RLKGLSAEKVKSEMEQIVMDLGL---PHKRTSrsnQLSGGMQRKLSVALAFVG 1052
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLdvdPDAKVE---DLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1053 GSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLccVGS 1117
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1918-2137 |
3.80e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 3.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKqkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlTEIDEVHQNMGY 1997
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQFDAINDL--LTGRE--------HLEFyaiLRGVPEKEVCKVADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:COG1121 80 VPQRAEVDWDfpITVRDvvlmgrygRRGL---FRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLGSVQH 2137
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
908-1112 |
4.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 908 NLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD---LNAIRQNLGVCPQ 984
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 H--NVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:PRK13639 86 NpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1063 TAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
896-1112 |
7.57e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 125.72 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 896 EPAHIDPGVYIENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLN 973
Cdd:COG2274 466 SLPRLKGDIELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIRQNLGVCPQHNVLFSMlTVEEHIWFYArlKGLSAEKV-----KSEMEQIVMDL--GLPHKRTSRSNQLSGGMQRKLSV 1046
Cdd:COG2274 546 SLRRQIGVVLQDVFLFSG-TIRENITLGD--PDATDEEIieaarLAGLHDFIEALpmGYDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1047 ALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTH---HMDEAdilgDRIAIISHGKL 1112
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRI 687
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
906-1112 |
8.05e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.80 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQN 978
Cdd:COG1135 4 LENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQH-NvLFSMLTVEEHIWFYARLKGLSaekvKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:COG1135 84 IGMIFQHfN-LLSSRTVAENVALPLEIAGVP----KAEIRKRVAELlelvGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
904-1117 |
1.76e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.41 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCP 983
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEEHIWFYARLKGLSaekvKSEMEQIVMD----LGLPHKRTSRSNQLSGG-MQRklsVAL--AFVGGSKV 1056
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVP----KAEIDRRVREaaelLGLEDLLDRKPKQLSGGqRQR---VALgrALVREPKV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1057 VILDEPTAGVDPYARrgiWDL------LLKyRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG3839 155 FLLDEPLSNLDAKLR---VEMraeikrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1943-2080 |
3.83e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 111.97 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL-TEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILR 2021
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2022 GVPEKEVCKVADWGIRKLGLM----KYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTT 2080
Cdd:pfam00005 88 GLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
912-1139 |
5.72e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.03 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 912 IYSNG----KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQG---------KDIRTdlnaIRQN 978
Cdd:PRK13646 11 TYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRP----VRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQ--HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSN-QLSGGMQRKLSVALAFVGGSK 1055
Cdd:PRK13646 87 IGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKTQLGTGYYL 1131
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkELFKDKKKLADWHI 245
|
250
....*....|...
gi 827475625 1132 TL-----VKKDFD 1139
Cdd:PRK13646 246 GLpeivqLQYDFE 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
917-1112 |
5.80e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 117.11 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLG-VCPQHNVLFSMLTVE 995
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGvVFGQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:COG4586 115 DSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 1075 WDLLLKYRQ--GRTIILSTHHMDeaDI--LGDRIAIISHGKL 1112
Cdd:COG4586 194 REFLKEYNRerGTTILLTSHDMD--DIeaLCDRVIVIDHGRI 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
904-1112 |
6.36e-28 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 113.39 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQNLG 980
Cdd:cd03262 1 IEIKNLHKSFGDFHV-LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQHNVLFSMLTVEEHIWFYAR-LKGLSaekvKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIkVKGMS----KAEAEERALELlekvGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
900-1111 |
8.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 8.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 900 IDPGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQN 978
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQ--HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK13647 81 VGLVFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
907-1112 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.31 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNG----KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD-----LNAIRQ 977
Cdd:PRK13641 6 ENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQ--HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSN-QLSGGMQRKLSVALAFVGGS 1054
Cdd:PRK13641 86 KVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1918-2136 |
1.28e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 113.99 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNM 1995
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-LASLSrrELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGRE--------HLEFYailrGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:COG1120 78 AYVPQEPPAPFGLTVRElvalgrypHLGLF----GRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2136
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1919-2128 |
2.76e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 111.81 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKR--KQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIDEVH-- 1992
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 -QNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2072 VVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEEcEALCTRMAIMVNGR 2128
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
907-1133 |
3.28e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQH 985
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 --NVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:PRK13652 87 pdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1064 AGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKTQLGTGYYLTL 1133
Cdd:PRK13652 166 AGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHLDL 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1919-2128 |
3.45e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 112.04 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQK-------------------PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYL 1979
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1980 AGNSVLTEIDEVHQNMGYCpqFDAINDL---LTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGN 2056
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVV--FGQKTQLwwdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2057 MRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1916-2138 |
3.50e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.47 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG---DSVVTSGEAYLAGNSVLTEIDEVH 1992
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 -QNMGYCPQ-FDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGP 2070
Cdd:COG1123 82 gRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2071 PVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
906-1112 |
4.37e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.81 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRtdLNAIRQNLGVCPQH 985
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 -NVLFSMLTVEEHIWFYARLKGLSAEKVksemEQIVMDLGL--PHKRTSRSnqLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03226 80 vDYQLFTDSVREELLLGLKELDAGNEQA----ETVLKDLDLyaLKERHPLS--LSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1063 TAGVDPYARRGIWDLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03226 154 TSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
913-1133 |
8.49e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 8.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQNLGVCPQH--NV 987
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 988 LFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:PRK13636 95 LFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1068 PYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG--SSLFLKTQLGTGYYLTL 1133
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRL 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1918-2128 |
9.37e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 111.67 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVY---KrkqkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIde 1990
Cdd:COG0411 4 LLEVRGLTKRFgglV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphRI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VH-------QNMGYCPQFDAINDLLTGREHLEFYAILRGV--------PEKEVCKVADWGIRKLGLMKYVDKAAGSYSGG 2055
Cdd:COG0411 77 ARlgiartfQNPRLFPELTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2056 NMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
927-1124 |
1.20e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 927 FYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-----RTDLNAIRQNLGVC---PQHNvLFSMlTVEEHI 998
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKPLRKKVGIVfqfPEHQ-LFEE-TVEKDI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 999 WFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSN-QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDL 1077
Cdd:PRK13634 108 CFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1078 L--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKTQ 1124
Cdd:PRK13634 188 FykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPD 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
916-1112 |
2.37e-26 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 107.90 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD--LNAIRQNLGVCP---QHNVLFS 990
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRAGIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 991 MLTVEEHIwfyarlkglsaekvksemeqivmdlglphkrtSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYA 1070
Cdd:cd03215 92 DLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 1071 RRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03215 140 KAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
906-1112 |
4.36e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.82 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGK---VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQN 978
Cdd:PRK11153 4 LKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1059 LDEPTAGVDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
907-1117 |
5.80e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.83 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNA-IRQNLGVCPQ 984
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNVLFSMLTVEEHIWFYARL-KGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1064 AGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
920-1112 |
5.97e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 107.25 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTAYIQGKDIrtDLNAIRQNLGVCPQHNVLFSMLTVEEH 997
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 998 IWFYARLKGlsaekvksemeqivmdlglphkrtsrsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDL 1077
Cdd:cd03213 103 LMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 827475625 1078 LLKYRQ-GRTIILSTHHMdEADILG--DRIAIISHGKL 1112
Cdd:cd03213 154 LRRLADtGRTIICSIHQP-SSEIFElfDKLLLLSQGRV 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
906-1110 |
6.37e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 108.47 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQ 984
Cdd:cd03254 5 FENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNVLFSMlTVEEHIwfyaRLKGLSA--EKVKSEMEQI-----VMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:cd03254 85 DTFLFSG-TIMENI----RLGRPNAtdEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMD---EAD--ILGDRIAIISHG 1110
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNADkiLVLDDGKIIEEG 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1919-2133 |
8.72e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 107.34 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDEVHQNMGYC 1998
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
913-1117 |
1.19e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSM 991
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 lTVEEHIwFYARlKGLSAEKV-----KSEMEQIVMDL--GLPHKRTSRSNQLSGGmQR-KLSVALAFVGGSKVVILDEPT 1063
Cdd:COG1132 429 -TIRENI-RYGR-PDATDEEVeeaakAAQAHEFIEALpdGYDTVVGERGVNLSGG-QRqRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1064 AGVDPYARRGIWDLLLKYRQGRTIILSTH------HMdeadilgDRIAIISHGKLCCVGS 1117
Cdd:COG1132 505 SALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGT 557
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
920-1119 |
1.78e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 107.17 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQnlgVCPQHNVLFSMLTVEEHIw 999
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1000 fYARLKGLSAEKVKSEMEQIVMD----LGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1076 DLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSL 1119
Cdd:TIGR01184 155 EELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIL 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
903-1140 |
1.96e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.29 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 903 GVYIENLMKIYSNGK----VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-----DLN 973
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIRQNLGVCPQ--HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSN-QLSGGMQRKLSVALAF 1050
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1051 VGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--------SLFL 1121
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdifqdvDFLE 240
|
250 260
....*....|....*....|...
gi 827475625 1122 KTQLG----TGYYLTLVKKDFDL 1140
Cdd:PRK13649 241 EKQLGvpkiTKFAQRLADRGISF 263
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1920-2133 |
2.50e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 106.08 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvlteIDEVHQNMGYCP 1999
Cdd:cd03235 1 EVEDLT--VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2000 QFDAIN--------DL-LTGRE-HLEFYAILRgvpeKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGG 2069
Cdd:cd03235 75 QRRSIDrdfpisvrDVvLMGLYgHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2070 PPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLG 2133
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
915-1096 |
3.18e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 106.71 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSG-TAYIQGKDI-RTDLNAIRQNLGvcpqhnvLFSMl 992
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIG-------LVSP- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 tvEEHIWFYARLKG----LSA--------EKVKSEMEQIVMD----LGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKV 1056
Cdd:COG1119 86 --ALQLRFPRDETVldvvLSGffdsiglyREPTDEQRERAREllelLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDE 1096
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEE 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
923-1116 |
3.81e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 105.65 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 923 LTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFyA 1002
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1003 RLKGLSAEKVKSE-MEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKY 1081
Cdd:cd03298 95 LSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 1082 RQGR--TIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:cd03298 175 HAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1918-2161 |
7.26e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 111.53 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVY---KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDE 1990
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCPQ--FDAINDLLTGREHLEF-YAILRGVPEKEVCKVADWGIRKLGLM-KYVDKAAGSYSGGNMRKLSTAMAL 2066
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNK 2141
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQ----ILNLLRDlqrelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
250 260
....*....|....*....|
gi 827475625 2142 FGDGYTIILrVAgADPRLEP 2161
Cdd:COG1123 496 PQHPYTRAL-LA-AVPSLDP 513
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1918-2128 |
9.04e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 104.90 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKP--AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEV---- 1991
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1992 HQNMGYCPQ--FDAINDLLTGREH----LEFYAILRGVPEKEVCKVADwgIRKLGLMKYV-DKAAGSYSGGNMRKLSTAM 2064
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQiaepLRIHGKLSKKEARKEAVLLL--LVGVGLPEEVlNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2065 ALIGGPPVVFLDEPTTGMDPKARRalwnCILSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQA----QILDLLKKlqeelGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1919-2129 |
1.44e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 103.74 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNMG 1996
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP-LSAMPppEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQfdaINDLLTG--REHLEFYAILRGVPEKEVcKVADWgIRKLGL-MKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:COG4619 78 YVPQ---EPALWGGtvRDNLPFPFQLRERKFDRE-RALEL-LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
904-1112 |
1.86e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 104.50 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNG---KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNL 979
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GVCPQH--NVLFSMLTVEEHIWFYARLKGLSAekVKSEMEQIVMDLGLPHK-RTSRSNQLSGG-MQRklsVAL--AFVGG 1053
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSfLDRYPHQLSGGqRQR---VAIarALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
914-1112 |
1.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 914 SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNA--IRQNLGVCPQH--NVLF 989
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKAGMVFQNpdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 SMLtVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1069
Cdd:PRK13633 100 ATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1070 ARR----GIWDLLLKYrqGRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PRK13633 179 GRRevvnTIKELNKKY--GITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1919-2138 |
1.92e-24 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 104.30 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDEVH--QNMG 1996
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVElrRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGL--MKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1918-2140 |
2.02e-24 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 104.28 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlteideVHQNM-- 1995
Cdd:TIGR04406 1 TLVAENLIKSYKKRK--VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI------THLPMhe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 ------GYCPQFDAINDLLTGREHLEfyAIL---RGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMAL 2066
Cdd:TIGR04406 73 rarlgiGYLPQEASIFRKLTVEENIM--AVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
919-1112 |
2.94e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 103.05 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEH 997
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 998 IwfyaRLKGLSAEkvKSEMEQIVMDLGLP-----HKR------TSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:cd03245 98 I----TLGAPLAD--DERILRAAELAGVTdfvnkHPNgldlqiGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1067 DPYARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKL 1112
Cdd:cd03245 172 DMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
886-1098 |
3.20e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 109.68 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 886 ENAEAVCIEEEPAHIDP--GVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI 963
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPasSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 964 QGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIWFYARlkGLSAEKVKSEMEQIVMD-------LGLPHKRTSRSNQ 1035
Cdd:TIGR02857 382 NGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAENIRLARP--DASDAEIREALERAGLDefvaalpQGLDTPIGEGGAG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1036 LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTH---HMDEAD 1098
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1935-2128 |
4.27e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 110.98 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEID----EVHQNMGYCPQ-FDAINDlLT 2009
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ----PVDagdiATRRRVGYMSQaFSLYGE-LT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2010 GREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGnMR-KLSTAMALIGGPPVVFLDEPTTGMDPKARR 2088
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLG-IRqRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 2089 ALWNCI--LSiIKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2128
Cdd:NF033858 435 MFWRLLieLS-REDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1919-2153 |
5.08e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.34 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVY--KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEID-EVHQNM 1995
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQ--FDAINDLLTGREHL-EFYAILR-GVPEKEVCKVADwgirKLGLMK-YVDKAAGSYSGGNMRKLSTAMALIGGP 2070
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILaEPLRIHGlPDREERIAELLE----QVGLPPsFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2071 PVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGYTII 2149
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRE 237
|
....
gi 827475625 2150 LRVA 2153
Cdd:COG1124 238 LLAA 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
918-1117 |
7.59e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 7.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNAIRQNLGVCPQHNVLFSMLTVE 995
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAQAAGIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWF---YARLKGLSAEKVKSEMEQIVMDLGL---PHKRTSRsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1069
Cdd:COG1129 98 ENIFLgrePRRGGLIDWRAMRRRARELLARLGLdidPDTPVGD---LSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1070 ARRGIWDLL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGKLccVGS 1117
Cdd:COG1129 175 EVERLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
895-1117 |
8.20e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.80 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 895 EEPAHIDPGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA 974
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 975 IRQNLGVCPQHNVLFSMLTVEEHIWFyarlkGLSAEKV-KSEMEQIVMD----LGLPHKRTSRSNQLSGGMQRKLSVALA 1049
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHMTVFENVAF-----GLRMQKTpAAEITPRVMEalrmVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1050 FVGGSKVVILDEPTAGVDpYARRGIWDLLLKYRQ---GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
906-1111 |
8.99e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.24 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG----KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIR----- 976
Cdd:COG1101 4 LKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKrakyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 ----QN--LGVCPqhnvlfSMlTVEEHIWF-YARLK--GLSAEKVKSEMEQI-----VMDLGLPHKRTSRSNQLSGGmQR 1042
Cdd:COG1101 83 grvfQDpmMGTAP------SM-TIEENLALaYRRGKrrGLRRGLTKKRRELFrellaTLGLGLENRLDTKVGLLSGG-QR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1043 K-LSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:COG1101 155 QaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
902-1117 |
1.01e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 902 PGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGV 981
Cdd:PRK11607 18 PLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIvmdLGLPH-----KRtsRSNQLSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEM---LGLVHmqefaKR--KPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1057 VILDEPTAGVDPYARR----GIWDLLlkYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK11607 171 LLLDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2008-2155 |
1.21e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 104.82 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2008 LTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2088 RALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGdGYTIILRVAGA 2155
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHA 247
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1919-2130 |
1.43e-23 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 101.36 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIDEVHQNMG 1996
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEkevckvADWGIRKL-----GLMKYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAK------RKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2072 VVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2130
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1943-2140 |
1.79e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 101.42 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL----TEIDEVHQNMGYCPQFDAINDLLTGREHLEFYa 2018
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMGMLFQSGALFDSLTVFENVAFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2019 iLR---GVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGnMRK-LSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCI 2094
Cdd:cd03261 102 -LRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGG-MKKrVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 2095 LSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:cd03261 180 RSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1919-2124 |
2.25e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 100.62 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVY--KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlTEIDEVHQNMG 1996
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGnMRK-LSTAMALIGGPPVVFL 2075
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGG-MRQrVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2076 DEPTTGMDPKARRALWNCILSII-KEGRSVVLTSHSMEECEALCTRMAIM 2124
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1918-2140 |
3.98e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 100.44 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKqkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDEVHQ 1993
Cdd:COG1127 5 MIEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NMGYCPQFDAINDLLTGREHLEFYaiLR---GVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGnMRK---LstAMALI 2067
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFP--LRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGG-MRKrvaL--ARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1919-2109 |
4.49e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.97 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGvPEKEVCKVAdwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHG-GAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1919-2138 |
1.02e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 105.23 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEiDEVHQNMG 1996
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdLDE-DDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQ----FDA-I-NDLLTGREHL---EFYAILRGVpekevcKVADWgIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:COG4987 413 VVPQrphlFDTtLrENLRLARPDAtdeELWAALERV------GLGDW-LAALpdGLDTWLGEGGRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKeGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
906-1113 |
1.30e-22 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 98.33 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENL-MKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCP 983
Cdd:cd03244 5 FKNVsLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMlTV-----------EEHIWFYARLKGLsAEKVKSemeqivMDLGLPHKRTSRSNQLSGGmQRKL-SVALAFV 1051
Cdd:cd03244 85 QDPVLFSG-TIrsnldpfgeysDEELWQALERVGL-KEFVES------LPGGLDTVVEEGGENLSVG-QRQLlCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1052 GGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEadILG-DRIAIISHGKLC 1113
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIDsDRILVLDKGRVV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
917-1112 |
1.68e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 98.37 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdIRTDLNAirqNLGVCPqhnvlfsMLTVEE 996
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGL---GGGFNP-------ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKL--SVALAFvgGSKVVILDEPTAGVDPYARRGI 1074
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 827475625 1075 WDLLL-KYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03220 182 QRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1918-2128 |
2.07e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.56 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDeVHQ---- 1993
Cdd:COG1137 3 TLEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLP-MHKrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NMGYCPQFDAINDLLTGREHLefYAIL--RGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNI--LAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2072 VVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1919-2134 |
5.69e-22 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 96.92 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT------EIDEVH 1992
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQfdaindlLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPV 2072
Cdd:cd03300 79 QNYALFPH-------LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2134
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
917-1108 |
6.38e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.63 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRqnlGVCPQHNVLFSMLTVEE 996
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR---GVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFYARLKGLSaekvKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARR 1072
Cdd:COG4525 96 NVAFGLRLRGVP----KAERRARAEELlalvGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 827475625 1073 GIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIIS 1108
Cdd:COG4525 172 QMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1920-2133 |
6.63e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 95.19 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGYC 1998
Cdd:cd03214 1 EVENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFdaindlltgrehlefyailrgvpekevckvadwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03214 79 PQA----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2079 TTGMDPKARRALwnciLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:cd03214 125 TSHLDIAHQIEL----LELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
930-1111 |
6.99e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.75 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWF--YARLKgL 1007
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQENNLFPHLTVAQNIGLglRPGLK-L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1008 SAEKvKSEMEQIVMDLGLPHKRTSRSNQLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYR 1082
Cdd:COG3840 103 TAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDLVdeLCRE 178
|
170 180
....*....|....*....|....*....
gi 827475625 1083 QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:COG3840 179 RGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1919-2128 |
7.58e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.31 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGI----PPGECFGLLGVNGAGKTSTFKMLTG--DSVVTSGEAYLAGNSVltEIDEVH 1992
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVsgkaKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQFDAINDLLTGREHLEFYAILRGVpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPV 2072
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHS-MEECEALCTRMAIMVNGR 2128
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1918-2138 |
9.29e-22 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 96.50 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYK--RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDEV 1991
Cdd:cd03258 1 MIELKNVSKVFGdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1992 HQNMGYCpqFDAINdLLTGREHLEFYAI---LRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:cd03258 81 RRRIGMI--FQHFN-LLSSRTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
906-1112 |
1.01e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVD---GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLNAIR-Q 977
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADiLGDRIAIISHGKL 1112
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
921-1136 |
1.24e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 96.07 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 921 DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIw 999
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1000 fyarlkGLSAEKVKSEMEQ----------IVMDlgLPHK-RT---SRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03249 98 ------RYGKPDATDEEVEeaakkanihdFIMS--LPDGyDTlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1066 VDPYARRGIWDLLLKYRQGRTIILSTHHMdeADILG-DRIAIISHGKLCCVGSSLFLKTQlgTGYYLTLVKK 1136
Cdd:cd03249 170 LDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRNaDLIAVLQNGQVVEQGTHDELMAQ--KGVYAKLVKA 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
918-1117 |
1.33e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR----TDLNAIR-QNLGVCPQHNVLFSML 992
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARR 1072
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1073 GIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK10070 202 EMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
915-1117 |
1.38e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQHNVL-FSmL 992
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLPQHSSLsFP-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGG-MQRklsVALAFV--------GGSKVVILDEPT 1063
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeQQR---VQLARVlaqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1064 AGVDPY--------ARRgiwdllLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK13548 169 SALDLAhqhhvlrlARQ------LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
915-1112 |
2.08e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.53 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMltv 994
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 eehiwfyarlkglsaekvksemeqivmdlglphkrTSRSN---QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYAR 1071
Cdd:cd03247 90 -----------------------------------TLRNNlgrRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 1072 RGIWDLLLKYRQGRTIILSTHHMdeadiLG----DRIAIISHGKL 1112
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHHL-----TGiehmDKILFLENGKI 174
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
916-1112 |
2.42e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNA--IRQNLGVCPQHNVLFSML 992
Cdd:PRK11614 16 GKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIwfyaRLKGLSAEKvKSEMEQI--VMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:PRK11614 96 TVEENL----AMGGFFAER-DQFQERIkwVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 1069 YARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK11614 171 IIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
920-1112 |
2.85e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLG-------F--YEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNAIRQNLGVCP---QH 985
Cdd:COG1129 259 VEGLSVGgvvrdvsFsvRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWF-----YARLKGLSAEKVKSEMEQIVMDLGLphkRTSRSNQ----LSGGMQRKlsVALA--FVGGS 1054
Cdd:COG1129 339 EGLVLDLSIRENITLasldrLSRGGLLDRRRERALAEEYIKRLRI---KTPSPEQpvgnLSGGNQQK--VVLAkwLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1112
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
901-1124 |
3.31e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.23 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLmKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTT---TMSILTGLFP--PTSGTAYIQGKDI---RTDL 972
Cdd:PRK14239 3 EPILQVSDL-SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 973 NAIRQNLGVCPQHNVLFSMlTVEEHIWFYARLKGLSAEKVKSE-MEQIVMDLGLPHKRTSRSNQ----LSGGMQRKLSVA 1047
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1048 LAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKTQ 1124
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFMNPK 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
915-1097 |
4.08e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDirtdlnairqNLGVCPQHNVLFSML-- 992
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEE--HIWFYAR---LKGLSAEKvKSEMEQIVMDLGLPHKRTSRSNQLSGG-MQRKLsVALAFVGGSKVVILDEPTAGV 1066
Cdd:NF040873 73 TVRDlvAMGRWARrglWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 827475625 1067 DPYARRGIWDLLLKY-RQGRTIILSTHHMDEA 1097
Cdd:NF040873 151 DAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
886-1116 |
1.28e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.34 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 886 ENAEAVCIEEEPAHIDPGVYIENLMKIY---SNGKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA 961
Cdd:TIGR03269 262 EGVSEVEKECEVEVGEPIIKVRNVSKRYisvDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 962 YIQGKDIRTDLNAIR--------QNLGVCPQHNVLFSMLTVEEHI---------WFYARLK--------GLSAEKVKSEM 1016
Cdd:TIGR03269 342 NVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYPHRTVLDNLteaiglelpDELARMKavitlkmvGFDEEKAEEIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1017 EQivmdlgLPHkrtsrsnQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHM 1094
Cdd:TIGR03269 422 DK------YPD-------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDM 488
|
250 260
....*....|....*....|..
gi 827475625 1095 DEADILGDRIAIISHGKLCCVG 1116
Cdd:TIGR03269 489 DFVLDVCDRAALMRDGKIVKIG 510
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
901-1093 |
1.29e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.20 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNL 979
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GVCPQHNVLFSMlTVEEHIWFyARlKGLSAEKVKSEMEQI-----VMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVG 1052
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRL-AR-PDATDEELWAALERVgladwLRALpdGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 1053 GSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHH 1093
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1918-2124 |
1.42e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 93.62 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQK--PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlTEIDEVHQNM 1995
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQfdaiNDLL----TGREHLEFYAILRGVPEKEVCKVADWGIRKLGLmkyvDKAAGSY----SGGnMRK-LSTAMAL 2066
Cdd:COG1116 83 GVVFQ----EPALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGL----AGFEDAYphqlSGG-MRQrVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIM 2124
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1919-2128 |
1.46e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 92.65 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNMG 1996
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRQLDpaDLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQfDAindlltgreHLeFYAILR-----GVP---EKEVCKVADWGirklGLMKYVDKAAGSY-----------SGGNM 2057
Cdd:cd03245 82 YVPQ-DV---------TL-FYGTLRdnitlGAPladDERILRAAELA----GVTDFVNKHPNGLdlqigergrglSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2058 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCiLSIIKEGRSVVLTSH--SMEEceaLCTRMAIMVNGR 2128
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
906-1112 |
1.74e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.38 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKV-----AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD--------- 971
Cdd:PRK13651 5 VKNIVKIF-NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 972 ----------------LNAIRQNLGVCPQ--HNVLFSMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRS 1033
Cdd:PRK13651 84 leklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1034 N-QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK13651 163 PfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
.
gi 827475625 1112 L 1112
Cdd:PRK13651 243 I 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
916-1128 |
2.03e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDlnAIRQNlgVCPQ---------H 985
Cdd:NF033858 12 GKTvALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRA--VCPRiaympqglgK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NvLFSMLTVEEHIWFYARLKGLSAekvkSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:NF033858 88 N-LYPTLSVFENLDFFGRLFGQDA----AERRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1062 PTAGVDPYARRGIWDLLLKYRQGR---TIILSTHHMDEADILgDRIAIISHGKLCCVGSSLFLKTQLGTG 1128
Cdd:NF033858 163 PTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1910-2133 |
2.18e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1910 LGGGGQTDILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGN-SVLTEI 1988
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 devhqNMGYCPQfdaindlLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:cd03220 92 -----GGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1916-2128 |
2.25e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 92.84 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSG-EAYLAGNSVLTE-IDEVHQ 1993
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NMGYC-----PQFD----AINDLLTGrehleFYAIL---RGVPEKEVCKVADWgIRKLGLMKYVDKAAGSYSGGNMRKLS 2061
Cdd:COG1119 79 RIGLVspalqLRFPrdetVLDVVLSG-----FFDSIglyREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2062 TAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEG-RSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
906-1106 |
2.67e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 94.35 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIY--SNGKV-AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYIQGKDIRT----DLNAI 975
Cdd:COG0444 4 VRNLKVYFptRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 976 RQN-LGVCPQH--NVLFSMLTVEEHIW-FYARLKGLSAEKVKSEMEQIVMDLGLPHKRtSRSN----QLSGGMQRKLSVA 1047
Cdd:COG0444 84 RGReIQMIFQDpmTSLNPVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPE-RRLDryphELSGGMRQRVMIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1048 LAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAI 1106
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
913-1112 |
2.98e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.91 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSM 991
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 lTVEEHIwFYARLKGlSAEKV-----KSEMEQIVMdlGLPHKRTS----RSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:cd03253 90 -TIGYNI-RYGRPDA-TDEEVieaakAAQIHDKIM--RFPDGYDTivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1063 TAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1919-2109 |
3.37e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.02 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVykRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:PRK13538 2 LEARNLACE--RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVCKVAdwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
922-1125 |
3.40e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI---RTDLNAIRQNLGVC---PQHNVLFSmlTVE 995
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYT--DID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1076 DLLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKTQL 1125
Cdd:PRK13638 177 AIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGApgEVFACTEA 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
929-1117 |
4.85e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-----YIQGKDIRTDLNAIRQNLGVCPQ--HNVLFSMlTVEEHIWFY 1001
Cdd:PRK13643 31 KGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TVLKDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1002 ARLKGLS---AEKVKSEMEQIVmdlGLPHKRTSRSN-QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDL 1077
Cdd:PRK13643 110 PQNFGIPkekAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 1078 LLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK13643 187 FESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
915-1131 |
4.88e-20 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 91.39 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMLT 993
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VE-----------EHIWFYARLKGlsAEKVKSEM----EQIVMDLGLphkrtsrsnQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:cd03252 93 RDnialadpgmsmERVIEAAKLAG--AHDFISELpegyDTIVGEQGA---------GLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1059 LDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKLCCVGSSLFLKTQLGTGYYL 1131
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1919-2128 |
5.24e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 89.55 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEV---HQNM 1995
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGREHLEFyailrgvpekevckvadwgirklGLmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL-----------------------GL-----------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1916-2128 |
5.26e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 91.20 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIdeV 1991
Cdd:COG0410 1 MPMLEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1992 HQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKevckvADWGIRK-------LGLMKyvDKAAGSYSGGNMRKLSTAM 2064
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAE-----VRADLERvyelfprLKERR--RQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2065 ALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1863-2129 |
5.67e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1863 MAIEGVIFFSITVLIQYRFCIKARSLSTK--------LKPIGEEDEDVAR--------ERQRILGGGgqTDILELRQLTK 1926
Cdd:TIGR03269 210 ALEEAVKASGISMVLTSHWPEVIEDLSDKaiwlengeIKEEGTPDEVVAVfmegvsevEKECEVEVG--EPIIKVRNVSK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1927 VY---KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAY-LAGNSV--LTE------------I 1988
Cdd:TIGR03269 288 RYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWvdMTKpgpdgrgrakryI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DEVHQNMGYCPQFDAINDLlTGREHLEF---YAILRGVpekEVCKVAdwGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:TIGR03269 368 GILHQEYDLYPHRTVLDNL-TEAIGLELpdeLARMKAV---ITLKMV--GFDEEKAEEILDKYPDELSEGERHRVALAQV 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
915-1093 |
6.15e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.11 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTV 994
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHIWFYARLKGLSAEKVKSEMEQIvmdlGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|
gi 827475625 1075 WDLLLKY-RQGRTIILSTHH 1093
Cdd:TIGR01189 167 AGLLRAHlARGGIVLLTTHQ 186
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1943-2109 |
6.28e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 90.79 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTG---DSVVTSGEAYLAGNSVltEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAI 2019
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2020 LR-------GVPEKEVckvADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPkarrALWN 2092
Cdd:cd03234 108 LRlprkssdAIRKKRV---EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTAL 180
|
170 180
....*....|....*....|.
gi 827475625 2093 CILSIIKE----GRSVVLTSH 2109
Cdd:cd03234 181 NLVSTLSQlarrNRIVILTIH 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
907-1112 |
6.52e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQNLGVC 982
Cdd:PRK10908 5 EHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1063 TAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
929-1112 |
7.60e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 90.43 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGkdirTDLNAIRQNLGVCP---------QHNVLFSMLTVEEHIW 999
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKINLPPqqrkiglvfQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1000 FyaRLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL- 1078
Cdd:cd03297 98 F--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELk 175
|
170 180 190
....*....|....*....|....*....|....*
gi 827475625 1079 -LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:cd03297 176 qIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
919-1112 |
1.07e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 90.12 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYIQGKDIRTdlNAIRQNLGVCPQHN---VLFSM 991
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLP--LSIRGRHIATIMQNprtAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 LTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRT---SRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:TIGR02770 79 FTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1069 YARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:TIGR02770 159 VNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1946-2142 |
1.23e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 90.09 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1946 GECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPE 2025
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2026 KEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVV 2105
Cdd:cd03299 104 KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 2106 L-TSHSMEECEALCTRMAIMVNGRFRCLGSVQ----HLKNKF 2142
Cdd:cd03299 184 LhVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEF 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
915-1092 |
1.41e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR-TDLNAIRQNLGvcpQHNVLFSMLT 993
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEEHIWFYARLKGLSAEKVKSEMEqivmDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRG 1073
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 827475625 1074 IWDLLLKYR-QGRTIILSTH 1092
Cdd:PRK13539 166 FAELIRAHLaQGGIVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1916-2135 |
1.62e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.14 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRKQKP--------------------AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSG 1975
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1976 EAYLAGN-SVLTEIdevhqNMGYCPQfdaindlLTGREHLEFYAILRGVPEKEVCKVADwGIRKL-GLMKYVDKAAGSYS 2053
Cdd:COG1134 82 RVEVNGRvSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFD-EIVEFaELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2054 GGnMR-KL--STAMALigGPPVVFLDEPTTGMDP----KARRAlwncILSIIKEGRSVVLTSHSMEECEALCTRMAIMVN 2126
Cdd:COG1134 149 SG-MRaRLafAVATAV--DPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*....
gi 827475625 2127 GRFRCLGSV 2135
Cdd:COG1134 222 GRLVMDGDP 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
906-1117 |
1.75e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQH 985
Cdd:PRK10851 5 IANIKKSFGRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWF----YARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:PRK10851 83 YALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1062 PTAGVDPYARRGIWDLL------LKYrqgrTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK10851 163 PFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
921-1093 |
1.75e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 921 DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWF 1000
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1001 YARLKG-LSAEKVKSEMEQI----VMDlgLPhkrtsrSNQLSGGMQRKlsVALA--FVGGSKVVILDEP-----TAGVDP 1068
Cdd:PRK13538 98 YQRLHGpGDDEALWEALAQVglagFED--VP------VRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQGVAR 167
|
170 180
....*....|....*....|....*
gi 827475625 1069 YARRgiwdLLLKYRQGRTIILSTHH 1093
Cdd:PRK13538 168 LEAL----LAQHAEQGGMVILTTHQ 188
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1919-2129 |
2.47e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 87.75 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQfdaindlltgREHLeFYAILRgvpekevckvADWGIRklglmkyvdkaagsYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03247 81 NQ----------RPYL-FDTTLR----------NNLGRR--------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEgRSVVLTSHSMEECEALcTRMAIMVNGRF 2129
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
901-1117 |
2.63e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.79 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLG 980
Cdd:COG4674 8 GPILYVEDLTVSF-DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VC-----PqhNVlFSMLTVEEH----------IW--FYARLKGLSAEKVKSEMEQIvmdlGLPHKRTSRSNQLSGGMQRK 1043
Cdd:COG4674 87 IGrkfqkP--TV-FEELTVFENlelalkgdrgVFasLFARLTAEERDRIEEVLETI----GLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1044 LSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
919-1117 |
2.66e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAI------RQNLGVC---PQHNvLF 989
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQ-LF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 SMlTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSN-QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1069 YARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK13645 184 KGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
916-1110 |
3.21e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRqnlGVCPQHNVLFSMLTVE 995
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER---GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 1076 DLLLK--YRQGRTIILSTHHMDEADILGDRIAIISHG 1110
Cdd:PRK11248 169 TLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
920-1112 |
5.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGkDIRTDLNA--IRQNLGVCPQH-NVLFSMLTVEE 996
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVwdIRHKIGMVFQNpDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWD 1076
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 827475625 1077 LLLKYRQ--GRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PRK13650 182 TIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1916-2128 |
5.77e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.18 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRKQK--PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EID 1989
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1990 EV-HQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:COG1136 82 RLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSmEECEALCTRMAIMVNGR 2128
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1919-2128 |
8.24e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.62 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG-----DSVVTSGEAYLAGNSVLTEID---E 1990
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVdvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCPQ----FDAindllTGREHLEFYAILRGV-PEKEVCKVADWGIRKLGLMKYV-DKA-AGSYSGGNMRKLSTA 2063
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVkDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEgRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1918-2128 |
8.91e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.54 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIdEVHQ-NMG 1996
Cdd:COG3842 5 ALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGL-PPEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEKEV-CKVADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIrARVAEL-LELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
914-1112 |
1.00e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.65 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 914 SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQH-NVLFSM 991
Cdd:PRK13648 19 SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNpDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 LTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYAR 1071
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 1072 RGIWDLLLKYRQGR--TIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PRK13648 179 QNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1919-2128 |
1.04e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 85.51 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNMG 1996
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDleSLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQfDAIndLLTG--REHlefyaILrgvpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVF 2074
Cdd:cd03228 80 YVPQ-DPF--LFSGtiREN-----IL--------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKeGRSVVLTSHSMEECEaLCTRMAIMVNGR 2128
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1919-2128 |
1.04e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 87.62 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDE-------- 1990
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 ---VHQNMGYCPQFDAINDLLTGR--EHLEFYAILRGVP--EKEVCKVAdwgIRKLGLMKYVDKAAGSYSGGNMRKLSTA 2063
Cdd:cd03256 80 igmIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPkeEKQRALAA---LERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSI-IKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1919-2109 |
1.18e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.39 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYC 1998
Cdd:cd03231 1 LEADELT--CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGvpeKEVCKVAdwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHS---DEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
916-1111 |
1.23e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--RTDLNAIRQNLGVCPQHNVLFSMLT 993
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIARMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEE------HIWFYAR-LKGLSAEKV--KSEMEQI--------VMDLgLPHKRTSRSNqLSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK11300 97 VIEnllvaqHQQLKTGlFSGLLKTPAfrRAESEALdraatwleRVGL-LEHANRQAGN-LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1919-2128 |
1.25e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 88.08 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVG----------------------IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGE 1976
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGkskeeilkktgqtvgvndvsldVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1977 AYLAGNSVLT------------EIDEVHQNMGYCPQfdaindlLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKY 2044
Cdd:cd03294 81 VLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2045 VDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAI 2123
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
....*
gi 827475625 2124 MVNGR 2128
Cdd:cd03294 234 MKDGR 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
903-1126 |
1.29e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.79 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 903 GVYIENLMKIYSNGKvAVDGLTLGFYEGQITSFLGHNGAGKTTTmSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVC 982
Cdd:NF000106 13 AVEVRGLVKHFGEVK-AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 -PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:NF000106 91 rPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1062 PTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKTQLG 1126
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
917-1117 |
1.40e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdIRT--DLNAirqnlGVCPQhnvlfsmLTV 994
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAllELGA-----GFHPE-------LTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHIWFYARLKGLSAEKVKSEMEQIV--MDLG----LPHKRtsrsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:COG1134 106 RENIYLNGRLLGLSRKEIDEKFDEIVefAELGdfidQPVKT------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1069 Y----ARRGIWDLLlkyRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:COG1134 180 AfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
901-1112 |
1.52e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.78 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLmKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTT---TMSILTGLFPP--TSGTAYIQGKDI---RTDL 972
Cdd:COG1117 9 EPKIEVRNL-NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGEDIydpDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 973 NAIRQNLGVCPQHNVLFSMlTVEEHIWFYARLKGLsaeKVKSEMEQIVmdlglphkRTS------------RSNQ----L 1036
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGI---KSKSELDEIV--------EESlrkaalwdevkdRLKKsalgL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1037 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
913-1134 |
1.62e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.50 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSM 991
Cdd:TIGR01193 483 YGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 lTVEEHIWFYAR--------LKGLSAEKVKSEMEQivMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:TIGR01193 563 -SILENLLLGAKenvsqdeiWAACEIAEIKDDIEN--MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1064 AGVDPYARRGIWDLLLKYrQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKTQlgTGYYLTLV 1134
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
917-1125 |
2.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDiRTDLNA-----IRQNLGVCPQH-NVLFS 990
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVD-GITLTAktvwdIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 991 MLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYA 1070
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1071 RRGIWDLL--LKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGS--SLFLKTQL 1125
Cdd:PRK13640 179 KEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSpvEIFSKVEM 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
916-1093 |
2.95e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVE 995
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGlsaekvKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:cd03231 92 ENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*....
gi 827475625 1076 DLLLKY-RQGRTIILSTHH 1093
Cdd:cd03231 166 EAMAGHcARGGMVVLTTHQ 184
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
906-1112 |
3.41e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.19 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCP 983
Cdd:cd03246 3 VENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSmltveehiwfyarlkGLSAEkvksemeqivmdlglphkrtsrsNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:cd03246 83 QDDELFS---------------GSIAE-----------------------NILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1064 AGVDPYARRGIWDLLLKYR-QGRTIILSTHHMdEADILGDRIAIISHGKL 1112
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
904-1126 |
4.78e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.24 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDlNAIrQNLGVCP 983
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-TH-RSI-QQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 --QHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQI--VMDLGLPHKRTsrSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:PRK11432 83 vfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEAleLVDLAGFEDRY--VDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1060 DEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS---------SLFLKTQLG 1126
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMASFMG 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
906-1112 |
6.01e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.57 E-value: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayIQGKDIRTD-----------LNA 974
Cdd:PRK11264 6 VKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGT--IRVGDITIDtarslsqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 975 IRQNLGVCPQHNVLFSMLTVEEH-IWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1054 SKVVILDEPTAGVDPYArrgIWDLLLKYRQ----GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK11264 163 PEVILFDEPTSALDPEL---VGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
906-1117 |
6.57e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNA--IRQNLGVCP 983
Cdd:PRK11231 5 TENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSSrqLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLTVEE--------HIWFYARLKGLSAEKVKSEMEQivmdLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQ----TRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
910-1118 |
6.98e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 910 MKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP------PTSGTAYIQGKDI-RTDLNAIRQNLGVC 982
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEK-VKSEMEQIVMDLGL---PHKR-TSRSNQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLwkeVYDRlNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
908-1101 |
7.49e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 908 NLMKIYSNGKVAVDGL---TLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIR-----QNL 979
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GVCPQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 827475625 1060 DEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILG 1101
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
906-1118 |
8.14e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYIQGKDI-RTDLNAIRQNL 979
Cdd:PRK14247 6 IRDLKVSFGQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GVCPQHNVLFSMLTVEEHIWFYARLKGLSA------EKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:PRK14247 85 QMVFQIPNPIPNLSIFENVALGLKLNRLVKskkelqERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
904-1117 |
1.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--RTDLNAIRQNLGV 981
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQH-NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILD 1060
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1061 EPTAGVDPYARRGIWDLLLK-YRQGRTIILSTHHMDEADIlGDRIAIISHGKLCCVGS 1117
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1918-2128 |
1.11e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 86.65 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKP--AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG---DSVVTSGEAYLAGNSVLT----EI 1988
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DEV-HQNMGYCPQ--FDAINDLLTGREHL-EFYAILRGVPEKEVCKVADWGIRKLGLmKYVDKAAGSY----SGGnMR-K 2059
Cdd:COG0444 81 RKIrGREIQMIFQdpMTSLNPVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYphelSGG-MRqR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2060 LSTAMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQ----ILNLLKDlqrelGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
895-1117 |
1.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 895 EEPAHIDPGVYIENLMKIY----SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT 970
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 971 DLNAIRQNLGVCPQHNVLFSML------------------TVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSR 1032
Cdd:PRK13631 93 KKNNHELITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1033 SN-QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHG 1110
Cdd:PRK13631 173 SPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
....*..
gi 827475625 1111 KLCCVGS 1117
Cdd:PRK13631 253 KILKTGT 259
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1918-2128 |
1.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV---LTEIDEVHQN 1994
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQfDAINDLLTGR--EHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPV 2072
Cdd:PRK13636 84 VGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1919-2128 |
1.23e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.09 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlteidevhqnmgyc 1998
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 pQFDAINDlltGREHlefyailrgvpekevckvadwGIRklglMKYvdkaagSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:cd03216 65 -SFASPRD---ARRA---------------------GIA----MVY------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1928-2127 |
1.26e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 83.46 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1928 YKRKQKpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-----LTEIDEVHQNMGYcpQF- 2001
Cdd:cd03226 9 YKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQDVDY--QLf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2002 --DAINDLLTGrehlefyaiLRGVPEKEvcKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPT 2079
Cdd:cd03226 86 tdSVREELLLG---------LKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 2080 TGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
922-1092 |
2.06e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-------RTDLNAirQNLGVCPQHNVLFSMLTV 994
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeeaRAKLRA--KHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|
gi 827475625 1075 WDLL--LKYRQGRTIILSTH 1092
Cdd:PRK10584 186 ADLLfsLNREHGTTLILVTH 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
927-1117 |
2.16e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 927 FYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYIQGKDIrtDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFYAR 1003
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1004 LK---GLSAEKVKSEMEQIVMDLGL---PHKRTSRSNQ---LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 1075 WDLLLKYRQGRTIILSTHHMDEADI--LGDRIAIISHGKLCCVGS 1117
Cdd:TIGR00955 206 VQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
916-1112 |
2.24e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.99 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQG---KDIRTDLNAIRQNLGVCPQHNVLFSM 991
Cdd:PRK09493 12 GPTQVlHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 LTVEEHIWFYA-RLKGLSaekvKSEMEQIVMDL----GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:PRK09493 92 LTALENVMFGPlRVRGAS----KEEAEKQARELlakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1067 DPYARRGIwdllLKYRQ-----GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK09493 168 DPELRHEV----LKVMQdlaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1919-2110 |
2.74e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.80 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGY 1997
Cdd:TIGR02868 335 LELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQ----FDA--INDLLTGREHL---EFYAILRGVpekevcKVADWgIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMAL 2066
Cdd:TIGR02868 414 CAQdahlFDTtvRENLRLARPDAtdeELWAALERV------GLADW-LRALpdGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRALWNCILSIIkEGRSVVLTSHS 2110
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
897-1112 |
2.75e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.29 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 897 PAHIDPGVYIENLMKIYSN--GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLN 973
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIRQNLGVCPQHNVLFSMlTVEEHIWFyaRLKGLSAEKVK------------SEMEQivmdlGLPHKRTSRSNQLSGGMQ 1041
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKeaaqkahahsfiSELAS-----GYDTEVGEKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1042 RKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKL 1112
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1885-2138 |
3.29e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 87.89 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1885 ARSLSTKLKPIGEEDEDVARERQRILGGGGQTDIlELRQLTKVYKrKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFK 1964
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1965 MLTGDSVVTSGEAYLAGNSvLTEIDE--VHQNMGYCPQFDAindLLTG--REHLEFYAilRGVPEKEVCKVAdwgiRKLG 2040
Cdd:COG4988 382 LLLGFLPPYSGSILINGVD-LSDLDPasWRRQIAWVPQNPY---LFAGtiRENLRLGR--PDASDEELEAAL----EAAG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2041 LMKYVDKAAGSY-----------SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSiIKEGRSVVLTSH 2109
Cdd:COG4988 452 LDEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITH 530
|
250 260
....*....|....*....|....*....
gi 827475625 2110 SMEECeALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:COG4988 531 RLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
916-1111 |
3.71e-17 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 83.05 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTV 994
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHIwFYARLkGLSAEKVKSEMEQ-------IVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:cd03251 93 AENI-AYGRP-GATREEVEEAARAanahefiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1068 PYARRGIWDLLLKYRQGRTII-----LSThhMDEAdilgDRIAIISHGK 1111
Cdd:cd03251 171 TESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
906-1112 |
4.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVA--VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD-LNAIRQNLGVC 982
Cdd:PRK13642 7 VENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQH-NVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:PRK13642 87 FQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1062 PTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1919-2128 |
4.41e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 81.11 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-LTEIDEVHQNMGY 1997
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQFDainDLLTG--REhlefyAILrgvpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03246 81 LPQDD---ELFSGsiAE-----NIL--------------------------------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2128
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
906-1112 |
5.32e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.53 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG-KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--------DIRTDLNAIR 976
Cdd:PRK13635 8 VEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 QNlgvcPQHNvlFSMLTVEEHIWFYARLKGLS----AEKVKSEMEQIVMDLGL---PHKrtsrsnqLSGGmqRKLSVALA 1049
Cdd:PRK13635 88 QN----PDNQ--FVGATVQDDVAFGLENIGVPreemVERVDQALRQVGMEDFLnrePHR-------LSGG--QKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1050 FVGGS--KVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PRK13635 153 GVLALqpDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1897-2143 |
5.51e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 87.58 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1897 EEDEDVARERQRILGGGgqtdiLELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGE 1976
Cdd:COG2274 457 EREEGRSKLSLPRLKGD-----IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1977 AYLAGNSvLTEID--EVHQNMGYCPQfDaiNDLLTG--REHLEFYAilRGVPEKEVCKVAdwgiRKLGLMKYVDKAAGSY 2052
Cdd:COG2274 532 ILIDGID-LRQIDpaSLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEIIEAA----RLAGLHDFIEALPMGY 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2053 -----------SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKeGRSVVLTSHSMeECEALCTRM 2121
Cdd:COG2274 602 dtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRI 679
|
250 260
....*....|....*....|..
gi 827475625 2122 AIMVNGRFRCLGSVQHLKNKFG 2143
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKG 701
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1918-2129 |
5.91e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.94 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTkvykrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIDEVHQNM 1995
Cdd:cd03215 4 VLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCP---QFDAINDLLTGREHLEFYAILrgvpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPV 2072
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
918-1117 |
6.94e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDG----LTLGFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYIQGKDIRT----DLNAIRQNLgvCPQHNVLF 989
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 SMltveeHIWFYARL---KGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGG-MQRklsVALAFV---------GGSKV 1056
Cdd:PRK03695 83 AM-----PVFQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGeWQR---VRLAAVvlqvwpdinPAGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1057 VILDEPTAGVDpYARRGIWDLLLKY--RQGRTIILSTH---H-MDEAdilgDRIAIISHGKLCCVGS 1117
Cdd:PRK03695 155 LLLDEPMNSLD-VAQQAALDRLLSElcQQGIAVVMSSHdlnHtLRHA----DRVWLLKQGKLLASGR 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1922-2128 |
8.64e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1922 RQLTKVYKRKQKPA------VDRLCVG---------IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-- 1984
Cdd:COG1129 239 RELEDLFPKRAAAPgevvleVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVri 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1985 LTEIDEVHQNMGYCP---QFDAINDLLTGRE-----HLEFYAILRGVPEKEVCKVADWGIRKLGL-MKYVDKAAGSYSGG 2055
Cdd:COG1129 319 RSPRDAIRAGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2056 NMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1918-2138 |
9.12e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE-IDEVHQNMG 1996
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCpqFDAINDLL---TGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:PRK13652 82 LV--FQNPDDQIfspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
900-1116 |
1.01e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 900 IDPGVYIENLMKIYSnGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR--TDLNAIRQ 977
Cdd:PRK09700 2 ATPYISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMLTVEEHIwFYARLK-----GLSA---EKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALA 1049
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENL-YIGRHLtkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1050 FVGGSKVVILDEPTAGVdpyARRGIWDLLLKYRQ----GRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
902-1105 |
1.15e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 902 PGVYIENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLfPPTSGTAYIQGK---------DIRTDL 972
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffnqniyERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 973 NAIRQNLG-VCPQHNvLFSMlTVEEHIWFYARLKGLsaeKVKSEMEQIV------MDL--GLPHKRTSRSNQLSGGMQRK 1043
Cdd:PRK14258 84 NRLRRQVSmVHPKPN-LFPM-SVYDNVAYGVKIVGW---RPKLEIDDIVesalkdADLwdEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1044 LSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIA 1105
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
914-1139 |
1.48e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.54 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 914 SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMl 992
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVLFND- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIwFYARLKGLSAEKVKSEME-----QIV--MDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:TIGR02203 421 TIANNI-AYGRTEQADRAEIERALAaayaqDFVdkLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1066 VDPYARRGIWDLLLKYRQGRTIILSTHHMdeADILG-DRIAIISHGKLCCVGSSLFLKTQlgTGYYLTLVKKDFD 1139
Cdd:TIGR02203 500 LDNESERLVQAALERLMQGRTTLVIAHRL--STIEKaDRIVVMDDGRIVERGTHNELLAR--NGLYAQLHNMQFR 570
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
907-1112 |
1.57e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 80.94 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVAV---DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLN-----AIR-Q 977
Cdd:COG4181 12 RGLTKTVGTGAGELtilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALDedaraRLRaR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMLTVEEHIWFYARLKGLS--AEKVKSEMEQIvmdlGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:COG4181 91 HVGFVFQSFQLLPTLTALENVMLPLELAGRRdaRARARALLERV----GLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHhmDEADIL-GDRIAIISHGKL 1112
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
920-1113 |
1.99e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTdlnairqnlgVCPQ--------------- 984
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQdglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNVLFSMLTVEEHIWFYArLKGLS--AEKVKSEMEQIVMD--LGLPHKRTSRSNQ----LSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK10762 338 RDGLVLGMSVKENMSLTA-LRYFSraGGSLKHADEQQAVSdfIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEadILG--DRIAIISHGKLC 1113
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRIS 474
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1918-2185 |
2.25e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEID-------E 1990
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE----PIKydkksllE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCpqFDAINDLL---TGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:PRK13639 76 VRKTVGIV--FQNPDDQLfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVqhlKNKFGDGYT 2147
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP---KEVFSDIET 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 827475625 2148 II---LRVagadPRLEPVMEFIERE--LP---GSTLKEKHRNMLQY 2185
Cdd:PRK13639 231 IRkanLRL----PRVAHLIEILNKEdnLPikmGYTIGEARRNIKEL 272
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1943-2109 |
2.82e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 79.21 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTG--DSVVTSGEAYLAGNsvltEIDEVHQN-MGYCPQFDAINDLLTGREHLEFYAI 2019
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGR----PLDKNFQRsTGYVEQQDVHSPNLTVREALRFSAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2020 LRGVpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIK 2099
Cdd:cd03232 106 LRGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD 156
|
170
....*....|
gi 827475625 2100 EGRSVVLTSH 2109
Cdd:cd03232 157 SGQAILCTIH 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1918-2134 |
3.56e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGN--SVLTEIDEVHQNM 1995
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGREHL-EFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2134
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
908-1112 |
4.70e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 908 NLMKIYSnGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdIRTDLN-AIRQNLGV--CPQ 984
Cdd:PRK15439 16 SISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-PCARLTpAKAHQLGIylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNVLFSMLTVEEHIWFyarlkGLSA-EKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:PRK15439 94 EPLLFPNLSVKENILF-----GLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1064 AGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1919-2128 |
6.65e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 78.99 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL----TEIDEVHQN 1994
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQ-FDAINDLlTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:cd03292 80 IGVVFQdFRLLPDR-NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
919-1111 |
6.79e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTD---------LNAIRQNLGVCPQhnvlf 989
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqeagIGIIHQELNLIPQ----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 smLTVEEHIW----FYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:PRK10762 94 --LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 1066 VDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK10762 172 LTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1918-2112 |
8.16e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkPAVDRLCVGIPPGE-CFgLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDEVH 1992
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQfdainD--LLTGR---EHLEFYAILRGVPEKEVCK-VADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMAL 2066
Cdd:COG2884 79 RRIGVVFQ-----DfrLLPDRtvyENVALPLRVTGKSRKEIRRrVREV-LDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSME 2112
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
919-1130 |
8.18e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLN--AIRQNLGVCPQHNVLFSMlTVEE 996
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSeaALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HiwfyarLKGLSAEKVKSEMEQIVMDLGLPHKRTSRS----------NQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:PRK11160 433 N------LLLAAPNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1067 DPYARRGIWDLLLKYRQGRTIILSTH------HMdeadilgDRIAIISHGKLCCVGSSLFLKTQLGtGYY 1130
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGTHQELLAQQG-RYY 568
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1916-2134 |
1.18e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDEVHQNM 1995
Cdd:PRK11607 17 TPLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2134
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
903-1121 |
1.23e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 903 GVYIENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVC 982
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFSMLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1063 TAGVDPYAR---RgIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFL 1121
Cdd:PRK11000 161 LSNLDAALRvqmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
903-1112 |
1.25e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 903 GVYIENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNA-----I 975
Cdd:COG4161 2 SIQLKNINCFYGSHQALFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 976 RQNLGVCPQHNVLFSMLTVEEH-IWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGS 1054
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
904-1118 |
1.46e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKvAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP----PTS------GTAYIQGKDIRtDLN 973
Cdd:PRK09984 5 IRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellgRTVQREGRLAR-DIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIRQNLGVCPQHNVLFSMLTVEEHIWFYAR---------LKGLSAEKvKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKL 1044
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1045 SVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
920-1113 |
1.63e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.18 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPT-SGTAYIQGK--DIRTDLNAIRQNLGVCPQ----HNVLfSML 992
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIV-PIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLP--HKRTSRSN----QLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1067 DPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLC 1113
Cdd:TIGR02633 435 DVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
907-1116 |
1.66e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.73 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYIQGKDIRT-DLNAI--RQN 978
Cdd:PRK14267 8 VNLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpDVDPIevRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQHNVLFSMLTVEEHIWFYARLKGLSaeKVKSEMEQIV----MDLGLPHKRTSRSN----QLSGGMQRKLSVALAF 1050
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAIGVKLNGLV--KSKKELDERVewalKKAALWDEVKDRLNdypsNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1051 VGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1943-2113 |
1.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTG-----DSVVTSGEAYLAGNSVLTEIDEVHQNMGYCPQF--------DAINDLLT 2009
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpesqlfeeTVLKDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2010 GREHLefyailrGVPEKEVCKVADWGIRKLGLMK-YVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2088
Cdd:PRK13643 109 GPQNF-------GIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180
....*....|....*....|....*
gi 827475625 2089 ALWNCILSIIKEGRSVVLTSHSMEE 2113
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDD 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
906-1117 |
1.85e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLmKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGlFP---PTSGTAYIQGKDIrTDLNA---IRQNL 979
Cdd:cd03217 3 IKDL-HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GVCPQHNVLFSMLTVEEhiwfYARL--KGLS-AEKVKSEMEQIVMdlglphkrtsrsnqlsggMQRKLsvalafvggskv 1056
Cdd:cd03217 80 FLAFQYPPEIPGVKNAD----FLRYvnEGFSgGEKKRNEILQLLL------------------LEPDL------------ 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEAD-ILGDRIAIISHGKLCCVGS 1117
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1924-2135 |
2.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1924 LTKVYKRK---QKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG------NSVLTEIDE---- 1990
Cdd:PRK13637 8 LTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLSDIRKkvgl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQnmgYcPQFDAINDllTGREHLEFYAILRGVPEKEVCKVADWGIRKLGL--MKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:PRK13637 88 VFQ---Y-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2135
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1918-2129 |
2.81e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYkrkqkPAV---DRLCVGIPPGECFGLLGVNGAGKtSTF-KMLTGDSVVTSGEAYLAGNSV-LTEIDE-- 1990
Cdd:COG1129 4 LLEMRGISKSF-----GGVkalDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVrFRSPRDaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 ------VHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVadwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAM 2064
Cdd:COG1129 78 aagiaiIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRAREL----LARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2065 ALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
922-1134 |
2.83e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIWF 1000
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1001 ---YARLKGLSAEKVKSEMEQIVMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIW 1075
Cdd:TIGR00958 578 gltDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1076 DllLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKTQlgTGYYLTLV 1134
Cdd:TIGR00958 658 E--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
902-1094 |
3.32e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 902 PGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRtdlNAIRQNL-G 980
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR---QALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQHNVL---FSMLtVEE--------HIWFYARLKGLSAEKVKSEMEQIVMdLGLPHKRTSrsnQLSGGMQRKLSVALA 1049
Cdd:PRK15056 82 YVPQSEEVdwsFPVL-VEDvvmmgrygHMGWLRRAKKRDRQIVTAALARVDM-VEFRHRQIG---ELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1050 FVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHM 1094
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1931-2128 |
3.86e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.21 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1931 KQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEID--EVHQNMGYCPQ------FD 2002
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQnpdnqiVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2003 AI--NDLLTGREHLefyailrGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTT 2080
Cdd:PRK13633 101 TIveEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 2081 GMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECeALCTRMAIMVNGR 2128
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
906-1112 |
4.76e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.32 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR--------------TD 971
Cdd:PRK10619 8 VIDLHKRYGEHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 972 LNAIRQNLGVCPQHNVLFSMLTVEEHIWFY-ARLKGLSAEKVKSEMEQIVMDLGLPHK-RTSRSNQLSGGMQRKLSVALA 1049
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1050 FVGGSKVVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
907-1105 |
5.41e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLmKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSI---LTGLFPP--TSGTAYIQGKDI---RTDLNAIRQN 978
Cdd:PRK14243 14 ENL-NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 LGVCPQHNVLFSMlTVEEHIWFYARLKGLSA---EKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSK 1055
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGARINGYKGdmdELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1056 VVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIA 1105
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1943-2127 |
6.51e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 76.35 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEIDE-------VHQNMGYCPqfdaindLLTGREH-- 2013
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK----QITEpgpdrmvVFQNYSLLP-------WLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2014 LEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNC 2093
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 827475625 2094 ILSIIKEGR-SVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:TIGR01184 157 LMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
906-1112 |
7.45e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 80.18 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCP 983
Cdd:COG4618 333 VENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMlTVEEHIwfyARLKGLSAEKVKS--------EMeqIvmdLGLPH----KRTSRSNQLSGG-MQRklsVALA- 1049
Cdd:COG4618 413 QDVELFDG-TIAENI---ARFGDADPEKVVAaaklagvhEM--I---LRLPDgydtRIGEGGARLSGGqRQR---IGLAr 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1050 -FVGGSKVVILDEPTAGVDPYARRGIWDLL--LKyRQGRTIILSTHHMdeaDILG--DRIAIISHGKL 1112
Cdd:COG4618 481 aLYGDPRLVVLDEPNSNLDDEGEAALAAAIraLK-ARGATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
902-1112 |
8.73e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 76.41 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 902 PGVYIENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKD-------------- 967
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRD-VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqlseaer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 968 ---IRTDLNAIRQN------LGVCPQHNVLFSMLTV-EEHiwfYARLKGlSAEKVKSEMEqivmdlgLPHKRTS-RSNQL 1036
Cdd:TIGR02323 81 rrlMRTEWGFVHQNprdglrMRVSAGANIGERLMAIgARH---YGNIRA-TAQDWLEEVE-------IDPTRIDdLPRAF 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1037 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
916-1112 |
9.06e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR----TD-LNA----IRQNLGVCPQhn 986
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfastTAaLAAgvaiIYQELHLVPE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 987 vlfsmLTVEEHIW---FYARL----KGLSAEKVKSEMEQIVMDLGlPHKRTSRsnqLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:PRK11288 94 -----MTVAENLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDID-PDTPLKY---LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1060 DEPTAGVDpyAR------RGIWDLllkYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK11288 165 DEPTSSLS--AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
893-1112 |
9.52e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 893 IEEEPAHIDPG-----VYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKD 967
Cdd:PRK13657 319 VRDPPGAIDLGrvkgaVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 968 IRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIwfyaRL--------KGLSAEKVKSEMEQIVM-DLGLPHKRTSRSNQLS 1037
Cdd:PRK13657 399 IRTvTRASLRRNIAVVFQDAGLFNR-SIEDNI----RVgrpdatdeEMRAAAERAQAHDFIERkPDGYDTVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1038 GGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRT--II---LSThhMDEAdilgDRIAIISHGKL 1112
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRV 547
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1919-2124 |
1.43e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.05 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVY--KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDE---VHQ 1993
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NmgycpqfDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:COG4525 84 K-------DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSI-IKEGRSVVLTSHSMEECEALCTRMAIM 2124
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
917-1120 |
1.66e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYIQGK-----DIRTDLNA-IRQNlgvcPQH- 985
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcALRGRKIAtIMQN----PRSa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 -NVLFSMLTveehiwfYAR--LKGLSAEKVKSEMEQIVMDLGLPH-KRTSRSN--QLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:PRK10418 92 fNPLHTMHT-------HARetCLALGKPADDATLTAALEAVGLENaARVLKLYpfEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1060 DEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL--CCVGSSLF 1120
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveQGDVETLF 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
906-1112 |
1.74e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSnGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQgKDIRtdlnairqnLGVCPQH 985
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR---------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWF-YARLKGLSAEKVK-------------------------------SEMEQIVMDLGLPHKRTSRS 1033
Cdd:COG0488 70 PPLDDDLTVLDTVLDgDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeARAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1034 -NQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRgiW--DLLLKYRqGrTIILSTHhmDEA--DILGDRIAIIS 1108
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSH--DRYflDRVATRILELD 223
|
....
gi 827475625 1109 HGKL 1112
Cdd:COG0488 224 RGKL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1943-2130 |
2.00e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDEVH------QNMGYCPQFDAINDLLTGREHLEF 2016
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2017 YAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILS 2096
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 827475625 2097 IIKE-GRSVVLTSHSmEECEALCTRMAIMVNGRFR 2130
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
906-1110 |
2.50e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.05 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQG-----------KDIRtdlnA 974
Cdd:PRK11124 5 LNGINCFYGAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIR----E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 975 IRQNLGVCPQHNVLFSMLTVEEH-IWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGG 1053
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTHHMDEADILGDRIA------IISHG 1110
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVymenghIVEQG 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1916-2128 |
2.71e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.54 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRKQ-KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsVLTE------- 1987
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEenvwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 --IDEVHQNmgycP--QFDAI---NDLLTGREHlefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKL 2060
Cdd:PRK13650 81 hkIGMVFQN----PdnQFVGAtveDDVAFGLEN-------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECeALCTRMAIMVNGR 2128
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1945-2148 |
3.10e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDS---VVTSGEAYLAGNSVltEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILR 2021
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2022 ---GVPEKEVCKVADWGIRKLGLMKYVDKAAG------SYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWN 2092
Cdd:TIGR00955 128 mprRVTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2093 CILSIIKEGRSVVLTSH--SMEECEaLCTRMAIMVNGRFRCLGSVQHLKNKFGD-GYTI 2148
Cdd:TIGR00955 208 VLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
936-1112 |
3.19e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 936 LGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRqnlgvcP-----QHNVLFSMLTVEEHIWF--YARLKgLS 1008
Cdd:PRK10771 31 LGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR------PvsmlfQENNLFSHLTVAQNIGLglNPGLK-LN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1009 AEKvKSEMEQIVMDLGLPHKRTSRSNQLSGGmQRKlSVALA--FVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGR- 1085
Cdd:PRK10771 104 AAQ-REKLHAIARQMGIEDLLARLPGQLSGG-QRQ-RVALArcLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERq 180
|
170 180
....*....|....*....|....*...
gi 827475625 1086 -TIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK10771 181 lTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
914-1112 |
3.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 914 SNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQnLGVC-----PQHNV 987
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRR-LGVAyipedRLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 988 LFSMLTVEEHIWF-------YARLKGLSAEKVKSEMEQIVMDLGLphkRTSRSNQ----LSGGMQRKLSVALAFVGGSKV 1056
Cdd:COG3845 347 LVPDMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDV---RTPGPDTparsLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1935-2128 |
4.40e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMGYCPQFD---------AIN 2005
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQhvrlfremtVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2006 DLLTGR-EHLE--FYAILRGVP-----EKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDE 2077
Cdd:PRK11300 100 NLLVAQhQQLKtgLFSGLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2078 PTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1919-2112 |
4.86e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 77.33 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYkRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDE--VHQNMG 1996
Cdd:TIGR02857 322 LEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADAdsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQ----FDAindllTGREHLEFYAilRGVPEKEVCKVAD----WGI---RKLGLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:TIGR02857 400 WVPQhpflFAG-----TIAENIRLAR--PDASDAEIREALEraglDEFvaaLPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPkARRALWNCILSIIKEGRSVVLTSHSME 2112
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDA-ETEAEVLEALRALAQGRTVLLVTHRLA 518
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1935-2141 |
4.92e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIDEVHQNMGYCPQFDAINDLLTGRE 2012
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2013 HLeFYAILrgvPEKEVC--KVADWG---------IRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTG 2081
Cdd:PRK09700 100 NL-YIGRH---LTKKVCgvNIIDWRemrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2082 MDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNK 2141
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1918-2141 |
5.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE-IDEVHQNMG 1996
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQfDAINDLLTGR--EHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:PRK13647 83 LVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNK 2141
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
915-1110 |
6.02e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlT 993
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEEHIWFYARLKglsaeKVKSEMEQIVMDL---GLP-HKRTSRSNQLSGGMQRKLSVA--LAFVggSKVVILDEPTAGVD 1067
Cdd:PRK10247 97 VYDNLIFPWQIR-----NQQPDPAIFLDDLerfALPdTILTKNIAELSGGEKQRISLIrnLQFM--PKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 1068 PYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHG 1110
Cdd:PRK10247 170 ESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
884-1112 |
6.34e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 884 RKENAEAVcIEEEPAHIDPGVYI---------------ENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMS 948
Cdd:COG0488 282 RIKALEKL-EREEPPRRDKTVEIrfppperlgkkvlelEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 949 ILTGLFPPTSGTaYIQGKDIRtdlnairqnLGVCPQHNVLFSM-LTVEEHIWfyarlkGLSAEKVKSEMEQIVMDLGLP- 1026
Cdd:COG0488 360 LLAGELEPDSGT-VKLGETVK---------IGYFDQHQEELDPdKTVLDELR------DGAPGGTEQEVRGYLGRFLFSg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1027 ---HKRTSRsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYrQGrTIILSTHHMDEADILGDR 1103
Cdd:COG0488 424 ddaFKPVGV---LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATR 498
|
....*....
gi 827475625 1104 IAIISHGKL 1112
Cdd:COG0488 499 ILEFEDGGV 507
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1920-2141 |
6.69e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.26 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKtSTF-KMLTGDSVVTSGEAYLAGNSV----LTEIDE---- 1990
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDGITIskenLKEIRKkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNmgycP--QFDAI---NDLLTGREHlefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:PRK13632 88 IFQN----PdnQFIGAtveDDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNGRFRCLGSVQH-LKNK 2141
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
920-1116 |
6.79e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR-TDLNAIRQNLGVCPQHNVL---FSMLTVE 995
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLsfeFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 E-----HIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSrsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDpyA 1070
Cdd:PRK09536 99 EmgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTS----LSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1071 RRGIWDLLLKYR---QGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:PRK09536 173 NHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
929-1112 |
7.22e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--RTDLNAIRQNLGVCPQH---NVLFSMLTVEEHIWFYAR 1003
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1004 LK--------GL---SAEKVKSEMEQIVMDLGLpHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARR 1072
Cdd:PRK09700 368 LKdggykgamGLfheVDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKA 446
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 1073 GIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK09700 447 EIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1894-2109 |
7.90e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.84 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1894 PIGEEDEDVARERQRILGGGGqtDILELRQLT-----KVYKRKQKPAVDRLCVgipPGECFGLLGVNGAGKTSTFKMLTG 1968
Cdd:TIGR00956 737 DLTDESDDVNDEKDMEKESGE--DIFHWRNLTyevkiKKEKRVILNNVDGWVK---PGTLTALMGASGAGKTTLLNVLAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1969 D---SVVTSGEAYLAGNsvltEIDEVHQ-NMGYCPQFDAINDLLTGREHLEFYAILR---GVPEKEVCKVADWGIRKLGL 2041
Cdd:TIGR00956 812 RvttGVITGGDRLVNGR----PLDSSFQrSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEM 887
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2042 MKYVDKAAG-SYSGGNM---RKLSTAMALIGGPP-VVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:TIGR00956 888 ESYADAVVGvPGEGLNVeqrKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1934-2113 |
9.96e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 9.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1934 PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLteidevhqnmGYCPQFDAINDLL--TGR 2011
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV----------AYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2012 EHLEF----YAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:NF040873 76 DLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180
....*....|....*....|....*.
gi 827475625 2088 RALWNCILSIIKEGRSVVLTSHSMEE 2113
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1934-2198 |
1.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1934 PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG-----NSVLTEIDE----VHQNmgycPQFDAI 2004
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdFSKLQGIRKlvgiVFQN----PETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2005 -----NDLLTGREHLefyailrGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPT 2079
Cdd:PRK13644 92 grtveEDLAFGPENL-------CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2080 TGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQhlkNKFGDgytIILRVAGADPrl 2159
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE---NVLSD---VSLQTLGLTP-- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 827475625 2160 EPVMEFIERelpgstLKeKHRNMLQYQLSSSLTSLA----RIF 2198
Cdd:PRK13644 236 PSLIELAEN------LK-MHGVVIPWENTSSPSSFAeeicRLF 271
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1923-2168 |
1.34e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1923 QLTKVYKRKQ-KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL---TEIDEVHQNMGYC 1998
Cdd:PRK11248 3 QISHLYADYGgKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREhlefyaiLRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:PRK11248 83 PWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2079 TTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRClgsVQHLKNKFGDGYtiilrVAG--- 2154
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRF-----VAGess 227
|
250
....*....|....*...
gi 827475625 2155 ----ADPRlepvmeFIER 2168
Cdd:PRK11248 228 rsikSDPQ------FIAM 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1917-2115 |
1.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG--------DSVVTSGEAYLAGNSVLtEI 1988
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW-DI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DE----VHQNmgycP--QFDAI---NDLLTGREHlefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRK 2059
Cdd:PRK13640 83 REkvgiVFQN----PdnQFVGAtvgDDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2060 LSTAMALIGGPPVVFLDEPTTGMDPKARralwNCILSIIKE-----GRSVVLTSHSMEECE 2115
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1919-2141 |
1.79e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 72.37 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKqkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDEVHQNMGYC 1998
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYaiLRGVPEKEVCKVADWGIRKLGLMKYV--DKAAGSY----SGGNMRKLSTAMALIGGPPV 2072
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFG--LRVKPRSERPPEAEIRAKVHELLKLVqlDWLADRYpaqlSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNK 2141
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
904-1113 |
1.85e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQnlgvc 982
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 pqhnvLFSmlTVEEHIWFYARLKGLSAEKVKSEMEQIVMD-LGLPHKRTSRSN-----QLSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK10522 398 -----LFS--AVFTDFHLFDQLLGPEGKPANPALVEKWLErLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHmDEADILGDRIAIISHGKLC 1113
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
906-1112 |
2.09e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.53 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG--------KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--------- 968
Cdd:TIGR02769 5 VRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrkqrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 969 --RTDLNAIRQNL--GVCPQHNVLFSMLTVEEHiwfYARLKGLSAEKVKSEMEQIVmdlGLPHKRTSR-SNQLSGGMQRK 1043
Cdd:TIGR02769 85 afRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRH---LTSLDESEQKARIAELLDMV---GLRSEDADKlPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1044 LSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1932-2128 |
2.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1932 QKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE-----IDEVHQNMGYCPQFDAiND 2006
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQFPE-AQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2007 LL--TGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYV-DKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMD 2083
Cdd:PRK13641 98 LFenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 2084 PKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1895-2128 |
2.50e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1895 IGEEDEDVARERQRILGGGGQTDILELRQLTKvYKRKQkpaVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTS 1974
Cdd:PRK09700 242 VGRELQNRFNAMKENVSNLAHETVFEVRNVTS-RDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1975 GEAYLAGN--SVLTEIDEVHQNMGYC----------PQFD-----AI-NDLLTGRehleFYAILRGVPEKEVCKVADWGI 2036
Cdd:PRK09700 318 GEIRLNGKdiSPRSPLDAVKKGMAYItesrrdngffPNFSiaqnmAIsRSLKDGG----YKGAMGLFHEVDEQRTAENQR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2037 RKLGLM-KYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECE 2115
Cdd:PRK09700 394 ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
|
250
....*....|...
gi 827475625 2116 ALCTRMAIMVNGR 2128
Cdd:PRK09700 474 TVCDRIAVFCEGR 486
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
932-1117 |
2.66e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.99 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 932 ITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-----RTDLNAIRQNLGVCPQHNVLFSMLTVEEHIwFYARLKG 1006
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVRGNL-RYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1007 LSAEKVKSEmEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--G 1084
Cdd:TIGR02142 104 RPSERRISF-ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAefG 182
|
170 180 190
....*....|....*....|....*....|...
gi 827475625 1085 RTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1917-2130 |
2.84e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLaGNSVlteidevhqNMG 1996
Cdd:COG0488 314 KVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQ-FDAINDLLTGREHLEFYAilRGVPEKEVCKVadwgirkLGLM----KYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:COG0488 382 YFDQhQEELDPDKTVLDELRDGA--PGGTEQEVRGY-------LGRFlfsgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2072 VVFLDEPTTGMDPKARRALwncILSIIK-EGrSVVLTSHSMEECEALCTRMAIMVNGRFR 2130
Cdd:COG0488 453 VLLLDEPTNHLDIETLEAL---EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
930-1112 |
2.95e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK--DIRTDLNAIRQNLGVCPQ---HNVLFSMLTVEEHIWFYARL 1004
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1005 KGLSA--------EKVKSEmEQI-VMDLGLPHKRTSRSNqLSGGMQRK--LSVALAfvGGSKVVILDEPTAGVDPYARRG 1073
Cdd:PRK11288 359 HHLRAgclinnrwEAENAD-RFIrSLNIKTPSREQLIMN-LSGGNQQKaiLGRWLS--EDMKVILLDEPTRGIDVGAKHE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 1074 IWDLLLKY-RQGRTIILSTHhmDEADILG--DRIAIISHGKL 1112
Cdd:PRK11288 435 IYNVIYELaAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1941-2146 |
3.07e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1941 VGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL----TEIDEVH-QNMGYCPQFDAINDLLTGREHLE 2015
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2016 FYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCIL 2095
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2096 SI-IKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGY 2146
Cdd:PRK10070 209 KLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1918-2128 |
3.64e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL-TEIDE------ 1990
Cdd:PRK09493 1 MIEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDErlirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 ---VHQNMGYCPQFDAINDLLTGREHLefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:PRK09493 79 agmVFQQFYLFPHLTALENVMFGPLRV------RGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
916-1112 |
3.66e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY-----IQGKDI--RTDLNAIRQNLGVCPQHNVL 988
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIfnYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 989 FSMlTVEEHIWFYARLKGLSAEK-----VKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:PRK14271 113 FPM-SIMDNVLAGVRAHKLVPRKefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1064 AGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1918-2128 |
4.42e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.97 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnSVLTE---------I 1988
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEetvwdvrrqV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DEVHQNmgycP--QF---DAINDLLTGREHlefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTA 2063
Cdd:PRK13635 84 GMVFQN----PdnQFvgaTVQDDVAFGLEN-------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2128
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1919-2138 |
4.88e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDE--VHQNMG 1996
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQfdaindlltgREHLeFYAILR-----GVPEK---EVCKVadwgIRKLGLMKYVDKAAG----------SYSGGNMR 2058
Cdd:PRK11160 418 VVSQ----------RVHL-FSATLRdnlllAAPNAsdeALIEV----LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2059 KLSTAMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE---GRSVVLTSH---SMEECEALCtrmaIMVNGRFRCL 2132
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQ----ILELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQ 554
|
....*.
gi 827475625 2133 GSVQHL 2138
Cdd:PRK11160 555 GTHQEL 560
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
907-1118 |
6.19e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKI----YSNG-KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQ 977
Cdd:PRK11831 5 ANLVDMrgvsFTRGnRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 978 NLGVCPQHNVLFSMLTVEEHIWFYARLKG-LSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKV 1056
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1057 VILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1945-2128 |
9.27e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 69.63 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlTEIDEVHQNMGYCPQFDAINDL---------LTGREHLE 2015
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKINLPPQQRKIGLVfqqyalfphLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2016 FyaILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCIL 2095
Cdd:cd03297 98 F--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 2096 SIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03297 176 QIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1917-2138 |
9.79e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DIlELRQLTKVYKRK---QKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLaGNSVLT------E 1987
Cdd:PRK13634 2 DI-TFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagkknkK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 IDEVHQNMGYCPQFDaindlltgrEHLEFYA-ILR---------GVPEKEVCKVADWGIRKLGL-MKYVDKAAGSYSGGN 2056
Cdd:PRK13634 80 LKPLRKKVGIVFQFP---------EHQLFEEtVEKdicfgpmnfGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2057 MRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2135
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
...
gi 827475625 2136 QHL 2138
Cdd:PRK13634 231 REI 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1919-2133 |
1.02e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.24 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGY 1997
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQ----FDAindllTGREHLefyAILRGV-PEK--EVCKVA---DWgIRKL--GlmkY---VDKAAGSYSGGNMRKLST 2062
Cdd:COG4618 411 LPQdvelFDG-----TIAENI---ARFGDAdPEKvvAAAKLAgvhEM-ILRLpdG---YdtrIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2063 AMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMeecEAL--CTRMAIMVNGRFRCLG 2133
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1915-2134 |
1.25e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG---NSVLTE---I 1988
Cdd:PRK09452 11 LSPLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdiTHVPAEnrhV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DEVHQNMGYCPQfdaindlLTGREHLEFYAILRGVPEKEVCK-VADwGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:PRK09452 89 NTVFQSYALFPH-------MTVFENVAFGLRMQKTPAAEITPrVME-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2134
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1918-2152 |
1.28e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQK-PAVDrlcVGIPPGECFGLLGVNGAGKTSTFK----MLTGDSVVTSgEAYLAGNSVLTE----- 1987
Cdd:PRK09984 4 IIRVEKLAKTFNQHQAlHAVD---LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQREgrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 -IDEVHQNMGYC-PQFDAINDLlTGREHLEFYAiLRGVPEKEVC---------KVADWGIRKLGLMKYVDKAAGSYSGGN 2056
Cdd:PRK09984 80 dIRKSRANTGYIfQQFNLVNRL-SVLENVLIGA-LGSTPFWRTCfswftreqkQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2057 MRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIK-EGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2135
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|....*...
gi 827475625 2136 QHLKN-KFGDGYTIILRV 2152
Cdd:PRK09984 238 QQFDNeRFDHLYRSINRV 255
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
930-1092 |
1.52e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.42 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGlfPPTSGTayIQGkDIRTDLNAIRQNL----GVCPQHNVLFSMLTVEEHIWFYARLK 1005
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAGV--ITG-EILINGRPLDKNFqrstGYVEQQDVHSPNLTVREALRFSALLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1006 GLSAEkvksemeqivmdlglphkrtsrsnqlsggmQRK-LSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKY-RQ 1083
Cdd:cd03232 108 GLSVE------------------------------QRKrLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDS 157
|
....*....
gi 827475625 1084 GRTIILSTH 1092
Cdd:cd03232 158 GQAILCTIH 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1919-2110 |
2.00e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVykRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVltEIDEVHQNMGYC 1998
Cdd:PRK13539 3 LEGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDAINDLLTGREHLEFYAILRGVPEKEVckvaDWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 827475625 2079 TTGMDPKARRALWNCILSIIKEGRSVVLTSHS 2110
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
906-1111 |
2.52e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.32 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYIQGKDIRtdlnairqnlgvcpqh 985
Cdd:cd03221 3 LENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 nvlfsmltveehIWFYArlkglsaekvksemeqivmdlglphkrtsrsnQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:cd03221 65 ------------IGYFE--------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1066 VDPYARRGIWDLLLKYRqgRTIILSTHhmDEA--DILGDRIAIISHGK 1111
Cdd:cd03221 101 LDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1916-2128 |
3.30e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYK-----RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGE-AYLAGNSV--LTE 1987
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSiLVRHDGGWvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 IDEVH------QNMGYCPQFdaindL-----LTGREHLEFYAILRGVPEKEVC-KVADWgIRKLGLMKYV-DKAAGSYSG 2054
Cdd:COG4778 82 ASPREilalrrRTIGYVSQF-----LrviprVSALDVVAEPLLERGVDREEARaRAREL-LARLNLPERLwDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2055 GNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1941-2079 |
3.35e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1941 VGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGE---------AYLA-------GNSVL--------------TEIDE 1990
Cdd:COG0488 19 LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEvsipkglriGYLPqepplddDLTVLdtvldgdaelraleAELEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMG-YCPQFDAINDLLTGREHLEFYAIlrgvpEKEVCKVADwgirKLGL-MKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:COG0488 99 LEAKLAePDEDLERLAELQEEFEALGGWEA-----EARAEEILS----GLGFpEEDLDRPVSELSGGWRRRVALARALLS 169
|
170
....*....|.
gi 827475625 2069 GPPVVFLDEPT 2079
Cdd:COG0488 170 EPDLLLLDEPT 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1915-2127 |
3.78e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTKVYkRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIdevHQN 1994
Cdd:PRK15056 3 QQAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 M-GYCPQFDAIN---------DLLTGRE-HLEFyaiLRgVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTA 2063
Cdd:PRK15056 79 LvAYVPQSEEVDwsfpvlvedVVMMGRYgHMGW---LR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTrMAIMVNG 2127
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1920-2135 |
4.02e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1920 ELRQLTKVY--KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDEVHQ 1993
Cdd:PRK11153 3 ELKNISKVFpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NMGYCPQ-FDaindLLTGREHLEFYAI---LRGVPEKEVCKvadwgiRKLGLMKYV---DKAaGSY----SGGNMRKLST 2062
Cdd:PRK11153 83 QIGMIFQhFN----LLSSRTVFDNVALpleLAGTPKAEIKA------RVTELLELVglsDKA-DRYpaqlSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 2063 AMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2135
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRS----ILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1918-2128 |
4.04e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYkrkqkPAV---DRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVltEIDE---- 1990
Cdd:COG3845 5 ALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRSprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 -------VHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADwgirKLGLmkYVDKAAgsysggNMRKLSTA 2063
Cdd:COG3845 78 ialgigmVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSE----RYGL--DVDPDA------KVEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2064 M--------ALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG3845 146 EqqrveilkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
920-1112 |
4.29e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYIQGK--DIRTDLNAIRQNLGVCP------------- 983
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 -QHNVLFSMLTVeehiwfYARLKGLSAEKVKSEMEQIVMDLglpHKRTS----RSNQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:PRK13549 358 vGKNITLAALDR------FTGGSRIDDAAELKTILESIQRL---KVKTAspelAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1059 LDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1112
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPE--VLGlsDRVLVMHEGKL 483
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1918-2128 |
4.31e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEID-EVHQNMG 1996
Cdd:PRK11231 2 TLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGRE--------HLEFYAILRGVPEKEVckvaDWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:PRK11231 80 LLPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1933-2148 |
4.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1933 KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLT------GDSVVTSGEAYLAGNSVLtEIDEVHQNMGYCPQFDAIND 2006
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIF-QIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2007 L--LTGREHLEFYAILRGVPEK-EVCKVADWGIRKLGLMKYV----DKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPT 2079
Cdd:PRK14246 102 FphLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2080 TGMDPKARRALWNCILSIIKEgRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNKFGDGYTI 2148
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
906-1111 |
4.49e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKvAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKD-----------------I 968
Cdd:PRK11701 9 VRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrrlL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 969 RTDLNAIRQN------LGVCPQHNV---LfsMLTVEEHiwfYARLKGLSA---EKVksEMEQIVMDlGLPhkRTsrsnqL 1036
Cdd:PRK11701 88 RTEWGFVHQHprdglrMQVSAGGNIgerL--MAVGARH---YGDIRATAGdwlERV--EIDAARID-DLP--TT-----F 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1037 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1946-2128 |
4.69e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1946 GECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE------------IDE------------VHQNMGYCpqf 2001
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangivyISEdrkrdglvlgmsVKENMSLT--- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2002 dAINDLLTGREHLEFYAilrgvpekEVCKVADWgIR----KLGLMkyvDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDE 2077
Cdd:PRK10762 355 -ALRYFSRAGGSLKHAD--------EQQAVSDF-IRlfniKTPSM---EQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2078 PTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
907-1117 |
4.97e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 907 ENLMKIYSNGKVAvDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQH 985
Cdd:PRK10253 11 EQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEE--------HIWFYARLKGLSAEKVKSEMEQIvmdlGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK10253 90 ATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1918-2128 |
5.18e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.57 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKR---KQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTE----- 1987
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 -IDEVHQN--MGYCPQfdaindlLTGREHLEFyAILRGvpekevcKVAD--WGIRK--------------LGLMKYVDKA 2048
Cdd:COG1101 81 yIGRVFQDpmMGTAPS-------MTIEENLAL-AYRRG-------KRRGlrRGLTKkrrelfrellatlgLGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2049 AGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPK-ARRalwncILS----IIKEGRsvvLTS----HSMEECEALCT 2119
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKtAAL-----VLEltekIVEENN---LTTlmvtHNMEQALDYGN 217
|
....*....
gi 827475625 2120 RMAIMVNGR 2128
Cdd:COG1101 218 RLIMMHEGR 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
930-1093 |
6.34e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFyarlkGLSA 1009
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY-----DIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1010 EKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTII 1088
Cdd:PRK13540 102 SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVL 181
|
....*
gi 827475625 1089 LSTHH 1093
Cdd:PRK13540 182 LTSHQ 186
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1918-2128 |
6.44e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQKP--AVDRLCVGIPPGECFGLLGVNGAGKtSTF-KMLTGDSVVTSGEAYLAGNsVLTEIDE---- 1990
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGV-DLTALSErelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 -VHQNMGYCPQ-FdaiNdLLTGR---EHLEFYAILRGVPEKEvckvadwgIRK--LGLMKYV---DKAaGSY----SGGN 2056
Cdd:COG1135 79 aARRKIGMIFQhF---N-LLSSRtvaENVALPLEIAGVPKAE--------IRKrvAELLELVglsDKA-DAYpsqlSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2057 MRKLSTAMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRS----ILDLLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1943-2129 |
6.93e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIDEVHQNMGYCPQ--------FDA-----INDL 2007
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnVCAL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2008 LTGRehLEFYaiLRGVPEKevcKVADWGIRKLGL-MKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2086
Cdd:PRK15439 366 THNR--RGFW--IKPAREN---AVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 2087 RRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1918-2115 |
7.31e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAY-LAGN--------SVLTEI 1988
Cdd:NF033858 1 VARLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDmadarhrrAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 devhqnmGYCPQfdainDL-------LTGREHLEFYAILRGVPEKEvckvADWGIRKL----GLMKYVDKAAGSYSGGNM 2057
Cdd:NF033858 79 -------AYMPQ-----GLgknlyptLSVFENLDFFGRLFGQDAAE----RRRRIDELlratGLAPFADRPAGKLSGGMK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2058 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE--GRSVVLTSHSMEECE 2115
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
919-1111 |
7.96e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYIQGKDI---------RTDLNAIRQNLGVCPQhnv 987
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkasnirdteRAGIVIIHQELTLVPE--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 988 lfsmLTVEEHIWFYARLKGLSAEKVKSEM----EQIVMDLGLPHKRTSRS-NQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:TIGR02633 93 ----LSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1063 TAGVDPYARRGIWDLL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:TIGR02633 169 SSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1946-2128 |
9.40e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1946 GECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL--TEIDEVHQNMGYCPQ---FDAINDLLTGRE-------- 2012
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIRAGIMLCPEdrkAEGIIPVHSVADninisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2013 -HLEFYAILRGVPEKEVckvADWGIRKLGL-MKYVDKAAGSYSGGNMRK------LSTAMAliggppVVFLDEPTTGMDP 2084
Cdd:PRK11288 359 hHLRAGCLINNRWEAEN---ADRFIRSLNIkTPSREQLIMNLSGGNQQKailgrwLSEDMK------VILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 827475625 2085 KARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1943-2128 |
9.97e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG-----NSVLTEIDEVHQNMGYCPQF--------DAINDLLT 2009
Cdd:PRK13649 30 IEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGLVFQFpesqlfeeTVLKDVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2010 GREHLefyailrGVPEKEVCKVADWGIRKLGLMK-YVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2088
Cdd:PRK13649 110 GPQNF-------GVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 827475625 2089 ALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13649 183 ELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
906-1111 |
1.08e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQ 984
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 985 HNV-----LFSMLTV-----EEHIWFYARLKGLsAEKVKSEMEQIVMDLGlphkrtSRSNQLSGGMQRKLSVALAFVGGS 1054
Cdd:PRK10790 423 DPVvladtFLANVTLgrdisEEQVWQALETVQL-AELARSLPDGLYTPLG------EQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMD---EAdilgDRIAIISHGK 1111
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQ 551
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1918-2129 |
1.42e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYkrkqkPAVDRL---CVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV---------L 1985
Cdd:PRK10762 4 LLQLKGIDKAF-----PGVKALsgaALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1986 TEIDEVHQNMGYCPQFDAINDLLTGREhleFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:PRK10762 79 AGIGIIHQELNLIPQLTIAENIFLGRE---FVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
915-1111 |
1.45e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 915 NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYIQGKDIRT----DLNA-----IRQNLGVCP 983
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQAsnirDTERagiaiIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QhnvlfsmLTVEEHIWFYARL-KG--LSAEKVKSEMEQIVMDLGL---PHKRTSrsnQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK13549 96 E-------LSVLENIFLGNEItPGgiMDYDAMYLRAQKLLAQLKLdinPATPVG---NLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
644-845 |
1.49e-11 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 68.19 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 644 MPLFMTLAWMYSVAIIIKGVVYEKEARLKETMRIMGLDNGILWLSWFISSLIPLLISAALLVLILkMGNLLPYSDPGVIY 723
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 724 LFLSSFAVVTIMQCFLISTLFSRANLAAACGGIIYFTLYLPYVLcVAWQNYVGFGAKIVVSLLSPVAFGFGceyfalfee 803
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGG-LFPLEDPPSFLQWIFSIIPFFSPIDG--------- 312
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 804 qgvgiqwsnLLSSPMQEDSYNLTTSICLMLFDSVLYAVMTWY 845
Cdd:pfam12698 313 ---------LLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1918-2128 |
1.80e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 66.75 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVY-------KRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG--------- 1981
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1982 --NSVLTEIDEVHQNmgyCPqfDAINDLLTGR----EHLEFYAILRGVPEKEvckvadwgiRKLGLMKYV-------DKA 2048
Cdd:TIGR02769 82 qrRAFRRDVQLVFQD---SP--SAVNPRMTVRqiigEPLRHLTSLDESEQKA---------RIAELLDMVglrsedaDKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2049 AGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDpkarRALWNCILSIIKE-----GRSVVLTSHSMEECEALCTRMAI 2123
Cdd:TIGR02769 148 PRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAV 223
|
....*
gi 827475625 2124 MVNGR 2128
Cdd:TIGR02769 224 MDKGQ 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1918-2128 |
1.97e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG--------DSVVTSGEAYLAGNSVLTE-- 1987
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdGEIYWSGSPLKASNIRDTEra 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 -IDEVHQNMGYCPQFDAINDLLTGRE-----HLEFYAILRGVPEKEVCKVadwgirKLGLMKyVDKAAGSYSGGNMRKLS 2061
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIFLGNEitlpgGRMAYNAMYLRAKNLLREL------QLDADN-VTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2062 TAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1933-2138 |
3.01e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1933 KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLT--GDSVVT---SGEAYLAGNSVLTEID--EVHQNMGYCPQ----- 2000
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmNDKVSGyrySGDVLLGGRSIFNYRDvlEFRRRVGMLFQrpnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2001 -FDAINDLLTG-REHlefyailRGVPEKEVCKVADWGIRKLGLMKYV-DKAAGS---YSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:PRK14271 114 pMSIMDNVLAGvRAH-------KLVPRKEFRGVAQARLTEVGLWDAVkDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSiIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1943-2109 |
3.39e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.75 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTG--DSVVTSGEAyLAGNSVLTEidEVHQNMGYCPQFDAINDLLTGREHLEFYAIL 2020
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTI-LANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2021 R---GVPEKEVCKVADWGIRKLGLMKYVDKAAGS-----YSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWN 2092
Cdd:PLN03211 168 RlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*..
gi 827475625 2093 CILSIIKEGRSVVLTSH 2109
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMH 264
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1945-2109 |
3.67e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 69.10 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDSvvTSGeaYLAGNSVLTEIDEVHQNM----GYCPQFDAINDLLTGREHLEFYAIL 2020
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2021 RgVPeKEVCKVADwgirklglMKYVDKAAGSYSGGNMR------------------KLSTAMALIGGPPVVFLDEPTTGM 2082
Cdd:PLN03140 981 R-LP-KEVSKEEK--------MMFVDEVMELVELDNLKdaivglpgvtglsteqrkRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*..
gi 827475625 2083 DPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1943-2140 |
4.46e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-------LTEIDEVHQNMGYCPQFDAINDLLTGREHL- 2014
Cdd:PRK11124 25 CPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLi 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2015 EFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKarraLWNCI 2094
Cdd:PRK11124 105 EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2095 LSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:PRK11124 181 VSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
923-1112 |
5.01e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 923 LTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVC--P---QHNVLF-------- 989
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPedrQSSGLYldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 -SMLTVEEHIWFY------ARLKGL-SAEKVK-SEMEQIVmdlglphkRTsrsnqLSGGMQRKLSVALAFVGGSKVVILD 1060
Cdd:PRK15439 362 vCALTHNRRGFWIkparenAVLERYrRALNIKfNHAEQAA--------RT-----LSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1061 EPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1914-2126 |
6.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1914 GQTDILELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV----LTEID 1989
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1990 E----VHQN-----MGYCPQFDAINDLltgREHLefyailrgVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKL 2060
Cdd:PRK13648 83 KhigiVFQNpdnqfVGSIVKYDVAFGL---ENHA--------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSiIKEGRSVVLTSHSMEECEALCTRMAIMVN 2126
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK-VKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1934-2133 |
6.14e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1934 PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-LTEIDEVHQNMGYCPQFDAINDLLTGRE 2012
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2013 --------HLEFYAILRGVPEKEVckvaDWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMD- 2083
Cdd:PRK09536 97 vvemgrtpHRSRFDTWTETDRAAV----ERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDi 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 2084 PKARRALwNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2133
Cdd:PRK09536 173 NHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1930-2109 |
6.80e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 64.55 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1930 RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGYCPQfDAIndLL 2008
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ-DTF--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2009 TG--REHlefyaILRGVP------EKEVCKV--ADWGIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLD 2076
Cdd:cd03254 90 SGtiMEN-----IRLGRPnatdeeVIEAAKEagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190
....*....|....*....|....*....|...
gi 827475625 2077 EPTTGMDPKARRALWNCILSiIKEGRSVVLTSH 2109
Cdd:cd03254 165 EATSNIDTETEKLIQEALEK-LMKGRTSIIIAH 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1919-2190 |
8.54e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.22 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKP------------------AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLA 1980
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1981 GNSVLTEIDEvhqnmgycpqfdAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKL 2060
Cdd:PRK13545 85 GSAALIAISS------------GLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2140
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2141 KFGD---GYTIILRVAGADPRLEPVMEFIERELP-GSTLKEKHRNMLQYQLSSS 2190
Cdd:PRK13545 233 HYDEflkKYNQMSVEERKDFREEQISQFQHGLLQeDQTGRERKRKKGKKTSRKF 286
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
895-1112 |
9.40e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 895 EEPAHIDPG--VYIENLMKIYSNGKVaVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtAYIQGkdiRTDL 972
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---TAPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 973 NAIRQNLGVCPQHNVLFSMLTVEEHIWFyaRLKGlsaeKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVG 1052
Cdd:PRK11247 77 AEAREDTRLMFQDARLLPWKKVIDNVGL--GLKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1053 GSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
916-1111 |
1.21e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--RTDLNAIRQNLGVCPQHNVLFSMLT 993
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 994 VEEHIWF--YArLKGL--SAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1069
Cdd:PRK10982 90 VMDNMWLgrYP-TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 1070 ARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:PRK10982 169 EVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1917-2109 |
1.22e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DILELRqltkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVHQNMG 1996
Cdd:PRK13540 3 DVIELD-----FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREH----LEFYAILRGVpeKEVCKVadwgirkLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPV 2072
Cdd:PRK13540 78 FVGHRSGINPYLTLRENclydIHFSPGAVGI--TELCRL-------FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1928-2112 |
1.23e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1928 YKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG------DSVVTSGEAY-------LA-GNSVLTEIDEVHQ 1993
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllrpqkGAVLWQGKPLdyskrglLAlRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1994 NMGYCpqfDAINDLLTGREHLefyailrGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:PRK13638 89 QIFYT---DIDSDIAFSLRNL-------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSME 2112
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
894-1112 |
1.82e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.02 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 894 EEEPAHIDPGVYIE--NLMkIYS-NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGlFPPTSGTAYIQGKDIRT 970
Cdd:PRK11174 338 GEKELASNDPVTIEaeDLE-ILSpDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 971 -DLNAIRQNLGVCPQHNVLFSMlTVEEHIwfyarLKG---LSAEKVKSEMEQ-----IV--MDLGLPHKRTSRSNQLSGG 1039
Cdd:PRK11174 416 lDPESWRKHLSWVGQNPQLPHG-TLRDNV-----LLGnpdASDEQLQQALENawvseFLplLPQGLDTPIGDQAAGLSVG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1040 MQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDEADILgDRIAIISHGKL 1112
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1943-2158 |
2.03e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 64.75 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAG---NSVLTEID-EVHQN-MGYCPQFDAINDLLTGREHLEfY 2017
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFlPPEKRrIGYVFQEARLFPHLSVRGNLR-Y 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2018 AILRGVPEKEVCKVADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSI 2097
Cdd:TIGR02142 99 GMKRARPSERRISFERV-IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2098 IKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNK-------FGD-GYTIILRVAGADPR 2158
Cdd:TIGR02142 178 HAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASpdlpwlaREDqGSLIEGVVAEHDQH 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1923-2128 |
2.44e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 62.51 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1923 QLTKVYKRKQKPAVDrLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT------EIDEVHQNMG 1996
Cdd:cd03298 2 RLDKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAappadrPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGRE-HLEfyaiLRGVPEKEVCKVAdwgiRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03298 81 LFAHLTVEQNVGLGLSpGLK----LTAEDRQAIEVAL----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1918-2109 |
2.59e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLaGNSVlteidevhqNMGY 1997
Cdd:TIGR03719 322 VIEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV---------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQFdaindlltgREHLEfyailrgvPEKEVCKVADWG--IRKLGLMK-----YV----------DKAAGSYSGGNMRKL 2060
Cdd:TIGR03719 390 VDQS---------RDALD--------PNKTVWEEISGGldIIKLGKREipsraYVgrfnfkgsdqQKKVGQLSGGERNRV 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIikeGRSVVLTSH 2109
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1900-2129 |
2.77e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1900 EDVARERQRILGGGGQTdILELRQLTkVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYL 1979
Cdd:COG3845 240 REVLLRVEKAPAEPGEV-VLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1980 AGNSVLTE------------IDEVHQNMGYCPQFDAINDLLTGREHLEFYA---ILRGVPEKEVCK--VADWGIRKLGlm 2042
Cdd:COG3845 318 DGEDITGLsprerrrlgvayIPEDRLGRGLVPDMSVAENLILGRYRRPPFSrggFLDRKAIRAFAEelIEEFDVRTPG-- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2043 kyVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMA 2122
Cdd:COG3845 396 --PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIA 473
|
....*..
gi 827475625 2123 IMVNGRF 2129
Cdd:COG3845 474 VMYEGRI 480
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1919-2143 |
2.93e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 62.89 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-LTEIDEVHQNMGY 1997
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQfdaiNDLLTGREHLEFYAILR-GVPEKEVCKVADWG-----IRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALIGG 2069
Cdd:cd03252 81 VLQ----ENVLFNRSIRDNIALADpGMSMERVIEAAKLAgahdfISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2070 PPVVFLDEPTTGMDPKARRALWNCILSIIKeGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNKFG 2143
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
904-1112 |
3.42e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMK---IYSNGK----------------VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQ 964
Cdd:PRK13546 5 VNIKNVTKeyrIYRTNKermkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 965 GkdirtDLNAIRQNLGVCPQhnvlfsmLTVEEHIWFYARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKL 1044
Cdd:PRK13546 85 G-----EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1045 SVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK13546 153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1918-2128 |
4.45e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlTEIDE---VHQN 1994
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQFDAINDLLTGREHLE---FYAIlRGVPEKEVCKVADWGIRklgLMKYVDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggFFAE-RDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2072 VVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1943-2110 |
5.16e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTS---TFKMLT--GDSVVTSGEAYLAGNSVLTE-ID--EVHQNMGYCPQFDAINDLLTGREHL 2014
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPdVDpiEVRREVGMVFQYPNPFPHLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2015 EFYAILRGV--PEKEVCKVADWGIRKLGLMKYV----DKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2088
Cdd:PRK14267 107 AIGVKLNGLvkSKKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180
....*....|....*....|..
gi 827475625 2089 ALWNCILSiIKEGRSVVLTSHS 2110
Cdd:PRK14267 187 KIEELLFE-LKKEYTIVLVTHS 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2016-2112 |
5.45e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2016 FYAILRGVPEKEVCKVADWGIRKLGL-MKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCI 2094
Cdd:PRK13631 140 FGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI 219
|
90
....*....|....*...
gi 827475625 2095 LSIIKEGRSVVLTSHSME 2112
Cdd:PRK13631 220 LDAKANNKTVFVITHTME 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1923-2127 |
7.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1923 QLTKVYKRK---QKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-----EIDEVHQN 1994
Cdd:PRK13646 7 NVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQF-------DAINdlltgREhLEFYAILRGVPEKEVCKVADWGIRKLGLMKYV-DKAAGSYSGGNMRKLSTAMAL 2066
Cdd:PRK13646 87 IGMVFQFpesqlfeDTVE-----RE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2067 IGGPPVVFLDEPTTGMDPKARRALWNCILSI-IKEGRSVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1919-2128 |
8.17e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKML----TGDS-VVTSGEAYLAGNSVLTE----ID 1989
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleQPEAgTIRVGDITIDTARSLSQqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1990 EVHQNMGYCpqFDAINdLLTGREHLEFY----AILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMA 2065
Cdd:PRK11264 82 QLRQHVGFV--FQNFN-LFPHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1919-2128 |
9.15e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-------LTEIDEV 1991
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1992 HQNMGYCPQFDAINDLLTGREHL-EFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGP 2070
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2071 PVVFLDEPTTGMDPKarraLWNCILSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG4161 161 QVLLFDEPTAALDPE----ITAQVVEIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1918-2130 |
1.04e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLT--KVYKRKQKpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGD-SVVTSGEAYLAGNSVLTE--IDEVH 1992
Cdd:TIGR02633 257 ILEARNLTcwDVINPHRK-RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRnpAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQ----FDAINDLLTGRE----HLEFYAILRGVPEKEVCKVADWGIRKLGLMKYV-DKAAGSYSGGNMRKLSTA 2063
Cdd:TIGR02633 336 AGIAMVPEdrkrHGIVPILGVGKNitlsVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2130
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
917-1093 |
1.11e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDiRTDLNAIRQNLGVCPQHNVLFSMLTVEE 996
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFYARL---KGLSAEKVKSEMEQIVMDLGLPH-KRTSRSNQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:PLN03211 160 TLVFCSLLrlpKSLTKQEKILVAESVISELGLTKcENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|....*.
gi 827475625 1069 Y-ARRGIWDLLLKYRQGRTIILSTHH 1093
Cdd:PLN03211 240 TaAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1928-2121 |
1.39e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1928 YKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEidEVHQNMGYCPQFDAINDL 2007
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2008 LTGREHLEFYAILRGVPEKEVCKVAdwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:PRK13543 97 LSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 2088 RALWNCILSIIKEGRSVVLTSHSMEECEALCTRM 2121
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
919-1067 |
1.40e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR----TDLNAIRQNLGVCPQhNVLFSM--- 991
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQ-DPLASLnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 992 LTVEEHI-----WFYARlkgLSAEKVKSEMEQIVMDLGL--------PHkrtsrsnQLSGGMQRKLSVALAFVGGSKVVI 1058
Cdd:PRK15079 115 MTIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVGLlpnlinryPH-------EFSGGQCQRIGIARALILEPKLII 184
|
....*....
gi 827475625 1059 LDEPTAGVD 1067
Cdd:PRK15079 185 CDEPVSALD 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1918-2127 |
1.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLtkVYKRKQKPAVDRL---CVGIPPGECFGLLGVNGAGKTSTFKMLTG------DSVVTSGEAYLAGN--SVLT 1986
Cdd:PRK13642 4 ILEVENL--VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefeGKVKIDGELLTAENvwNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1987 EIDEVHQNMGycPQFDAI---NDLLTGREHlefyailRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTA 2063
Cdd:PRK13642 82 KIGMVFQNPD--NQFVGAtveDDVAFGMEN-------QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNG 2127
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
906-1110 |
1.55e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.53 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYS----NGK--VAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLN------ 973
Cdd:COG4778 7 VENLSKTFTlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAqaspre 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 --AIRQN-LGVCPQH-NVL--FSML-TVEEHiwfyARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRS-NQLSGGMQRKLS 1045
Cdd:COG4778 87 ilALRRRtIGYVSQFlRVIprVSALdVVAEP----LLERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 1046 VALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEADILGDRIAIISHG 1110
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
906-1115 |
1.63e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKV---AVDGLTLGFYEGQITSFLGHNGAGKT-TTMSILTGLfpPTSGTAYIQGkDIR-----------T 970
Cdd:PRK15134 8 IENLSVAFRQQQTvrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhaseQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 971 DLNAIRQN----------LGVCPQHNV---LFSMLTVEehiwfyarlKGLSAEKVKSEMEQIVMDLGL--PHKRTSR-SN 1034
Cdd:PRK15134 85 TLRGVRGNkiamifqepmVSLNPLHTLekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIrqAAKRLTDyPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1035 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKl 1112
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR- 234
|
...
gi 827475625 1113 cCV 1115
Cdd:PRK15134 235 -CV 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1919-2158 |
1.66e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNMG 1996
Cdd:PRK13548 3 LEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWSpaELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALI------GGP 2070
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2071 PVVFLDEPTTGMDPK--------ARRALWNCILSIIkegrsVVLtsHSMEECEALCTRMAIMVNGRFRCLGSVQH-LKNK 2141
Cdd:PRK13548 160 RWLLLDEPTSALDLAhqhhvlrlARQLAHERGLAVI-----VVL--HDLNLAARYADRIVLLHQGRLVADGTPAEvLTPE 232
|
250
....*....|....*..
gi 827475625 2142 fgdgytIILRVAGADPR 2158
Cdd:PRK13548 233 ------TLRRVYGADVL 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1915-2129 |
2.06e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV---------L 1985
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1986 TEIDEVHQNMGYCPQFDAINDLLTGRehleFYAILRGVPEKEVCKVADWGIRKLGLmkYVDKAA--GSYSGGNMRKLSTA 2063
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLGQ----LPHKGGIVNRRLLNYEAREQLEHLGV--DIDPDTplKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2064 MALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
916-1121 |
2.15e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMLTV 994
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHI------WFYA--RLKGLSAEKVksemEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:PRK10575 103 RELVaigrypWHGAlgRFGAADREKV----EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 1067 DPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFL 1121
Cdd:PRK10575 179 DIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
906-1112 |
2.45e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNG--------KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--------- 968
Cdd:PRK10419 6 VSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 969 --RTDLNAIRQN-LG-VCPQHNVLFSMLTVEEHiwfyarLKGLS----AEKVKSEMEQIVMDLGLPHKRTSrsnQLSGGM 1040
Cdd:PRK10419 86 afRRDIQMVFQDsISaVNPRKTVREIIREPLRH------LLSLDkaerLARASEMLRAVDLDDSVLDKRPP---QLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1041 QRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1112
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
922-1092 |
2.81e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGlfPPTSGtaYIQGkDIRTDLNAIRQNL-----GVCPQHNVLFSMLTVEE 996
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISGFPKKQETfarisGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFYARLKgLSAEKVKSE--------MEQIVMD------LGLPHkrtsrSNQLSGGMQRKLSVALAFVGGSKVVILDEP 1062
Cdd:PLN03140 973 SLIYSAFLR-LPKEVSKEEkmmfvdevMELVELDnlkdaiVGLPG-----VTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 1063 TAGVDPYAR-------RGIWDlllkyrQGRTIILSTH 1092
Cdd:PLN03140 1047 TSGLDARAAaivmrtvRNTVD------TGRTVVCTIH 1077
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
930-1111 |
3.66e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.63 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdirtdlnairqnLGVCPQHNVLFSMlTVEEHIWFYARLkglSA 1009
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQNG-TIRENILFGKPF---DE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1010 EKVKSEME--QIVMDLG-LPHK-RT---SRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLL--K 1080
Cdd:cd03250 95 ERYEKVIKacALEPDLEiLPDGdLTeigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgL 174
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 1081 YRQGRTIILSTHHMD---EAdilgDRIAIISHGK 1111
Cdd:cd03250 175 LLNNKTRILVTHQLQllpHA----DQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
929-1067 |
3.67e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.81 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYIQGKDIRTDLNAIRQNLGVCPQHNVLFSMLTVEEHIWFYARLK 1005
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1006 GlsaekvksemEQIVmdlglphkrtsRSnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:cd03233 112 G----------NEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1943-2128 |
3.73e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.63 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvlteidevhqnMGYCPQFDAI-NDllTGREHlefyaILR 2021
Cdd:cd03250 28 VPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIqNG--TIREN-----ILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2022 GVPE-----KEV----CKVADWGIRKLGLMKYV-DKAAgSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALW 2091
Cdd:cd03250 89 GKPFdeeryEKVikacALEPDLEILPDGDLTEIgEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 827475625 2092 -NCILSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2128
Cdd:cd03250 168 eNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
930-1110 |
3.79e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIqgkdirtdlnaIRQNLGVCPQHNVLFSMlTVEEHIWFYARLKGLSA 1009
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRENILFGSDFESERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1010 EK-VKSEMEQIVMDLGLPHKRTS---RSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QG 1084
Cdd:PLN03232 711 WRaIDVTALQHDLDLLPGRDLTEigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKG 790
|
170 180
....*....|....*....|....*.
gi 827475625 1085 RTIILSTHHMDEADILgDRIAIISHG 1110
Cdd:PLN03232 791 KTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1917-2138 |
3.84e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DILELRQLTKvykRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTST----FKMLTGDSVVTSGEAYLAGNSVL------T 1986
Cdd:PRK10418 3 QQIELRNIAL---QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVApcalrgR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1987 EIDEVHQNmgycPQfDAINDLLTGREHLEFYAILRGVPEKEVCKVAdwGIRKLGLMKyVDKAAGSY----SGGNMRKLST 2062
Cdd:PRK10418 80 KIATIMQN----PR-SAFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLEN-AARVLKLYpfemSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2063 AMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1916-2109 |
4.21e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYK--RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVH 1992
Cdd:PRK10535 2 TALLELKDIRRSYPsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 Q----NMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIG 2068
Cdd:PRK10535 82 QlrreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 2069 GPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
897-1112 |
4.30e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.58 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 897 PAHIDpgVYIENLMKIYS-NGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNA 974
Cdd:cd03369 2 PEHGE--IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 975 IRQNLGVCPQHNVLFSMlTVEEHiwfyarlkgLSAEKVKSEmEQIVMDLglphKRTSRSNQLSGGMQRKLSVALAFVGGS 1054
Cdd:cd03369 80 LRSSLTIIPQDPTLFSG-TIRSN---------LDPFDEYSD-EEIYGAL----RVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1055 KVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMDE-ADIlgDRIAIISHGKL 1112
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1919-2128 |
4.35e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 58.70 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL---TEIDEVHQNM 1995
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQ-FDAINDLlTGREHLEFYAI-LRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:cd03262 79 GMVFQqFNLFPHL-TVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2074 FLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1919-2112 |
4.47e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRK---QKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSG------------------EA 1977
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1978 YLAGNSV-------LTEIDEVHQNMGYCPQFdAINDLL--TGREHLEFYAILRGVPEKEVCKVADWGIRKLGL-MKYVDK 2047
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2048 AAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSME 2112
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1935-2142 |
5.08e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvltEIDEVHQNMGycpqfdaINDLLTGREHL 2014
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAG-------LSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2015 EFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCI 2094
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 2095 LSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKF 2142
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1951-2134 |
5.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1951 LLGVNGAGKTSTFKMLTGDSVVTSGEAYL------AGNSVLTEIDEVHQNMGYC---PQFDAINDllTGREHLEFYAILR 2021
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVfqfPEYQLFQE--TIEKDIAFGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2022 GVPEKEVCKVADWGIRKLGLMK-YVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE 2100
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKE 199
|
170 180 190
....*....|....*....|....*....|....*
gi 827475625 2101 -GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2134
Cdd:PRK13645 200 yKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
928-1112 |
7.91e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 928 YEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI--RTDLNAIRQNLGVCPQHNV---LFSMLTVE-----EH 997
Cdd:PRK10982 272 HKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFALVTEERRstgIYAYLDIGfnsliSN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 998 IWFYARLKGL-SAEKVKSEMEQIV--MDLGLPHKRTSRSNqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGI 1074
Cdd:PRK10982 352 IRNYKNKVGLlDNSRMKSDTQWVIdsMRVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 827475625 1075 WDLLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1112
Cdd:PRK10982 431 YQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
919-1111 |
8.14e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS--GTAYIQG-----KDIRtDLNA-----IRQNLGVCPQhn 986
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIR-DSEAlgiviIHQELALIPY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 987 vlfsmLTVEEHIWF---YARLKGLSAEKVKSEMEQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPT 1063
Cdd:NF040905 93 -----LSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 827475625 1064 AGVDPYARRGIWDLLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:NF040905 168 AALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
930-1130 |
1.01e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.50 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQHNVLFSMlTVEEHIwfyarlkGLS 1008
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTPFLFSD-TVANNI-------ALG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1009 -AEKVKSEMEQI-----VMD--LGLPHKRTS----RSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWD 1076
Cdd:PRK10789 413 rPDATQQEIEHVarlasVHDdiLRLPQGYDTevgeRGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1077 LLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKLCCVGSSLFLKTQlgTGYY 1130
Cdd:PRK10789 493 NLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQ--SGWY 543
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
937-1068 |
1.31e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 937 GHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQhnvLFSMLTVEEHIWFYARLKGLSAEKVKSE 1015
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPG---LKADLSTLENLHFLCGLHGRRAKQMPGS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1016 MEQIVmdlGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:PRK13543 121 ALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
925-1092 |
1.48e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 925 LGFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQnlgvcpqhnvLFSmlTVeehiwF-- 1000
Cdd:COG4615 353 LTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQ----------LFS--AV-----Fsd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1001 ---YARLKGLSAEKVKSEMEQIVMDLGLPHKrTSRSN------QLSGGmQRK-LSVALAFVGGSKVVILDEPTAGVDPYA 1070
Cdd:COG4615 415 fhlFDRLLGLDGEADPARARELLERLELDHK-VSVEDgrfsttDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDPEF 492
|
170 180
....*....|....*....|....*..
gi 827475625 1071 RRgiW---DLL--LKyRQGRTIILSTH 1092
Cdd:COG4615 493 RR--VfytELLpeLK-ARGKTVIAISH 516
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1919-2109 |
2.16e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.15 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGeaylagnsvlteIDEVHQN--MG 1996
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------IVTWGSTvkIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQFdaindlltgrehlefyailrgvpekevckvadwgirklglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFLD 2076
Cdd:cd03221 67 YFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|...
gi 827475625 2077 EPTTGMDPKARRALwncILSIIKEGRSVVLTSH 2109
Cdd:cd03221 96 EPTNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2050-2128 |
2.22e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 2.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2050 GSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1918-2128 |
2.27e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEA-YLAGNSVLTEIDE------ 1990
Cdd:PRK11701 6 LLSVRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYAlseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 ----------VHQN--MGYCPQFDA---INDLL--TGREHlefYAILRgvpekevCKVADWGIR-KLGLMKyVDKAAGSY 2052
Cdd:PRK11701 84 rrllrtewgfVHQHprDGLRMQVSAggnIGERLmaVGARH---YGDIR-------ATAGDWLERvEIDAAR-IDDLPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2053 SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
917-1110 |
2.48e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTG--LFPPTSGTAYIQGKDIRTDLNAIrqnlgvcpqhnvlfsmltv 994
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 eEHIW----FYARLKGLSAekvksemeqivMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP-Y 1069
Cdd:COG2401 104 -DAIGrkgdFKDAVELLNA-----------VGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 827475625 1070 ARRG--IWDLLLKyRQGRTIILSTHHMD-EADILGDRIAIISHG 1110
Cdd:COG2401 172 AKRVarNLQKLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
911-1110 |
2.59e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 911 KIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSIL-----TGLFppTSGTAYIQGKDIRTdlnAIRQNLGVCPQH 985
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDS---SFQRSIGYVQQQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKgLSAEKVKSE----MEQIVMDLGLphkrTSRSNQLSG----GM---QRK-LSVALAFVGG 1053
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSAYLR-QPKSVSKSEkmeyVEEVIKLLEM----ESYADAVVGvpgeGLnveQRKrLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1054 SKVVI-LDEPTAGVDPYARRGIWDLLLKY-RQGRTiILSTHHMDEADILG--DRIAIISHG 1110
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLaDHGQA-ILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
919-1118 |
3.22e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQG-------------------KDIRTDLNAiRQNL 979
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifQDPSTSLNP-RQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GvcpqhnvlfsmltveEHIWFYARLK-GLSAEKVKSEMEQIVMDLGL-PHKRTSRSNQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK15112 107 S---------------QILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1118
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
917-1112 |
3.28e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.54 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKT-TTMSILtGLFPP----TSGTAYIQGKDIRT----DLNAIRQN--------- 978
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGlserELRRIRGNriamifqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 979 ---LgvcpqhNVLFsmlTVEEHIWFYARL-KGLSAEKVKSEMEQIVMDLGLPHKRtSRSN----QLSGGMQRKLSVALAF 1050
Cdd:COG4172 102 mtsL------NPLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPE-RRLDayphQLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1051 VGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHhmDeadiLG------DRIAIISHGKL 1112
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH--D----LGvvrrfaDRVAVMRQGEI 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
923-1092 |
3.34e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 923 LTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI----RTDLNAIRQNLGvcpqhnvLFSMLTVEEHI 998
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLG-------LKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 999 WFYARLKGlSAEKVKSEMEQIVMDLGLPHKRTSrsnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL 1078
Cdd:PRK13541 92 KFWSEIYN-SAETLYAAIHYFKLHDLLDEKCYS----LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
170
....*....|....*
gi 827475625 1079 -LKYRQGRTIILSTH 1092
Cdd:PRK13541 167 vMKANSGGIVLLSSH 181
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
919-1116 |
3.38e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT----DLNAIRQNL---------GVCPQH 985
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIqfifqdpyaSLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLtveEHIWFYARLKGLSAEKVKSEMEQIVmdlGL-PHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1064
Cdd:PRK10261 419 TVGDSIM---EPLRVHGLLPGKAAAARVAWLLERV---GLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 1065 GVDPYARRGIWDLLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1116
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1915-2090 |
3.81e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlteIDEVHQN 1994
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQFD--AINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPV 2072
Cdd:PRK11432 78 RDICMVFQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|....*...
gi 827475625 2073 VFLDEPTTGMDPKARRAL 2090
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSM 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
929-1117 |
4.17e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIWF-----YA 1002
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIANNIAYarteqYS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1003 RLKGLSAEKVKSEMEQIV-MDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKY 1081
Cdd:PRK11176 447 REQIEEAARMAYAMDFINkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
170 180 190
....*....|....*....|....*....|....*.
gi 827475625 1082 RQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGS 1117
Cdd:PRK11176 527 QKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGT 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
930-1091 |
4.83e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.29 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVEEHIWfYARLkGLS 1008
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFND-TIAYNIA-YGRP-DAS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1009 AEKVKS--EMEQI---VMDL-----------GLphkrtsrsnQLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPY 1069
Cdd:COG5265 461 EEEVEAaaRAAQIhdfIESLpdgydtrvgerGL---------KLSGGeKQR---VAIArtLLKNPPILIFDEATSALDSR 528
|
170 180
....*....|....*....|....*..
gi 827475625 1070 ARRGIWDLLLKYRQGRT--II---LST 1091
Cdd:COG5265 529 TERAIQAALREVARGRTtlVIahrLST 555
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1933-2109 |
5.32e-08 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 56.08 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1933 KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEIDEVHQN-----MGYCPQfDAI--N 2005
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVTLDslrraIGVVPQ-DTVlfN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2006 DLLtgrehleFYAILRGVPE------KEVCKVADWGIRKLGLMKYVDKAAGS----YSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03253 89 DTI-------GYNIRYGRPDatdeevIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKeGRSVVLTSH 2109
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
904-1117 |
7.24e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIENLMKIYSNGKVAVDgLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdIRtdlnairqnLGVCP 983
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSD-VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-LR---------IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSM--LTVEEhiwfYARLKGlsaeKVKSEmeqivmDLGLPHKRTSRSN-------QLSGG-MQRKLsVALAFVGG 1053
Cdd:PRK09544 74 QKLYLDTTlpLTVNR----FLRLRP----GTKKE------DILPALKRVQAGHlidapmqKLSGGeTQRVL-LARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1054 SKVVILDEPTAGVDPYARRGIWDLLLKYRQ--GRTIILSTH--HMDEADIlgDRIAIISHgKLCCVGS 1117
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHdlHLVMAKT--DEVLCLNH-HICCSGT 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1945-2109 |
1.64e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGdsvvtsgeaylagnsvlteidEVHQNMG-YC--PQFDAINDLLTGREHLEFYAILR 2021
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSELQNYFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2022 GVPEKEVCKVA--------------------------DWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:cd03236 84 EGDVKVIVKPQyvdlipkavkgkvgellkkkdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1943-2109 |
1.81e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTG-----DSVVTSGEAYLAGNSVLT--------EIDEVHQNMGYCPQFDAINDLLT 2009
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmdvielrrRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2010 GrehLEFYAILRGvpEKEVCKVADWGIRKLGLMKYV----DKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPK 2085
Cdd:PRK14247 106 G---LKLNRLVKS--KKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE 180
|
170 180
....*....|....*....|....
gi 827475625 2086 ARRALWNCILSIIKEgRSVVLTSH 2109
Cdd:PRK14247 181 NTAKIESLFLELKKD-MTIVLVTH 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1945-2127 |
1.88e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV--LTEIdEVHQnMG-Y-CPQFDAINDLLTGREHlefyaIL 2020
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPA-KAHQ-LGiYlVPQEPLLFPNLSVKEN-----IL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2021 RGVPEKEVC--KVADWgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSII 2098
Cdd:PRK15439 109 FGLPKRQASmqKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELL 187
|
170 180
....*....|....*....|....*....
gi 827475625 2099 KEGRSVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:PRK15439 188 AQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1942-2109 |
2.49e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1942 GIP---PGECFGLLGVNGAGKTSTFKMLTG---------------DSVVTsgeaYLAGNSVLT--------EIDEVHQnm 1995
Cdd:COG1245 92 GLPvpkKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswDEVLK----RFRGTELQDyfkklangEIKVAHK-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 gycPQF-DAINDLLTG--REhlefyaILRGVPEKevcKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPV 2072
Cdd:COG1245 166 ---PQYvDLIPKVFKGtvRE------LLEKVDER---GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 827475625 2073 VFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSH 2109
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1919-2146 |
2.59e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.30 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDS--VVTSGEAYLAGNSVLT-EIDE-VHQN 1994
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDlPPEErARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1995 MGYCPQfdaindlltgrEHLEFyailRGVpekevcKVADwgirklgLMKYVDKaagSYSGGNMRKLSTAMALIGGPPVVF 2074
Cdd:cd03217 79 IFLAFQ-----------YPPEI----PGV------KNAD-------FLRYVNE---GFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2075 LDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEAL-CTRMAIMVNGRFRCLGS---VQHLKNKfgdGY 2146
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDkelALEIEKK---GY 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1943-2128 |
2.67e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 53.99 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL-TEIDE-----------------VHQNMGYcpqfdAI 2004
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTaLPPAErpvsmlfqennlfphltVAQNIGL-----GL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2005 N-DL-LTGREHLEFYAILRgvpekevckvadwgirKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGM 2082
Cdd:COG3840 97 RpGLkLTAEQRAQVEQALE----------------RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 827475625 2083 DPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:COG3840 161 DPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1935-2176 |
3.15e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT----EIDEVHQNMGYCPQ--FDAINDLL 2008
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2009 TG----REHLEFYAILRGvpeKEVCKVADWGIRKLGLM-KYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMD 2083
Cdd:PRK10261 419 TVgdsiMEPLRVHGLLPG---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2084 PKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKFGDGYT--IILRVAGADP-RL 2159
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTrkLMAAVPVADPsRQ 575
|
250
....*....|....*..
gi 827475625 2160 EPVMEFIERELPGSTLK 2176
Cdd:PRK10261 576 RPQRVLLSDDLPSNIHL 592
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2048-2130 |
3.51e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2048 AAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
...
gi 827475625 2128 RFR 2130
Cdd:PRK13549 482 KLK 484
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1918-2083 |
3.51e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYK--RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-----EIDE 1990
Cdd:PRK11629 5 LLQCDNLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaaKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCPQFDAINDLLTGREHLEFYAILRGVPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGP 2070
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170
....*....|...
gi 827475625 2071 PVVFLDEPTTGMD 2083
Cdd:PRK11629 165 RLVLADEPTGNLD 177
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1035-1092 |
3.89e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 3.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1035 QLSGGMQRKLSVALAF----VGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQ-GRTIILSTH 1092
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITH 139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1943-2109 |
3.93e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLaGNSVlteidevhqNMGYCPQFdaindlltgREHLEfyailrg 2022
Cdd:PRK11819 347 LPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------KLAYVDQS---------RDALD------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2023 vPEKEVCKVADWG--IRKLGLMK-----YV----------DKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPK 2085
Cdd:PRK11819 401 -PNKTVWEEISGGldIIKVGNREipsraYVgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
170 180
....*....|....*....|....
gi 827475625 2086 ARRALWNCILSIikeGRSVVLTSH 2109
Cdd:PRK11819 480 TLRALEEALLEF---PGCAVVISH 500
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
906-1112 |
4.16e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAV-DGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYIQGKDIRT-DLNAIRQNLGVCP 983
Cdd:cd03289 5 VKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNVLFSMLT----------VEEHIWFYARLKGLSA--EKVKSEMEQIVMDLGLphkrtsrsnQLSGGMQRKLSVALAFV 1051
Cdd:cd03289 84 QKVFIFSGTFrknldpygkwSDEEIWKVAEEVGLKSviEQFPGQLDFVLVDGGC---------VLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1052 GGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKL 1112
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1918-2128 |
5.08e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKrkQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG--------DSVVTSGEAYLAGNSVLTE-- 1987
Cdd:PRK13549 5 LLEMKNITKTFG--GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyeGEIIFEGEELQASNIRDTEra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1988 -IDEVHQNMGYCPQFDAINDLLTGREhlefyaILRGvpekevcKVADWG---------IRKLGLMKYVDKAAGSYSGGNM 2057
Cdd:PRK13549 83 gIAIIHQELALVKELSVLENIFLGNE------ITPG-------GIMDYDamylraqklLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2058 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRALwnciLSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVL----LDIIRDlkahGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
906-1095 |
5.28e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.30 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IEN--LMKIY-SNGKVAVDGLTLGFYE---------------GQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYIQGKD 967
Cdd:TIGR01271 1203 IENphAQKCWpSGGQMDVQGLTAKYTEagravlqdlsfsvegGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVS 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 968 IRT-DLNAIRQNLGVCPQHNVLFS----------MLTVEEHIWFYARLKGLSA--EKVKSEMEQIVMDLGLphkrtsrsn 1034
Cdd:TIGR01271 1282 WNSvTLQTWRKAFGVIPQKVFIFSgtfrknldpyEQWSDEEIWKVAEEVGLKSviEQFPDKLDFVLVDGGY--------- 1352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1035 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHHMD 1095
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
919-1117 |
5.87e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIR------TDLNAIRQ---------NLGVCP 983
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqvIELSEQSAaqmrhvrgaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 984 QHNV--LFSMLTVEEHIWFYARL-KGLSAEKVKSEMEQIVMDLGLPHKRTSRS---NQLSGGMQRKLSVALAFVGGSKVV 1057
Cdd:PRK10261 111 QEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSrypHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1058 ILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
919-1092 |
6.58e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYIQGKDI----RTDLNAIR--------------- 976
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaeqismifqdpmtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 977 --------QNLGVCPQHNVLFSMLTVEEHIwfyarlKGLSAEKVKSEMEQIVMdlgLPHkrtsrsnQLSGGMQRKLSVAL 1048
Cdd:PRK09473 111 npymrvgeQLMEVLMLHKGMSKAEAFEESV------RMLDAVKMPEARKRMKM---YPH-------EFSGGMRQRVMIAM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1049 AFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTH 1092
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1945-2083 |
8.54e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGD---SVVTSGEAYLAGNSVLtEIDEVHQ-NMGYCPQFDAINDLLTGREHLEFYAIL 2020
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYK-EFAEKYPgEIIYVSEEDVHFPTLTVRETLDFALRC 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2021 RGvpekevckvaDWGIRKLglmkyvdkaagsySGGNMRKLSTAMALIGGPPVVFLDEPTTGMD 2083
Cdd:cd03233 111 KG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1945-2128 |
8.60e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.18 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVL----TEIDEVHQNMGYCPQfdaINDLLTGR---EHLEFY 2017
Cdd:PRK10908 27 PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIGMIFQ---DHHLLMDRtvyDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2018 AILRGVPEKEVCKVADWGIRKLGLMkyvDKAAG---SYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDpkarRALWNCI 2094
Cdd:PRK10908 104 LIIAGASGDDIRRRVSAALDKVGLL---DKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 827475625 2095 LSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2128
Cdd:PRK10908 177 LRLFEEfnrvGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
930-1067 |
8.68e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTG-----LFPPTSGTAY--IQGKDIRtdlNAIRQNLGVCPQHNVLFSMLTVEEHIWFYA 1002
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITYdgITPEEIK---KHYRGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 827475625 1003 RLK-------GLSAEKVKSEMEQIVMD-LGLPHKR-TSRSNQL----SGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:TIGR00956 164 RCKtpqnrpdGVSREEYAKHIADVYMAtYGLSHTRnTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1933-2109 |
1.18e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 53.63 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1933 KPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG--DsvVTSGEAYLAGNSVlTEID--EVHQNMGYCPQfDAIndLL 2008
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyD--PTSGRILIDGVDI-RDLTleSLRRQIGVVPQ-DTF--LF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2009 TG--REhlefyAILRGVPE------KEVCKVA---DWgIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFL 2075
Cdd:COG1132 427 SGtiRE-----NIRYGRPDatdeevEEAAKAAqahEF-IEALpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190
....*....|....*....|....*....|....
gi 827475625 2076 DEPTTGMDPKARRALWNCILSIIKeGRSVVLTSH 2109
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2045-2129 |
1.46e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2045 VDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIM 2124
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVM 477
|
....*
gi 827475625 2125 VNGRF 2129
Cdd:NF040905 478 NEGRI 482
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
922-1112 |
1.63e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 922 GLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQHNVLFS------MLTV 994
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFSgtvrfnIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEH----IWfyarlKGLSAEKVKSEMEQivMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYA 1070
Cdd:PLN03232 1334 SEHndadLW-----EALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 827475625 1071 RRGIWDLLLKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1112
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1945-2111 |
2.01e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1945 PGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEaylagnsvlteIDEVHQ-NMGYCPQ---FDAINDLLTGRehleFYAIL 2020
Cdd:PRK09544 29 PGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-----------IKRNGKlRIGYVPQklyLDTTLPLTVNR----FLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2021 RGVPEKEVCKVadwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE 2100
Cdd:PRK09544 94 PGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|..
gi 827475625 2101 -GRSVVLTSHSM 2111
Cdd:PRK09544 170 lDCAVLMVSHDL 181
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1934-2083 |
2.24e-06 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 52.82 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1934 PAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEID--EVHQNMGYCPQFDAI------- 2004
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIDrhTLRQFINYLPQEPYIfsgsile 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2005 NDLLTGREHLEFYAIlrgvpeKEVCKVADwgIRK------LGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:TIGR01193 567 NLLLGAKENVSQDEI------WAACEIAE--IKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 827475625 2079 TTGMD 2083
Cdd:TIGR01193 639 TSNLD 643
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
906-1109 |
2.31e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.84 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTSGTayiqgkdirtdlnairqnLGVC 982
Cdd:cd03223 3 LENLSLATPDGRVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGR------------------IGMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 983 PQHNVLFsmltVEEHIWFYA-RLKglsaekvksemEQIVmdlgLPHKRTsrsnqLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:cd03223 62 EGEDLLF----LPQRPYLPLgTLR-----------EQLI----YPWDDV-----LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1062 PTAGVDPYARRGIWDLLlkyRQGRTIILSTHHMDEADILGDRIAIISH 1109
Cdd:cd03223 118 ATSALDEESEDRLYQLL---KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
920-1117 |
2.32e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 920 VDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAIRQNLGVcpQHNVLFSmltveehiw 999
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL--RENILFG--------- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1000 fyarlKGLSAEKVKSEMEQIVM--DLG-LPH-KRTS---RSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARR 1072
Cdd:TIGR00957 723 -----KALNEKYYQQVLEACALlpDLEiLPSgDRTEigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 1073 GIWDLLLKYR---QGRTIILSTHHMDEADILgDRIAIISHGKLCCVGS 1117
Cdd:TIGR00957 798 HIFEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1919-2136 |
2.45e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlTEIDEVH---QNM 1995
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHardRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAINDLLTGREHLEFYaiLRGVPEKEVCKVA--DWGIRKLGLMKYVDKAAGSY----SGGNMRKLSTAMALIGG 2069
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFG--LTVLPRRERPNAAaiKAKVTQLLEMVQLAHLADRYpaqlSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 2070 PPVVFLDEPTTGMDPKARRALWNCILSIIKEGR--SVVLTsHSMEECEALCTRMAIMVNGRFRCLGSVQ 2136
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKftSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
937-1067 |
2.48e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 937 GHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFSMlTVE-------EH----IWfyarl 1004
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSG-TVRfnldpfnEHndadLW----- 1345
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1005 KGLSAEKVKSEMEQivMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1067
Cdd:PLN03130 1346 ESLERAHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1919-2109 |
2.87e-06 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 50.69 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGY 1997
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1998 CPQfDAI--NDllTGREHLEFYAilRGVPEKEVCKVAdwgiRKLGLMKYVDKAAGSY-----------SGGNMRKLSTAM 2064
Cdd:cd03251 81 VSQ-DVFlfND--TVAENIAYGR--PGATREEVEEAA----RAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 2065 ALIGGPPVVFLDEPTTGMDPKARRALWNCiLSIIKEGRSVVLTSH 2109
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAA-LERLMKNRTTFVIAH 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1918-2127 |
3.01e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLT--GD---SVVTSGEAYLAGNSVL---TEID 1989
Cdd:PRK14239 5 ILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYsprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1990 EVHQNMGYCpqFDAINDL-LTGREHLEFYAILRGVPEKEVC-KVADWGIRKLGLMKYV-----DKAAGsYSGGNMRKLST 2062
Cdd:PRK14239 83 DLRKEIGMV--FQQPNPFpMSIYENVVYGLRLKGIKDKQVLdEAVEKSLKGASIWDEVkdrlhDSALG-LSGGQQQRVCI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2063 AMALIGGPPVVFLDEPTTGMDPKARRALWNCILSiIKEGRSVVLTSHSMEECEALCTRMAIMVNG 2127
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1924-2156 |
4.30e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1924 LTKVYKRKQKPAVDRL--CVG-IPPGECFGLLGVNGAGKTSTFKMLTGDSV-----VTSGEAYlagnSVLTEIDEVHQNM 1995
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILkpMDGlIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhigVEGVITY----DGITPEEIKKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 G---YCPQFDAINDLLTGREHLEFYAILR-------GVPEKE-VCKVADWGIRKLGLMKYVDKAAGS-----YSGGNMRK 2059
Cdd:TIGR00956 138 GdvvYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2060 LSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTS--HSMEECEALCTRMAIMVNGRFRCLGSVQH 2137
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
250 260
....*....|....*....|
gi 827475625 2138 LKNKFGD-GYTIILRVAGAD 2156
Cdd:TIGR00956 298 AKQYFEKmGFKCPDRQTTAD 317
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2042-2112 |
6.08e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2042 MKYVDK------AAGSY----SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSM 2111
Cdd:PRK10619 133 VKYLAKvgiderAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
.
gi 827475625 2112 E 2112
Cdd:PRK10619 213 G 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
904-1067 |
6.53e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIE--NLMKIYSNGKVAVDGLTLgfYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtayiqgkDIRTDLNairqnLGV 981
Cdd:COG1245 340 TLVEypDLTKSYGGFSLEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLK-----ISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMLTVEEHiwfyarLKGLSAEKVKSEM--EQIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVIL 1059
Cdd:COG1245 406 KPQYISPDYDGTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
....*...
gi 827475625 1060 DEPTAGVD 1067
Cdd:COG1245 480 DEPSAHLD 487
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
930-1094 |
6.93e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 49.25 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRTDLNAI-----RQNLGVCPQHNVLFSMlTVEEHIWFYARL 1004
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1005 kglSAEKVKSEME----QIVMDLgLPHKRTS----RSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY-----AR 1071
Cdd:cd03290 106 ---NKQRYKAVTDacslQPDIDL-LPFGDQTeigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQ 181
|
170 180
....*....|....*....|...
gi 827475625 1072 RGIWDLLLKYRqgRTIILSTHHM 1094
Cdd:cd03290 182 EGILKFLQDDK--RTLVLVTHKL 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1930-2138 |
8.85e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.88 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1930 RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDEV--HQNMGYCPQfdaiNDL 2007
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP-LVQYDHHylHRQVALVGQ----EPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2008 LTGREHLEFYAI-LRGVPEKEVCKVA-----DWGIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPT 2079
Cdd:TIGR00958 566 LFSGSVRENIAYgLTDTPDEEIMAAAkaanaHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 2080 TGMDPKARRAL--WNCilsiiKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:TIGR00958 646 SALDAECEQLLqeSRS-----RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1935-2129 |
9.58e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE---------IDEVHQNMGYCPQFDAIN 2005
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKsskealengISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2006 DLLTGREHLEFYAILRGVPEKEVCKVADwgirKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPK 2085
Cdd:PRK10982 93 NMWLGRYPTKGMFVDQDKMYRDTKAIFD----ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 827475625 2086 ARRALWNCILSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1916-2128 |
1.06e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1916 TDILELRQLTKVYKRK--QKPAVDRLCVGIPPGECFGLLGVNGAGKT----STFKMLTGDSVV-TSGEAYLAGNSVLtEI 1988
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLL-HA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DE-----VHQN---MGYCPQFDAINDLLTGREHL-EFYAILRGVPEK----EVCKVADW-GIRKlglmkyvdkAAG---- 2050
Cdd:PRK15134 82 SEqtlrgVRGNkiaMIFQEPMVSLNPLHTLEKQLyEVLSLHRGMRREaargEILNCLDRvGIRQ---------AAKrltd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2051 ---SYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMEECEALCTRMA 2122
Cdd:PRK15134 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQ----ILQLLRElqqelNMGLLFITHNLSIVRKLADRVA 228
|
....*.
gi 827475625 2123 IMVNGR 2128
Cdd:PRK15134 229 VMQNGR 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
906-1119 |
1.55e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.19 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSG-----------TAYIQG------- 965
Cdd:TIGR03269 3 VKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekCGYVERpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 966 --------KDIRTDL--------NAIRQNLGVCPQHN-VLFSMLTVEEHIWFYARLKGLSAEK-VKSEMEQIVMdLGLPH 1027
Cdd:TIGR03269 82 cpvcggtlEPEEVDFwnlsdklrRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEaVGRAVDLIEM-VQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1028 KRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLK--YRQGRTIILSTHHMDEADILGDRIA 1105
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....
gi 827475625 1106 IISHGKLCCVGSSL 1119
Cdd:TIGR03269 241 WLENGEIKEEGTPD 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
930-1112 |
1.63e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 930 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIqgkdirtdlnaIRQNLGVCPQHNVLFSMlTVEEHIWFYARLKGLSA 1009
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1010 EKVkSEMEQIVMDLG-LP-HKRTS---RSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-Q 1083
Cdd:PLN03130 711 ERA-IDVTALQHDLDlLPgGDLTEigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190
....*....|....*....|....*....|..
gi 827475625 1084 GRTIILST---HHMDEAdilgDRIAIISHGKL 1112
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMI 817
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1923-2083 |
1.67e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.83 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1923 QLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEID-EVHQNMGYCPQF 2001
Cdd:PRK10253 12 QLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2002 DAINDLLTGRE--------HLEFYAILRGVPEKEVCKvadwGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVV 2073
Cdd:PRK10253 90 ATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170
....*....|
gi 827475625 2074 FLDEPTTGMD 2083
Cdd:PRK10253 166 LLDEPTTWLD 175
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
923-1094 |
2.39e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 923 LTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQG----KDIrtDLNAIRQNLGVCPQHNVLFSML---TVE 995
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQDPLLFSNSiknNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 996 EHIWFYARLKGLSAE---------------------------------------KVKSEMEQI----VMDL--------- 1023
Cdd:PTZ00265 482 YSLYSLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIkdseVVDVskkvlihdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1024 --GLPHKRT----SRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHM 1094
Cdd:PTZ00265 562 vsALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
917-1083 |
2.58e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYIQGKDIRTdLNAiRQNLGVCPQHNVLFS------ 990
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHN-LNR-RQLLPVRHRIQVVFQdpnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 991 --MLTVEEHIWFYARL--KGLSAEKVKSEMEQIVMDLGL-PHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1065
Cdd:PRK15134 376 npRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170
....*....|....*...
gi 827475625 1066 VDPYARRGIWDLLLKYRQ 1083
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQ 473
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1918-2115 |
2.69e-05 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 47.85 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYK-RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV-LTEIDEVHQNM 1995
Cdd:cd03248 11 IVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQfdaiNDLLTGREHLEFYAI-LRGVPEKEVCKVADWG-----IRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALI 2067
Cdd:cd03248 91 SLVGQ----EPVLFARSLQDNIAYgLQSCSFECVKEAAQKAhahsfISELasGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 827475625 2068 GGPPVVFLDEPTTGMDPKARRALwNCILSIIKEGRSVVLTSHSMEECE 2115
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVE 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
904-1067 |
2.78e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 904 VYIE--NLMKIYSNGKVAVDGLTLgfYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtayiqgkDIRTDLnairqNLGV 981
Cdd:PRK13409 339 TLVEypDLTKKLGDFSLEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPEL-----KISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 982 CPQHNVLFSMLTVEEhiWFYARLKGLSAEKVKSEmeqIVMDLGLPHKRTSRSNQLSGG-MQRkLSVALAFVGGSKVVILD 1060
Cdd:PRK13409 405 KPQYIKPDYDGTVED--LLRSITDDLGSSYYKSE---IIKPLQLERLLDKNVKDLSGGeLQR-VAIAACLSRDADLYLLD 478
|
....*..
gi 827475625 1061 EPTAGVD 1067
Cdd:PRK13409 479 EPSAHLD 485
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1919-2142 |
3.14e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 49.03 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkpAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTG--DSVVTSGEaylagnsvlteideVHQNMG 1996
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGR--------------IIYHVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1997 YCPQ--------------------FDAINDLLTGREHLEFYAILR-----------------------------GVPEKE 2027
Cdd:TIGR03269 65 LCEKcgyverpskvgepcpvcggtLEPEEVDFWNLSDKLRRRIRKriaimlqrtfalygddtvldnvlealeeiGYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2028 VCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVL 2106
Cdd:TIGR03269 145 AVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVL 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 827475625 2107 TSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNKF 2142
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
897-1090 |
3.29e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 897 PAHIDPGVYI-----ENL------MKIYSNG---KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY 962
Cdd:PRK10636 291 PAHVDNPFHFsfrapESLpnpllkMEKVSAGygdRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 963 IqGKDIRtdlnairqnLGVCPQHNVLFsMLTVEEHIWFYARLkglsAEKvksEMEQIVMD-LG----LPHKRTSRSNQLS 1037
Cdd:PRK10636 371 L-AKGIK---------LGYFAQHQLEF-LRADESPLQHLARL----APQ---ELEQKLRDyLGgfgfQGDKVTEETRRFS 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 1038 GGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYrQGRTIILS 1090
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-EGALVVVS 484
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1943-2083 |
3.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEI-------------DEVHQNMG----YCPQFDAIN 2005
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLqqdpprnvegtvyDFVAEGIEeqaeYLKRYHDIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2006 DLLT---GREHLEFYAILRGVPE-----------KEVCKvadwgirKLGLMKyvDKAAGSYSGGNMRKLSTAMALIGGPP 2071
Cdd:PRK11147 106 HLVEtdpSEKNLNELAKLQEQLDhhnlwqlenriNEVLA-------QLGLDP--DAALSSLSGGWLRKAALGRALVSNPD 176
|
170
....*....|..
gi 827475625 2072 VVFLDEPTTGMD 2083
Cdd:PRK11147 177 VLLLDEPTNHLD 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
927-1104 |
3.94e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.40 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 927 FYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtayiqgkDIRTDLNAIRQNlgvcPQHNVLFSMLTVEEhiWFYARLKG 1006
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTVSYK----PQYIKADYEGTVRD--LLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1007 L-SAEKVKSEmeqIVMDLGLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYAR----RGIWDLLLKY 1081
Cdd:cd03237 89 FyTHPYFKTE---IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENN 165
|
170 180
....*....|....*....|...
gi 827475625 1082 RqgRTIILSTHHMDEADILGDRI 1104
Cdd:cd03237 166 E--KTAFVVEHDIIMIDYLADRL 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1943-2138 |
4.08e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGN----------------------SVLTeideVHQN--MGYC 1998
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvsmlfqennlfSHLT----VAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1999 PQFDaindlLTGREHLEFYAILRgvpekevckvadwgirKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEP 2078
Cdd:PRK10771 98 PGLK-----LNAAQREKLHAIAR----------------QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2079 TTGMDPkarrALWNCILSIIKE---GRSVVL--TSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2138
Cdd:PRK10771 157 FSALDP----ALRQEMLTLVSQvcqERQLTLlmVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1780-2112 |
4.34e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.77 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1780 VNILIGINGSVSTFVLELFgsneigginDILKNVFLIFPHFCLGRGLIDMVKNQAMadaleRFGENRFRSPLAWDMVGKN 1859
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEAL---------RFLADFDALVIGLTDERSRNGGIGGIPS-----LLNGIDPKEPIEFEISEFL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1860 lfamaIEGVIFFSITVLIQYRFCIKARSLSTKLKPIGEEDEDVARERQRILGGGGQTDILELRQLTKVYKRKQKPAVDRL 1939
Cdd:pfam13304 67 -----EDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1940 CVGIPPGECFGLLGVNgagktSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEvhqnmgYCPQFDAINDLLTGREHLEFYAI 2019
Cdd:pfam13304 142 LLLLSIISPLSFLLLL-----DEGLLLEDWAVLDLAADLALFPDLKELLQR------LVRGLKLADLNLSDLGEGIEKSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2020 LRGVPEKEVCKVadWGIRKLGlmKYVDkaAGSYSGGNMRKLSTAMALI---GGPPVVFLDEPTTGMDPKARRALWNCILS 2096
Cdd:pfam13304 211 LVDDRLRERGLI--LLENGGG--GELP--AFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKE 284
|
330
....*....|....*.
gi 827475625 2097 IIKEGRSVVLTSHSME 2112
Cdd:pfam13304 285 LSRNGAQLILTTHSPL 300
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1939-2083 |
4.35e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1939 LCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnSVLTEIDE--VHQNMGYCPQFDAINDLLTGRehlEF 2016
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPLESWSSkaFARKVAYLPQQLPAAEGMTVR---EL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 827475625 2017 YAILR----------GVPEKEvcKVADwGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMD 2083
Cdd:PRK10575 106 VAIGRypwhgalgrfGAADRE--KVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1858-2143 |
4.63e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1858 KNLFAMAIEGVIFFSITVLIQYRFCIKARSLSTKLKPI---GEEDEDVARERQRILGGGGQTdiLELRQLTKVYKRKQKP 1934
Cdd:TIGR00957 575 KAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIflsHEELEPDSIERRTIKPGEGNS--ITVHNATFTWARDLPP 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1935 AVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGnsvlteidevhqNMGYCPQFDAI-NDLLtgREH 2013
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWIqNDSL--REN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2014 LEFYAILRGVPEKEVCK----VADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRA 2089
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEacalLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 827475625 2090 LWNCILSI--IKEGRSVVLTSHSMEECEALcTRMAIMVNGRFRCLGSVQHLKNKFG 2143
Cdd:TIGR00957 799 IFEHVIGPegVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
906-1110 |
5.06e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 906 IENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIrTDLNAIRQNLGVCPQH 985
Cdd:PRK11650 6 LQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 986 NVLFSMLTVEEHIWFYARLKGLSaekvKSEMEQIVMD----LGLPHKRTSRSNQLSGGmQRKlSVAL--AFVGGSKVVIL 1059
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKIRGMP----KAEIEERVAEaariLELEPLLDRKPRELSGG-QRQ-RVAMgrAIVREPAVFLF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1060 DEPTAGVDpyAR-RGIWDLLLKYRQGR---TIILSTHHMDEADILGDRIAIISHG 1110
Cdd:PRK11650 159 DEPLSNLD--AKlRVQMRLEIQRLHRRlktTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
974-1104 |
5.07e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 974 AIRQNLGvcpQHNVLFSMLTVEEhIWFYARLkgLSA-EKVKSEMEQIVmDLGLPHKRTSRS-NQLSGG-MQRklsVALAF 1050
Cdd:cd03270 81 AIDQKTT---SRNPRSTVGTVTE-IYDYLRL--LFArVGIRERLGFLV-DVGLGYLTLSRSaPTLSGGeAQR---IRLAT 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1051 VGGSKVV----ILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTHhmDEADIL-GDRI 1104
Cdd:cd03270 151 QIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEH--DEDTIRaADHV 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
899-1090 |
5.58e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 899 HIDPG-------VYIENLMKIYsNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGT---------AY 962
Cdd:TIGR03719 311 YIPPGprlgdkvIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetvklAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 963 I-QGKDirtDLNairqnlgvcPQHNVlfsmltveehiWfyarlkglsaekvksemEQI-----VMDLGlphKRT------ 1030
Cdd:TIGR03719 390 VdQSRD---ALD---------PNKTV-----------W-----------------EEIsggldIIKLG---KREipsray 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 1031 -SRSN-----------QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYrQGRTIILS 1090
Cdd:TIGR03719 427 vGRFNfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS 497
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
918-1111 |
5.58e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 918 VAVDGLTLGFYEGQITSFLGHNGAGKTTT-MSILtGLFpPTSGTAYIQGKDI----RTDLNAIRQNLgvcpQhnVLF--- 989
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLI-PSEGEIRFDGQDLdglsRRALRPLRRRM----Q--VVFqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 990 --SM---LTVEEHIwfyarLKGLSAEKV---KSEMEQIVMDL----GL--------PHkrtsrsnQLSGGmQR-KLSVAL 1048
Cdd:COG4172 372 fgSLsprMTVGQII-----AEGLRVHGPglsAAERRARVAEAleevGLdpaarhryPH-------EFSGG-QRqRIAIAR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1049 AFVGGSKVVILDEPTAGVDPYARRGIWDLL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1111
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLrdLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
917-1125 |
5.73e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 917 KVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQgkdirtdlnairQNLGVCPQHNVLFSMlTVEE 996
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RSIAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 997 HIWFY-----ARLkglsAEKVK-SEMEQIVMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:PTZ00243 740 NILFFdeedaARL----ADAVRvSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1069 Y-ARRGIWDLLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSL-FLKTQL 1125
Cdd:PTZ00243 816 HvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSAdFMRTSL 873
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1019-1110 |
6.34e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1019 IVMDLGLPHKRTSRS-NQLSGGMQRKlsVALAFVGGSKVV----ILDEPTAGVDPYARRGIWDLLLKYR-QGRTIILSTH 1092
Cdd:PRK00635 459 ILIDLGLPYLTPERAlATLSGGEQER--TALAKHLGAELIgityILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEH 536
|
90
....*....|....*....
gi 827475625 1093 hmDEADI-LGDRIAIISHG 1110
Cdd:PRK00635 537 --DEQMIsLADRIIDIGPG 553
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1943-2083 |
7.40e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTsTF-KMLTGDSVVTSGEaylagnsVLTEIDevhqnMGYCPQFdaindlLTGREHLEFYAILR 2021
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGE-------VDPELK-----ISYKPQY------IKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2022 GVPEK--------EVckvadwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMD 2083
Cdd:PRK13409 423 SITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
932-1117 |
8.85e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 932 ITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGK---DIRTDLN--AIRQNLGVCPQHNVLFSMLTVEehiwfyARLKG 1006
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGIClpPEKRRIGYVFQDARLFPHYKVR------GNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1007 LSAEKVKSEMEQIVMDLGLPH--KRTSRSnqLSGG-MQRklsVAL--AFVGGSKVVILDEPTAGVD-PYARRgiwdlLLK 1080
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPllDRYPGS--LSGGeKQR---VAIgrALLTAPELLLMDEPLASLDlPRKRE-----LLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 1081 Y-----RQGRTIIL-STHHMDEADILGDRIAIISHGKLCCVGS 1117
Cdd:PRK11144 170 YlerlaREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
937-1112 |
1.07e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 937 GHNGAGKTTTMSILTGLFPPTSGtaYIQgkdIRTDLNAIRqnLGVCPQHNV---LFSMLT-----VEEHIWFYARLKGLS 1008
Cdd:PRK11147 36 GRNGAGKSTLMKILNGEVLLDDG--RII---YEQDLIVAR--LQQDPPRNVegtVYDFVAegieeQAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1009 A----EKVKSEMEQI--VMD-----------------LGL-PHKRTSrsnQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1064
Cdd:PRK11147 109 EtdpsEKNLNELAKLqeQLDhhnlwqlenrinevlaqLGLdPDAALS---SLSGGWLRKAALGRALVSNPDVLLLDEPTN 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 827475625 1065 GVDPYARRGIWDLLLKYrQGrTIILSTHhmDEADI--LGDRIAIISHGKL 1112
Cdd:PRK11147 186 HLDIETIEWLEGFLKTF-QG-SIIFISH--DRSFIrnMATRIVDLDRGKL 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2039-2110 |
1.17e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2039 LGLMKyVDKAAGSYSGGNMRKLSTAMALIGGP-PVVF-LDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHS 2110
Cdd:cd03238 76 LGYLT-LGQKLSTLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
929-1107 |
1.27e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGT-----------AYIQGKDIRTDLNAIRQN-LGVC--PQHNVLFSML-- 992
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevlKRFRGTELQDYFKKLANGeIKVAhkPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 -TVEEHIwfyarlkglsaEKV--KSEMEQIVMDLGLPHKRTSRSNQLSGG-MQRkLSVALAFVGGSKVVILDEPTAGVDP 1068
Cdd:COG1245 178 gTVRELL-----------EKVdeRGKLDELAEKLGLENILDRDISELSGGeLQR-VAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 827475625 1069 YAR----RGIWDLLlkyRQGRTIILSTHHMDEADILGDRIAII 1107
Cdd:COG1245 246 YQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1919-2087 |
1.34e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQkPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTE------IDEVH 1992
Cdd:PRK11650 4 LKLQAVRKSYDGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepadrdIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQfdaindlLTGREHLEfYAI-LRGVP----EKEVCKVAdwgiRKLGLMKYVDKAAGSYSGGNMRKLstAM--A 2065
Cdd:PRK11650 83 QNYALYPH-------MSVRENMA-YGLkIRGMPkaeiEERVAEAA----RILELEPLLDRKPRELSGGQRQRV--AMgrA 148
|
170 180
....*....|....*....|..
gi 827475625 2066 LIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLR 170
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2045-2113 |
1.36e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 1.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2045 VDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSI-IKEGRSVVLTSHSMEE 2113
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1941-2109 |
1.39e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1941 VGIPPGECFGLLGVNGAGKTSTFkmltgdsvvtsgeaylagnsvlteidevhqnmgycpqfDAINDLLTGRehleFYAIL 2020
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTIL--------------------------------------DAIGLALGGA----QSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2021 RGVPEKEVCKVADwgiRKLGLMKYVDKAagsySGGNMRKLSTAMAL----IGGPPVVFLDEPTTGMDPKARRALWNCILS 2096
Cdd:cd03227 54 RRSGVKAGCIVAA---VSAELIFTRLQL----SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|...
gi 827475625 2097 IIKEGRSVVLTSH 2109
Cdd:cd03227 127 HLVKGAQVIVITH 139
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1915-2140 |
1.84e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.53 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTkvYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSV----LTEIDE 1990
Cdd:PRK11831 4 VANLVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCPQFDAINDLLTGREHLEFyailrgvPEKEVCKVADWGIRKLGLMKYvdKAAG----------SYSGGNMRKL 2060
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKL--EAVGlrgaaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDPKARRALwnciLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2135
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVL----VKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
....*
gi 827475625 2136 QHLKN 2140
Cdd:PRK11831 229 QALQA 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
916-1112 |
2.23e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 916 GKVAVDGLTLGFYEGQITSFLGHNGAGKT-TTMSILT---GLFppTSGTAYIQGK--DIRTDLNAI----------RQNL 979
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyGRN--ISGTVFKDGKevDVSTVSDAIdaglayvtedRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 980 GvcpqhnvlfsmLTVEEHIWF---YARLKGLSAEKVKSEMEQIVMDLGLPHK---RTSRSNQ----LSGGMQRKlsVALA 1049
Cdd:NF040905 350 G-----------LNLIDDIKRnitLANLGKVSRRGVIDENEEIKVAEEYRKKmniKTPSVFQkvgnLSGGNQQK--VVLS 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 827475625 1050 ---FVGgSKVVILDEPTAGVDPYARRGIWDLLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1112
Cdd:NF040905 417 kwlFTD-PDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPE--LLGmcDRIYVMNEGRI 482
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1915-2113 |
2.31e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.09 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1915 QTDILELRQLTkvYKRKQKPAVDRLCVGIPPGEcFGLL-GVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLTEIDEVH- 1992
Cdd:PRK10247 4 NSPLLQLQNVG--YLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQFDAI-NDllTGREHLEF-YAILRGVPEKEvcKVADwGIRKLGLMKYV-DKAAGSYSGGNMRKLSTAMALIGG 2069
Cdd:PRK10247 81 QQVSYCAQTPTLfGD--TVYDNLIFpWQIRNQQPDPA--IFLD-DLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 827475625 2070 PPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVL-TSHSMEE 2113
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHDKDE 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
901-1082 |
2.65e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.28 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 901 DPGVYIENLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdirtdlnairQNLG 980
Cdd:TIGR00954 449 DNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK----------GKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 981 VCPQHNvLFSMLTVEEHIWFYARL-----KGLSaekvKSEMEQIVMDLGLPHKRTSR---------SNQLSGGMQRKLSV 1046
Cdd:TIGR00954 519 YVPQRP-YMTLGTLRDQIIYPDSSedmkrRGLS----DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAM 593
|
170 180 190
....*....|....*....|....*....|....*.
gi 827475625 1047 ALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR 1082
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFG 629
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
919-1092 |
2.80e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 919 AVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGL--FPP--TSGTAYIQGKDIRTDLNAIRQNLgVCPQHNVLFSMLTV 994
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGrvMAEKLEFNGQDLQRISEKERRNL-VGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 EEHIWFYARLKGLSAEKV-----KSEMEQIVMDL----GLPHKrTSR----SNQLSGGMQRKLSVALAFVGGSKVVILDE 1061
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVhqggnKKTRRQRAIDLlnqvGIPDP-ASRldvyPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190
....*....|....*....|....*....|...
gi 827475625 1062 PTAGVDPYARRGIWDLLLKYRQGR--TIILSTH 1092
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKEnmALVLITH 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
923-1067 |
4.50e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.71 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 923 LTLGFYEGQITSFLGHNGAGKTttmSILTGLF---PPTSGTAYIQGKDI-RTDLNAIRQNLGVCPQHNVLFS-MLTV--- 994
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSgSLRMnld 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 995 ------EEHIWFYARLkglsaekvkSEMEQIVMDL--GLPHKRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1066
Cdd:TIGR00957 1382 pfsqysDEEVWWALEL---------AHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
.
gi 827475625 1067 D 1067
Cdd:TIGR00957 1453 D 1453
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1907-2141 |
5.35e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1907 QRILGGGGQTDIlelRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTgDSVVTSGEAYLAG---NS 1983
Cdd:TIGR01271 1209 QKCWPSGGQMDV---QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswNS 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1984 VltEIDEVHQNMGYCPQFDAIndlLTG--REHLEFYAilrGVPEKEVCKVAD-WGIRKLgLMKYVDK-----AAGSY--S 2053
Cdd:TIGR01271 1285 V--TLQTWRKAFGVIPQKVFI---FSGtfRKNLDPYE---QWSDEEIWKVAEeVGLKSV-IEQFPDKldfvlVDGGYvlS 1355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2054 GGNMRKLSTAMALIGGPPVVFLDEPTTGMDP--------KARRALWNCilsiikegrSVVLTSHSME---ECEALctrma 2122
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPvtlqiirkTLKQSFSNC---------TVILSEHRVEallECQQF----- 1421
|
250 260
....*....|....*....|
gi 827475625 2123 IMVNG-RFRCLGSVQHLKNK 2141
Cdd:TIGR01271 1422 LVIEGsSVKQYDSIQKLLNE 1441
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
2051-2111 |
8.24e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 8.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 827475625 2051 SYSGGNMRKLSTAMALIGG---PPVVFLDEPTTGMDPKARRALWNCILSIIKEGRSVVLTSHSM 2111
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1919-2141 |
8.60e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTgDSVVTSGEAYLAG---NSVltEIDEVHQNM 1995
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswNSV--PLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1996 GYCPQFDAIndlLTG--REHLEFYAILRgvpEKEVCKVADwgirKLGLMKYVDKAAGS-----------YSGGNMRKLST 2062
Cdd:cd03289 80 GVIPQKVFI---FSGtfRKNLDPYGKWS---DEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2063 AMALIGGPPVVFLDEPTTGMDP--------KARRALWNCilsiikegrSVVLTSHSMeecEAL--CTRMAIMVNGRFRCL 2132
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPityqvirkTLKQAFADC---------TVILSEHRI---EAMleCQRFLVIEENKVRQY 217
|
....*....
gi 827475625 2133 GSVQHLKNK 2141
Cdd:cd03289 218 DSIQKLLNE 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1930-2109 |
1.13e-03 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 42.91 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1930 RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVLT-EIDEVHQNMGYCPQ----FDAi 2004
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQepvlFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2005 ndllTGREHLEFYAILRGVPE-KEVCKVA--DWGIRKL--GLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPT 2079
Cdd:cd03249 92 ----TIAENIRYGKPDATDEEvEEAAKKAniHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190
....*....|....*....|....*....|
gi 827475625 2080 TGMDPKARRALWNCiLSIIKEGRSVVLTSH 2109
Cdd:cd03249 168 SALDAESEKLVQEA-LDRAMKGRTTIVIAH 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1918-2162 |
1.34e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.90 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYKR--KQKPAVDRLCVGIPPGECFGLLGVNGAGKT----STFKMLTGDSVVTSGEAYLAGNSVLT----- 1986
Cdd:COG4172 6 LLSVEDLSVAFGQggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1987 -------EIDEVHQN-MgycpqfDAINDLLT-GREHLEFYAILRGVPEKEV-CKVADW----GIRklglmkyvDKA--AG 2050
Cdd:COG4172 86 lrrirgnRIAMIFQEpM------TSLNPLHTiGKQIAEVLRLHRGLSGAAArARALELlervGIP--------DPErrLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2051 SY----SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRAlwncILSIIKE-----GRSVVLTSHSMeeceALCTRM 2121
Cdd:COG4172 152 AYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQ----ILDLLKDlqrelGMALLLITHDL----GVVRRF 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 827475625 2122 A----IMVNGRFRCLGSVQHLKNKFGDGYTIILrvAGADPRLEPV 2162
Cdd:COG4172 224 AdrvaVMRQGEIVEQGPTAELFAAPQHPYTRKL--LAAEPRGDPR 266
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
884-1093 |
1.59e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 43.64 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 884 RKENAEAVCIEEEPahiDPGVYIENLmKIYS-NGKVAVDGLTLGFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTSG 959
Cdd:COG4178 346 DALPEAASRIETSE---DGALALEDL-TLRTpDGRPLLEDLSLSLKPGErllIT---GPSGSGKSTLLRAIAGLWPYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 960 TAyiqgkdirtdlnairqnlgVCPQH-NVLF----SMLTVeehiwfyARLKGL-----SAEKVK-SEMEQIVMDLGLPH- 1027
Cdd:COG4178 419 RI-------------------ARPAGaRVLFlpqrPYLPL-------GTLREAllypaTAEAFSdAELREALEAVGLGHl 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 827475625 1028 -----KRTSRSNQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYRQGRTIILSTHH 1093
Cdd:COG4178 473 aerldEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1919-2084 |
2.05e-03 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 42.10 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1919 LELRQLTKVYKRKQKPAVDRLCVGIPPGECFGLLGVNGAGKTST----FKMLTgdsvVTSGEAYLAGNSvLTEID--EVH 1992
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVD-ISKIGlhDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1993 QNMGYCPQfDAIndLLTG--REHL---------EFYAILRGVPEKEVCKvadwgiRKLGLMKYVDKAAGS-YSGGNMRKL 2060
Cdd:cd03244 78 SRISIIPQ-DPV--LFSGtiRSNLdpfgeysdeELWQALERVGLKEFVE------SLPGGLDTVVEEGGEnLSVGQRQLL 148
|
170 180
....*....|....*....|....
gi 827475625 2061 STAMALIGGPPVVFLDEPTTGMDP 2084
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDP 172
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
929-1096 |
2.15e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 929 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdirTDLNAIRQNLGvcpqhnvlfSMLTVEEHIWFYARLKGLS 1008
Cdd:PRK13545 49 EGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---AALIAISSGLN---------GQLTGIENIELKGLMMGLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1009 AEKVKSEMEQIV--MDLGLPHKRTSRSnqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYARRGIWDLLLKYR-QGR 1085
Cdd:PRK13545 117 KEKIKEIIPEIIefADIGKFIYQPVKT--YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGK 194
|
170
....*....|.
gi 827475625 1086 TIILSTHHMDE 1096
Cdd:PRK13545 195 TIFFISHSLSQ 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1946-2087 |
2.31e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 42.01 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1946 GECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSVlteidevhqnmGYCPQFDAINDLLTGREHLefYAILRGVPE 2025
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLL--SSITKDFYT 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 827475625 2026 KEVCKVADwgIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:cd03237 92 HPYFKTEI--AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
908-1092 |
2.92e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.61 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 908 NLMKIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQgKDIrtdlnairqNLGVCPQHNV 987
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGI---------KVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 988 LFSMLTVEEHIW--------FYARLKGLSA---------EKVKSEME------------------QIVMD-LGLPHKRTS 1031
Cdd:TIGR03719 79 LDPTKTVRENVEegvaeikdALDRFNEISAkyaepdadfDKLAAEQAelqeiidaadawdldsqlEIAMDaLRCPPWDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 1032 RSNqLSGGMQRKlsVALAFVGGSK--VVILDEPTAGVDpyARRGIW--DLLLKYrQGrTIILSTH 1092
Cdd:TIGR03719 159 VTK-LSGGERRR--VALCRLLLSKpdMLLLDEPTNHLD--AESVAWleRHLQEY-PG-TVVAVTH 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
913-1112 |
3.17e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 913 YSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQGKdIRtdlnairqnLGVCPQHNVLFSML 992
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VR---------MAVFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 993 TVEEHIWFYARLKGLSAEKVKSEMEQ--IVMDLGLPHKRTsrsnqLSGGmqRKLSVALAFVGGSK--VVILDEPTAGVDP 1068
Cdd:PLN03073 588 SSNPLLYMMRCFPGVPEQKLRAHLGSfgVTGNLALQPMYT-----LSGG--QKSRVAFAKITFKKphILLLDEPSNHLDL 660
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 827475625 1069 YARRGIWDLLLKYRQGrtIILSTHhmDEADILG--DRIAIISHGKL 1112
Cdd:PLN03073 661 DAVEALIQGLVLFQGG--VLMVSH--DEHLISGsvDELWVVSEGKV 702
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1939-2110 |
3.81e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1939 LCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNsvltEIDEVHQN-MGYCPQFDAINDLLTGREHLEFY 2017
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC----NINNIAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2018 AILRGVPEkevckVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSI 2097
Cdd:PRK13541 95 SEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 827475625 2098 IKEGRSVVLTSHS 2110
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
911-964 |
3.96e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 3.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 827475625 911 KIYSNGKVAVDGLTLGFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIQ 964
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA 67
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1943-2087 |
4.10e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.94 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1943 IPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLaGNSVLTEIDEVHQNMGYCPQFDAINDLLTGREHLEFYAILRG 2022
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 827475625 2023 VPEKEVCKVADWGIRKLGLMKYVDKAAGSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2087
Cdd:PRK11000 105 AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1918-2109 |
4.42e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1918 ILELRQLTKVYK-------RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKMLTGDSVVTSGEAYLAGNSvLTEIDE 1990
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1991 VHQNMGYCPQFDAINDLLTGREH----LEFYAILR---GVPEKEvcKVADWGIRKLGLMKyvDKAagSY-----SGGNMR 2058
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTSLNPRQRisqiLDFPLRLNtdlEPEQRE--KQIIETLRQVGLLP--DHA--SYyphmlAPGQKQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 827475625 2059 KLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSII-KEGRS-VVLTSH 2109
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISyIYVTQH 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2050-2147 |
4.80e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2050 GSYSGGNMRKLSTAMALIGGPPVVFLDEPTTGMDpkarRALWNCILSIIKE-----GRSVVLTSHSMEECEALCTRMAIM 2124
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQVIVL 499
|
90 100
....*....|....*....|...
gi 827475625 2125 VNGRFRCLGSVQHLKNKFGDGYT 2147
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1917-2159 |
4.89e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1917 DILELRQLTKVYK--RKQKPAVDRLCVGIPPGECFGLLGVNGAGKTSTFKML-----TGDSVVTSGEAYLAG-NSVLTEI 1988
Cdd:PRK10261 11 DVLAVENLNIAFMqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALmrlleQAGGLVQCDKMLLRRrSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1989 DEVHQN-----------MGYCPQFDAINDLLT-GREHLEFYAILRGVPEKEVCKVADwgiRKLGLMKYVDKAA--GSY-- 2052
Cdd:PRK10261 91 SEQSAAqmrhvrgadmaMIFQEPMTSLNPVFTvGEQIAESIRLHQGASREEAMVEAK---RMLDQVRIPEAQTilSRYph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2053 --SGGNMRKLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2129
Cdd:PRK10261 168 qlSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270
....*....|....*....|....*....|
gi 827475625 2130 RCLGSVQHLKNKFGDGYTIILrvAGADPRL 2159
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRAL--LAAVPQL 275
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
936-1117 |
7.87e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 936 LGHNGAGKTTTMSILTGLFPPTSGTAYIQGKDIRT-DLNAIRQNLGVCPQHNVLFS---MLTVE-------EHIWFYARL 1004
Cdd:PTZ00243 1342 VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyGLRELRRQFSMIPQDPVLFDgtvRQNVDpfleassAEVWAALEL 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 1005 KGLSaEKVKSEMEQIvmdlglphkrtsRSNQLSGGM-----QRKL-SVALAFVG-GSKVVILDEPTAGVDPYARRGIWDL 1077
Cdd:PTZ00243 1422 VGLR-ERVASESEGI------------DSRVLEGGSnysvgQRQLmCMARALLKkGSGFILMDEATANIDPALDRQIQAT 1488
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 827475625 1078 LLKYRQGRTIILSTHHMDEADILgDRIAIISHGKLCCVGS 1117
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2059-2141 |
8.47e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 40.66 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 827475625 2059 KLSTAMALIGGPPVVFLDEPTTGMDPKARRALWNCILSIIK-EGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQH 2137
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 827475625 2138 LKNK 2141
Cdd:COG4170 246 ILKS 249
|
|
| |
