|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2212 |
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: 2374.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1 MAIGTQLYLLLWKNFTYRRRNKVQLVVELLWPLFLFLILIAVRQSHPPYKQSQCHFPNKALPSAGTLAWIQGIICNVNNP 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 81 CFHQPTAGETPGLVSNFDNSILSRLLVDMRTVLTISGNRT----TFSGLQDLSKTIQRLGERPD--AWPNLPVGEYLRAN 154
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQhlgqVWAELRTLSQFMDTLRTHPEriAGRGIRIRDILKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 155 ESFSSYLRTNTSIPSAFVEQLLRARLNLQVVTLAGEGVRLSDIVCNASLLSRYLTVEEGDSFPELQGALCVVPSDIMQKA 234
Cdd:TIGR01257 161 EALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGVPDLELKDIACSEALLERFIIFSQRRGAQTVRDALCSLSQGTLQWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 235 EQIFLSQLDFSKIvtrdrlqanaadFRIISRAVSSASQEL-----ASIMDDIS-SLSSFSELNSEIRLLTPeNRSVLPRE 308
Cdd:TIGR01257 241 EDTLYANVDFFKL------------FHVLPTLLDSRSQGInlrswGGILSDMSpRIQEFIHRPSVQDLLWV-TRPLLQNG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 309 SFRAFSRIM-------CGHPEAGGERIPSFNWYEDQDIKSFLGRNASEETSLEN-DNSTTSFCENLIQNLESNPLSRIVW 380
Cdd:TIGR01257 308 GPETFTQLMgilsdllCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSyDKRTTSFCNALIQSLESNPLTKIAW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 381 RGIKPLFIGKLLYTPDTPITRTIMSEVNKTFQDFEILKDVHEAWQEVGPRIKTFMESSVEIRLLQDLLRRPEVAVIVNMR 460
Cdd:TIGR01257 388 RAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 461 LENTSWTASRIARFLSTQDPDTPRKDGAQLTWFDLYQDLNNTFTTLSELTKCFSLNKLEGLTTEGEMVERALELLEDRQF 540
Cdd:TIGR01257 468 LGEEGITAEAVLNFLYNGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 541 WAGIVF--LLPNSSSsvLPPHVKYKIRMDIDDVTRTNKIKDKFWDPGPAAEPFSDMRYVWGGFVYVQDLVERAVTRLLTG 618
Cdd:TIGR01257 548 WAGVVFpdMYPWTSS--LPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQ 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 619 KEAKTGIYVQQMPYPCFVDDVFIRVLNRSLPLFMTLAWIYSVAMIIKGVVYEKEARLKETMRIMGLGSGMLWFSWFISSY 698
Cdd:TIGR01257 626 AEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSF 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 699 LPFLFSAALLIAALKWGDILPYSDPAVVFFFLAAFATATIMLCFLISTFFSRANLAAACGGLIYFTLYLPYVLCVAWREY 778
Cdd:TIGR01257 706 SIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDR 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 779 LTSTHRILASFLSPVAFGFGCEYFSQYEEQGVGIQWFNLKSSPMEGDTYSFNTSIMMLYADALIYALATWYIEAVFPGQY 858
Cdd:TIGR01257 786 MTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDY 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 859 GIPRPWYFIFQLNYWGG---------------VPLELGLPIPPAPREEQDARIEAEPTNLILGVSIRNLVKIYKKGAKLA 923
Cdd:TIGR01257 866 GTPLPWYFLLQESYWLGgegcstreeralektEPLTEEMEDPEHPEGINDSFFERELPGLVPGVCVKNLVKIFEPSGRPA 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEEHVW 1003
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1004 FYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLL 1083
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1084 KYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKARLGTGYYLTLVKREMHRTPSNTSSGKIPSAASPKDS 1163
Cdd:TIGR01257 1106 KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGGCEGTCSCTSKGFS 1185
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1164 DSSVSDDTGLGSEE--NGfDVAALMALAQQYVPDAQLVEDIGREAVINLPNAASEDGTLALFLNELDKRQGEFGVVSYGL 1241
Cdd:TIGR01257 1186 TRCPARVDEITPEQvlDG-DVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGI 1264
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1242 SDTTLEEIFLRVAEETGV-------------DADPEDP---PVSQEPQGAPSEDRDAEAQETDPLSG----DGQSDSAPL 1301
Cdd:TIGR01257 1265 SDTPLEEIFLKVTEDADSgslfaggaqqkreNANLRHPcsgPTEKAGQTPQASHTCSPGQPAAHPEGqpppEPEDPGVPL 1344
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1302 -TGCFHTCQQLRALFTKRLKYAFRSRRGIFAQIVLPAVFVLIALLFSLIVPPFGKYPSLELQPWMYGEQFTFFSNDAPQD 1380
Cdd:TIGR01257 1345 nTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPNS 1424
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1381 PAMQNLLKALLDPPGFGTKCMQPNGDTECLAKAETKFVRPQIPYSMWQLFHNGNFSIEKPSPECECSTEKIRRMLPECPE 1460
Cdd:TIGR01257 1425 EHLEVLADVLLNKPGFGNRCLKEEWLPEYPCGNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPECPE 1504
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1461 GAGGVPPPQMQQITGDILQNLTGRNISDYLIKTYPQILKKSLKTKKWVNEFRYGGFSLGAKSSLTMSEPHHLEESVLAIR 1540
Cdd:TIGR01257 1505 GAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPITGEALVGFLSDLG 1584
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1541 RRYNIAENGSLDQLLQRLPDVLSGLTSQNNVKVWFNNKGWHAMASFVNIMNNGLLRANLPPKTERRKYGITAYNHPLNLT 1620
Cdd:TIGR01257 1585 QMMNVSGGPVTREASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLT 1664
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1621 KEQLTEMALMTTSVDVLVSICVIFAMSFVPASFVLFLIEERVSKSKHLQFVSGVKPILYWTTNYVWDMVNYTVPATMVVF 1700
Cdd:TIGR01257 1665 KEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVG 1744
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1701 IFISFQQESYVSEKNLPALVLLLLLYGWSITPLMYPASFIFSVPSTAYVVLTSINLFIGINGSVATFVLELFVDEH-LNE 1779
Cdd:TIGR01257 1745 IFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRtLLR 1824
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1780 VNRILKKVFLIFPHFCLGRGLIDMAKNQAMADAFQRLGTKQNLDPLSWDFVGKNLFAMAMEGIVFFLFTVLLQYKFFvnF 1859
Cdd:TIGR01257 1825 FNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFF--L 1902
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1860 SRWSGF-VLPPLGMEDEDVARERERVKNGRALGDILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTF 1938
Cdd:TIGR01257 1903 SRWIAEpAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTF 1982
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1939 RMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQ 2018
Cdd:TIGR01257 1983 KMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSL 2062
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2019 YADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAI 2098
Cdd:TIGR01257 2063 YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAI 2142
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2099 MVNGRFQCLGSVQHLKNRFGDGYTIILRLSTPSAEPC----PVDAYIQNAFPGIQLKERHQNVLQYQLPSQtcSLARVFE 2174
Cdd:TIGR01257 2143 MVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLpdlnPVEQFFQGNFPGSVQRERHYNMLQFQVSSS--SLARIFQ 2220
|
2250 2260 2270
....*....|....*....|....*....|....*...
gi 1207110406 2175 VLSNNYEELGIADYSVSQTTLDQVFVNFAKDQTDDDQL 2212
Cdd:TIGR01257 2221 LLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
907-1126 |
2.14e-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: 2.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLK 1126
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1894-2114 |
4.42e-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: 357.97 E-value: 4.42e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2054 TTGMDPKAKRFLWNCILSvVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLK 2114
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
907-1141 |
3.12e-88 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 287.73 E-value: 3.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKARLGTGYYLTLVKRE 1141
Cdd:COG1131 159 TSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEE 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1894-2117 |
1.64e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 253.83 E-value: 1.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRF 2117
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
914-1130 |
7.65e-66 |
|
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: 226.12 E-value: 7.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 914 KIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLF 993
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 994 DILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY 1073
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1074 SRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKARLG 1130
Cdd:TIGR01188 159 TRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
907-1116 |
1.18e-65 |
|
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: 220.35 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVwfygrmkgmsleevnkemnslledvglqhkrfeqtkNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03230 123 TSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
907-1126 |
1.11e-63 |
|
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: 216.47 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLK 1126
Cdd:cd03265 159 TIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
909-1116 |
2.35e-62 |
|
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: 213.57 E-value: 2.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQ 988
Cdd:COG4555 4 VENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 HNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1069 GVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1901-2202 |
4.81e-60 |
|
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: 209.55 E-value: 4.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1901 KVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAII 1980
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1981 DLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPK 2060
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2061 AKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGDgytiilrlSTPSAEP-CPVDA 2139
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK--------DTLESRPrDIQSL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2140 YIQNAFPGIQLKERHQNVLQYQLPSQTCSL---------ARVFEVLS-NNYEelgIADYSVSQTTLDQVFVNF 2202
Cdd:TIGR01188 231 KVEVSMLIAELGETGLGLLAVTVDSDRIKIlvpdgdetvPEIVEAAIrNGIR---IRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1894-2104 |
8.41e-58 |
|
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: 197.62 E-value: 8.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEfyarlrgvpesyvekvaqwgvqklglsqyadreaggYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1894-2119 |
3.80e-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: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVP-ESYVEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFdEELKKRIEEL-IELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGD 2119
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1902-2114 |
2.09e-55 |
|
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: 192.97 E-value: 2.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1902 VYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIID 1981
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1982 LLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKA 2061
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2062 KRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLK 2114
Cdd:cd03265 167 RAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
907-1120 |
7.39e-54 |
|
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: 188.17 E-value: 7.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKgaKLAVNHLNIKFYEGqITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCG 1120
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
907-1122 |
1.03e-51 |
|
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: 182.53 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRRTLGV 985
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQH--NVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGmQRKLsVAIAfiG----GSK 1059
Cdd:COG1122 80 VFQNpdDQLFA-PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGG-QKQR-VAIA--GvlamEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1060 VVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
908-1115 |
1.43e-51 |
|
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: 181.51 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVC 986
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
907-1134 |
7.92e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 182.62 E-value: 7.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDmdiIRRTLGVC 986
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKARLGTGYY 1134
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
907-1116 |
3.77e-48 |
|
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: 171.63 E-value: 3.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRtLGVC 986
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSleevNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1894-2105 |
9.09e-47 |
|
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: 167.76 E-value: 9.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRkpAVNRLCLGIPRGeCFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2054 TTGMDPKAK-RFLwNcILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:cd03264 158 TAGLDPEERiRFR-N-LLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
907-1115 |
5.40e-46 |
|
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: 165.53 E-value: 5.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirSDMDI-IRRTLGV 985
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIaARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
907-1122 |
6.80e-46 |
|
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: 166.14 E-value: 6.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRT 982
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQHNVLFDILTVEEHVWFYGRMKG-MSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1893-2103 |
1.47e-43 |
|
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: 158.69 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKP--AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLM 1970
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
907-1116 |
2.63e-43 |
|
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: 157.91 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAK--LAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLG 984
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
907-1122 |
2.70e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 161.13 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYReGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13537 166 TTGLDPQARHLMWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
907-1122 |
3.09e-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: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRT 982
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQHNVLFDILTVEEHVWFYGRM-KGMSLEEVNKEMNSLLEDVGLQH--KRF--EqtknLSGGMQRKLSVAIAFIGG 1057
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGaaDKMpsE----LSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1058 SKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
907-1112 |
3.85e-43 |
|
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: 157.63 E-value: 3.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY--KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSdmdiIRRTLG 984
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHkrFEQ--TKNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSG--FENayPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLK--YREGRTIILSTHYMDEADLLGDRIAIIS 1112
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1896-2103 |
5.82e-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: 156.61 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQlMGycpq 1975
Cdd:cd03268 3 TNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 fdAIIDL------LTGREHLEFYARLRGVPESYVEKVaqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:cd03268 76 --ALIEApgfypnLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1894-2084 |
1.51e-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: 155.33 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESyVEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD-REAIDEA-LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
881-1122 |
4.11e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 158.84 E-value: 4.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 881 GLPIPPAPREEQ------DARIEAEPTnliLGVSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSIL 954
Cdd:PRK13536 13 RLELSPIERKHQgiseakASIPGSMST---VAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 955 TGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRF 1034
Cdd:PRK13536 88 LGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1035 EQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYReGRTIILSTHYMDEADLLGDRIAIIS 1112
Cdd:PRK13536 168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLrsLLAR-GKTILLTTHFMEEAERLCDRLCVLE 246
|
250
....*....|
gi 1207110406 1113 QGKLCCCGTP 1122
Cdd:PRK13536 247 AGRKIAEGRP 256
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
924-1068 |
1.46e-41 |
|
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: 150.49 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD-MDIIRRTLGVCPQHNVLFDILTVEEHV 1002
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 WFYGRMKGMSLEEVNKEMNSLLEDVGLQHKR----FEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1893-2103 |
1.89e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 155.73 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGY 1972
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
907-1122 |
1.99e-41 |
|
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: 153.61 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQ--TKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
907-1114 |
2.26e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.09 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY--KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSdmdiIRRTLG 984
Cdd:COG1116 8 LELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----PGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHkrFEQT--KNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAG--FEDAypHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
908-1122 |
3.63e-41 |
|
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: 152.59 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLGV 985
Cdd:cd03219 2 EVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHV------------WFYGRMKGMslEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIA 1053
Cdd:cd03219 80 TFQIPRLFPELTVLENVmvaaqartgsglLLARARREE--REARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
907-1116 |
1.02e-40 |
|
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: 150.72 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAK--LAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-----DMDII 979
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 RRTLGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSK 1059
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1060 VVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADlLGDRIAIISQGKL 1116
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
907-1108 |
2.03e-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: 149.17 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVnkEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYRE-GRTIILSTHymDEADLLGDRI 1108
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLArGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
907-1116 |
3.91e-40 |
|
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: 148.82 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03259 158 LSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
908-1122 |
7.84e-40 |
|
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: 149.42 E-value: 7.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIR----R 981
Cdd:COG0411 6 EVRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIARlgiaR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLgvcpQHNVLFDILTVEEHV---------------WFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQR 1046
Cdd:COG0411 84 TF----QNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1047 KLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1893-2206 |
3.64e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 148.72 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTemEKVHQLMGY 1972
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-LD--PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 cpqfdaiidL---------LTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIG 2043
Cdd:COG4152 76 ---------LpeerglypkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2044 AAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR--FQclGSVQHLKNRFGdgy 2121
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRkvLS--GSVDEIRRQFG--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2122 TIILRLSTPSaepcpvDAYIQNAFPGIQLKERHQNVLQYQLPSQTcSLARVFEVLSNNYEelgIADYSVSQTTLDQVFVN 2201
Cdd:COG4152 222 RNTLRLEADG------DAGWLRALPGVTVVEEDGDGAELKLEDGA-DAQELLRALLARGP---VREFEEVRPSLNEIFIE 291
|
....*
gi 1207110406 2202 FAKDQ 2206
Cdd:COG4152 292 VVGEK 296
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
908-1115 |
7.46e-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: 142.77 E-value: 7.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRRTLGVC 986
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQhnvlfdiltveehvwfygrmkgmsleevnkemnslledvglqhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1867-2103 |
1.66e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 148.44 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1867 LPPLGMEDEDVARERERVKNGRALGDILI-LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDT 1945
Cdd:PRK13536 14 LELSPIERKHQGISEAKASIPGSMSTVAIdLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1946 RITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAG 2025
Cdd:PRK13536 92 SPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2026 GYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1894-2103 |
1.86e-37 |
|
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: 140.88 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEmekVHQLMGYC 1973
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
907-1116 |
2.61e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKL--AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIR 980
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 R-TLGVCPQ-HNvLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGG-MQRklsVAIA--FI 1055
Cdd:COG1136 85 RrHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGqQQR---VAIAraLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADlLGDRIAIISQGKL 1116
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
907-1122 |
4.79e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 4.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHkrFEQTK--NLSGG-MQRklsVAIA--FIGGSKVV 1061
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEG--LADRYphQLSGGqQQR---VALAraLAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
877-1122 |
1.02e-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: 147.36 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 877 PLELGLPIPPAPREEQDARIEAEPTNLIlgvSIRNLVKIY---KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSI 953
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAEPLL---EVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 954 LTGLFPPTAGTIYVKGMDI----RSDMDIIRRTLGVCPQH--NVLFDILTVEEHVWF----YGRMKGmslEEVNKEMNSL 1023
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLtklsRRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEplrlHGLLSR---AERRERVAEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1024 LEDVGL--QHKR---FEqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTH 1096
Cdd:COG1123 388 LERVGLppDLADrypHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISH 463
|
250 260
....*....|....*....|....*.
gi 1207110406 1097 YMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
907-1116 |
3.18e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.88 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGaKLAVNHLNIKFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRR 981
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLGVCPQ-HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:COG2884 80 RIGVVFQdFRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1896-2103 |
5.95e-36 |
|
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: 136.44 E-value: 5.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL-TEMEKVHQLMGYCP 1974
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1975 QF-DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
917-1158 |
9.32e-36 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 141.14 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 917 KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMD------IIRRTLGVCPQHN 990
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENI-MKQSpvelreVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 991 VLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGV 1070
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1071 DPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP--------------LFLKARLGTGYY 1134
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQAtlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPdeilrnpaneyveeFIGKVDLSQVFD 240
|
250 260
....*....|....*....|....
gi 1207110406 1135 LTLVKREMHRTPSNTSSGKIPSAA 1158
Cdd:TIGR01186 241 AERIAQRMNTGPITKTADKGPRSA 264
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
907-1122 |
1.97e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDmdiiRRTLGVC 986
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHnVLFDI---LTVEE--------HVWFYGRMKGMSLEEVNKemnsLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFI 1055
Cdd:COG1121 81 PQR-AEVDWdfpITVRDvvlmgrygRRGLFRRPSRADREAVDE----ALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGkLCCCGTP 1122
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPP 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
907-1122 |
2.38e-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: 135.75 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRT-LGV 985
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRArLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 C--PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:cd03218 78 GylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLKYREgRTI-ILST-HYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKD-RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
908-1122 |
8.00e-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: 134.32 E-value: 8.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRT---LG 984
Cdd:TIGR04406 3 VAENLIKSYKK--RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-THLPMHERArlgIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVW-FYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
919-1117 |
1.37e-34 |
|
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: 132.66 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDmdiiRRTLGVCPQH-NVLFDI-L 996
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQRrSIDRDFpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEE--------HVWFYGRMKgmslEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:cd03235 86 SVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1069 GVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKLC 1117
Cdd:cd03235 162 GVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
915-1122 |
1.70e-34 |
|
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: 134.31 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 915 IYKK-GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRR-TLGVCPQ 988
Cdd:cd03294 30 ILKKtGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 HNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLqhKRFEQTK--NLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL--EGWEHKYpdELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03294 188 FSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
907-1115 |
6.19e-34 |
|
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: 129.43 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDiltveehvwfygrmkgMSLEEvnkemnslledvglqhkrfeqtkN-LSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:cd03228 81 VPQDPFLFS----------------GTIRE-----------------------NiLSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADlLGDRIAIISQGK 1115
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
907-1116 |
7.98e-34 |
|
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: 131.16 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYK--KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIR 980
Cdd:cd03258 2 IELKNVSKVFGdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
907-1122 |
8.90e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 132.86 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKG---AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI---RSDMDIIR 980
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVC---PQHNvLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK--NLSGGMQRKLSVAIAFI 1055
Cdd:PRK13637 83 KKVGLVfqyPEYQ-LFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
909-1115 |
1.03e-33 |
|
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: 128.84 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDII---RRTLGV 985
Cdd:cd03229 3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVWFygrmkgmsleevnkemnslledvglqhkrfeqtkNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1066 PTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
908-1122 |
1.20e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 130.92 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRT---LG 984
Cdd:COG1137 5 EAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMHKRArlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLKYREgRTI-ILST-HYMDEAdlLG--DRIAIISQGKLCCCGTP 1122
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
907-1122 |
4.58e-33 |
|
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: 129.78 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDI--IRRTLG 984
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRreLARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVL-FDiLTVEE--------HVWFYGRMKGMSLEEVNKemnsLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFI 1055
Cdd:COG1120 79 YVPQEPPApFG-LTVRElvalgrypHLGLFGRPSAEDREAVEE----ALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
907-1122 |
7.52e-33 |
|
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: 135.80 E-value: 7.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTA---GTIYVKGMDIR-SDMDIIRRT 982
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLeLSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
881-1131 |
7.63e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 139.49 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 881 GLPIPP-APREEQDARIEAeptnlilgvsiRNLVKiyKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFP 959
Cdd:NF033858 251 PVVIPPrPADDDDEPAIEA-----------RGLTM--RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 960 PTAGTIYVKGMDIR-SDMDiIRRTLGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK 1038
Cdd:NF033858 318 ASEGEAWLFGQPVDaGDIA-TRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1039 NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEAdLLGDRIAIISQGKL 1116
Cdd:NF033858 397 SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIFISTHFMNEA-ERCDRISLMHAGRV 475
|
250
....*....|....*
gi 1207110406 1117 CCCGTPLFLKARLGT 1131
Cdd:NF033858 476 LASDTPAALVAARGA 490
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
887-1142 |
1.05e-32 |
|
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: 138.04 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 887 APREEQDARIEAEPTNLILGVSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY 966
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 967 VKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVEEHVWFyGRmKGMSLEEVNK--EMNSLLEDV-----GLQHKRFEQTK 1038
Cdd:COG2274 534 IDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITL-GD-PDATDEEIIEaaRLAGLHDFIealpmGYDTVVGEGGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1039 NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLgDRIAIISQGKLCC 1118
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVE 689
|
250 260
....*....|....*....|....
gi 1207110406 1119 CGTPLFLKARlgTGYYLTLVKREM 1142
Cdd:COG2274 690 DGTHEELLAR--KGLYAELVQQQL 711
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
907-1116 |
1.08e-32 |
|
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: 128.01 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY--KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIR 980
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVCPQH--NVLFDILTVEEHV----WFYGRMKGMSLEEVNKEMnsLLEDVGLQHKRFEQTKN-LSGGMQRKLSVAIA 1053
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIaeplRIHGKLSKKEARKEAVLL--LLVGVGLPEEVLNRYPHeLSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
910-1122 |
1.34e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.44 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKKG----AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI--IRRTL 983
Cdd:PRK13633 8 KNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVC---PQHNVLFDIltVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGmqRKLSVAIAFIGG--S 1058
Cdd:PRK13633 88 GMVfqnPDNQIVATI--VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGG--QKQRVAIAGILAmrP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEAdLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
910-1122 |
1.48e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.04 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKKGAkLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD---MDIIRRTLGVC 986
Cdd:PRK13639 5 RDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQH--NVLFdILTVEEHVWFyGRMK-GMSLEEVNKEMNSLLEDVGLQHkrFEQT--KNLSGGmQRKlSVAIAFIGGSK-- 1059
Cdd:PRK13639 84 FQNpdDQLF-APTVEEDVAF-GPLNlGLSKEEVEKRVKEALKAVGMEG--FENKppHHLSGG-QKK-RVAIAGILAMKpe 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1060 VVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
907-1122 |
2.31e-32 |
|
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: 126.97 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1067 TAGVDPYSRRgiwDLLLKYRE-----GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03300 158 LGALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
885-1140 |
2.36e-32 |
|
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: 135.28 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 885 PPAPREEQDARIEAEPTNLilgvSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGT 964
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSL----ELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 965 IYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVEEHVwfygRM-KGMSLEEvnkEMNSLLEDVGLqHKRFEQTK---- 1038
Cdd:COG4987 392 ITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLRENL----RLaRPDATDE---ELWAALERVGL-GDWLAALPdgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1039 --------NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADlLGDRIAI 1110
Cdd:COG4987 463 twlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILV 541
|
250 260 270
....*....|....*....|....*....|
gi 1207110406 1111 ISQGKLCCCGTPLFLKARlgTGYYLTLVKR 1140
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQ--NGRYRQLYQR 569
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1896-2103 |
3.22e-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: 123.89 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQLMGYCP 1974
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1975 QFdaiidlltgrehlefyarlrgvpesyvekvaqwgvqklglsqyadreaggySGGNKRKLSTAIALIGAAPVIFLDEPT 2054
Cdd:cd00267 80 QL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 2055 TGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
910-1116 |
5.49e-32 |
|
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: 125.21 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRTLGV 985
Cdd:cd03292 4 INVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
908-1120 |
9.25e-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: 123.31 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVC 986
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQhnvlfdiltveehvwfygrmkgmsleevnkemnsLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCG 1120
Cdd:cd03214 125 TSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1894-2103 |
1.13e-31 |
|
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: 124.75 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRkPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTE-MEKVHQLMGY 1972
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQF-DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLD 2051
Cdd:COG1122 80 VFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2052 EPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
907-1116 |
1.34e-31 |
|
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: 124.60 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFP-----PTAGTIYVKGMDIRS-DMDII- 979
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDlDVDVLe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 -RRTLGVCPQHNVLFDiLTVEEHVWFYGRMKGMSLEEVNKE-MNSLLEDVGL--QHKRFEQTKNLSGGMQRKLSVAIAFI 1055
Cdd:cd03260 79 lRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
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 ... |
908-1115 |
2.19e-31 |
|
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: 123.70 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLGV 985
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVwfygRMKGMSLEEVNKEMNslLEDV-----GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:cd03224 80 VPEGRRIFPELTVEENL----LLGAYARRRAKRKAR--LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
887-1122 |
6.84e-31 |
|
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: 130.65 E-value: 6.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 887 APREEQDARIEAEPTNLILGVSIRNLVKIYKkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY 966
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 967 VKGMDIRS-DMDIIRRTLGVCPQHNVLFDiLTVEEHVWFYGRmkGMSLEEVNK--EMNSLLEDV-----GLQHKRFEQTK 1038
Cdd:COG4988 396 INGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRP--DASDEELEAalEAAGLDEFVaalpdGLDTPLGEGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1039 NLSGG-MQRkLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHymDEADL-LGDRIAIISQGKL 1116
Cdd:COG4988 473 GLSGGqAQR-LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRI 549
|
....*.
gi 1207110406 1117 CCCGTP 1122
Cdd:COG4988 550 VEQGTH 555
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
905-1122 |
7.15e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.47 E-value: 7.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 905 LGVSIRNLVKIYKKGAKL---AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD---MDI 978
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 --IRRTLGVCPQ--HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKlsVAIA 1053
Cdd:PRK13649 81 kqIRKKVGLVFQfpESQLFE-ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRR--VAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1054 FIGG--SKVVVLDEPTAGVDPYSRRGIWDLLLK-YREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13649 158 GILAmePKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
908-1116 |
2.28e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVkiYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDII--RRTLGV 985
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPPPewRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDiLTVEEHV--WFYGRMKGMSLEEVNKemnsLLEDVGLQHKRFEQ-TKNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:COG4619 79 VPQEPALWG-GTVRDNLpfPFQLRERKFDRERALE----LLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKYR--EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1894-2103 |
3.82e-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: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMekVHQL-MGY 1972
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
907-1123 |
5.89e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.25 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD-MDIIRRTLGV 985
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGM-QRklsVAIAFIGG--SKVV 1061
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQkQR---VAIASVLAlnPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKYREGR--TIILSTHYMDEAdLLGDRIAIISQGKLCCCGTPL 1123
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
907-1116 |
5.98e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.68 E-value: 5.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG--MDIRSDMDIIRRTLG 984
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFY---GRMKGMSLEEVNKEMNSLLEDVGLQ---HKRFEQtknLSGGMQRKlsVAI--AFIG 1056
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDvdpDAKVED---LSVGEQQR--VEIlkALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1057 GSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
909-1115 |
1.17e-29 |
|
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: 119.60 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI----IRRTLG 984
Cdd:cd03256 3 VENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFyGRMKGMSL----------EEVNKEMnSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAF 1054
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLS-GRLGRRSTwrslfglfpkEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1894-2103 |
2.34e-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: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQL-MG 1971
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRARLgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLD 2051
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2052 EPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1893-2198 |
5.87e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.81 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKP-------------------AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAf 1953
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1954 lsnqSVLtemekvhqlmGYCPQ-----FDAIIDLLTG-----------REHLEFYARLRGVPES-YVEKVAQWgVQKLGL 2016
Cdd:COG4586 80 ----RVL----------GYVPFkrrkeFARRIGVVFGqrsqlwwdlpaIDSFRLLKAIYRIPDAeYKKRLDEL-VELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2017 SQYADREAggysggnkRKLS--------TAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSME 2087
Cdd:COG4586 145 GELLDTPV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2088 ECEALCTRMAIMVNGRFQCLGSVQHLKNRFGDGYTIILRLSTPsaepcPVDAYIQnafPGIQLKERHQNVLQYQLPSQTc 2167
Cdd:COG4586 217 DIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP-----VPPLELP---RGGEVIEREGNRVRLEVDPRE- 287
|
330 340 350
....*....|....*....|....*....|.
gi 1207110406 2168 SLARVFEVLSNNYEelgIADYSVSQTTLDQV 2198
Cdd:COG4586 288 SLAEVLARLLARYP---VRDLTIEEPPIEEV 315
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
907-1116 |
6.66e-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: 114.45 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGM--DIRSDMDIIRRTLG 984
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQhnvlfdiltveehvwfygrmkgmsleevnkemnslledvglqhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1065 EPTAGVDPYSRRGIWDLL--LKyREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
909-1122 |
7.02e-29 |
|
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: 117.05 E-value: 7.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKgakLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVCPQ 988
Cdd:cd03299 3 VENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 HNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1069 GVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
907-1116 |
8.17e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.42 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYK--------KGA-----------KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYV 967
Cdd:COG4586 2 IEVENLSKTYRvyekepglKGAlkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 968 KGMDIRSDMDIIRRTLGVcpqhnV-------LFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNL 1040
Cdd:COG4586 82 LGYVPFKRRKEFARRIGV-----VfgqrsqlWWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1041 SGGmQR-KLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG4586 156 SLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
920-1127 |
1.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.20 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 920 AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-----DMDIIRRTLGVC---PQHNv 991
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkKLKPLRKKVGIVfqfPEHQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 992 LFDiLTVEEHVWFyGRMK-GMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKlsVAIAFIGG--SKVVVLDEPT 1067
Cdd:PRK13634 98 LFE-ETVEKDICF-GPMNfGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRR--VAIAGVLAmePEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1068 AGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP--LFLKA 1127
Cdd:PRK13634 174 AGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFADP 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
907-1137 |
1.32e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.96 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGA---KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS---DMDI-- 978
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKYIrp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 IRRTLGVC---PQHNVLFDilTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKLSVAIAF 1054
Cdd:PRK13646 83 VRKRIGMVfqfPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP--LFLKARLG 1130
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPkeLFKDKKKL 240
|
....*..
gi 1207110406 1131 TGYYLTL 1137
Cdd:PRK13646 241 ADWHIGL 247
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
905-1122 |
1.66e-28 |
|
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: 116.28 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 905 LGVSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLG 984
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLE----EVNKEMNSLLEDVGLQ--HKRFEQtkNLSGGMQRKLSVAIAFIGGS 1058
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDwlADRYPA--QLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGI--WDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
907-1123 |
1.87e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQH--KRFeqTKNLSGG-MQRklsVAI--AFIGGSKVV 1061
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDllDRK--PKQLSGGqRQR---VALgrALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1062 VLDEPTAGVDPYSRrgiWDL------LLKyREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPL 1123
Cdd:COG3839 156 LLDEPLSNLDAKLR---VEMraeikrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
905-1116 |
2.28e-28 |
|
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: 115.51 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 905 LGVSIRNLVKiYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLG 984
Cdd:cd03267 19 LIGSLKSLFK-RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 -VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:cd03267 98 vVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLKYREGR--TIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
916-1101 |
3.39e-28 |
|
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: 113.67 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI---RSDMDIIRRTLGVCPQH--N 990
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 991 VLFDIlTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGV 1070
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 1207110406 1071 DPYSRRGIWDLLLKYR-EGRTIILSTHYMDEA 1101
Cdd:TIGR01166 159 DPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1547-1850 |
4.59e-28 |
|
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: 117.88 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1547 ENGSLDQLLQRLPDVLSGLTSQNN--VKVWFNNKGWHAMASFVNIMNNGLLRANLPPKTERRKYGITAYNHPLNLTKEQL 1624
Cdd:pfam12698 75 KNGKIDGLLVIPKGFSKDLLKGESatVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1625 TEMAlmttSVDVLVSICVIFAMSFVPASFVLFLIEERVSKSKHLQFVSGVKPILYWTTNYVWDMVNYTVPatMVVFIFIS 1704
Cdd:pfam12698 155 PQSG----YAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ--LLIILLLL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1705 FQQesYVSEKNLPALVLLLLLYGWSITPLMYPASFIFSVPSTAYVVLTSINLFIGInGSVATFVLELFvdehlnevNRIL 1784
Cdd:pfam12698 229 FGI--GIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDP--------PSFL 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1785 KKVFLIFPHFCLGRGLIDMAKNQAMADAFQrlgtkqnldplswdfvgkNLFAMAMEGIVFFLFTVL 1850
Cdd:pfam12698 298 QWIFSIIPFFSPIDGLLRLIYGDSLWEIAP------------------SLIILLLFAVVLLLLALL 345
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
921-1120 |
4.98e-28 |
|
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: 114.29 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 921 KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TAGTIYVKGMDIRSDMdiIRRTLGVCPQHNVLFDILT 997
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHVWFYGRMKG--MSLEEVNKEM--NSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY 1073
Cdd:cd03234 98 VRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1074 SRRGIWDLLLKY-REGRTIILSTHyMDEADL--LGDRIAIISQGKLCCCG 1120
Cdd:cd03234 178 TALNLVSTLSQLaRRNRIVILTIH-QPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1893-2112 |
6.76e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltemEKVHQLMGY 1972
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQFDAI--------IDL-LTGRehlefYAR---LRGVPESYVEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIA 2040
Cdd:COG1121 80 VPQRAEVdwdfpitvRDVvLMGR-----YGRrglFRRPSRADREAVDEA-LERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRmAIMVNGRFQCLGSVQH 2112
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
907-1116 |
1.84e-27 |
|
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: 112.24 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI---RSDMDIIRRTL 983
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQHNVLFDILTVEEHVWFyGRMK--GMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITL-APIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
920-1122 |
4.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 920 AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-----DMDIIRRTLGVCPQ--HNVL 992
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIKPVRKKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 993 FDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PRK13643 98 FE-ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1072 PYSRRGIWDLLLK-YREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13643 177 PKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1911-2055 |
5.57e-27 |
|
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: 108.50 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1911 VNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL-TEMEKVHQLMGYCPQFDAIIDLLTGREHL 1989
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 EFYARLRGVPESYVEKVAQWGVQKLGLSQYADR----EAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
908-1116 |
5.92e-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: 110.42 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKGAKLaVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDiiRRTLGVCP 987
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 988 Q---HNVLFDilTVEEHVwfygRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:cd03226 78 QdvdYQLFTD--SVREEL----LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLK-YREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1910-2115 |
5.95e-27 |
|
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: 111.37 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEmeKVHQL----MGYCPQFDAIIDLLTG 1985
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL--PPHEIarlgIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1986 REHLE-----------FYARLRGVPESYVEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPT 2054
Cdd:cd03219 93 LENVMvaaqartgsglLLARARREEREARERAEEL-LERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2055 TGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:cd03219 172 AGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
926-1116 |
1.34e-26 |
|
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: 109.89 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 926 HLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFy 1005
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1006 GRMKGMSLEEVNKE-MNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLK 1084
Cdd:cd03298 94 GLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1207110406 1085 YREGR--TIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03298 174 LHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
911-1122 |
1.60e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.37 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 911 NLVKIYKkgAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDI---IRRTLGVCP 987
Cdd:PRK10895 8 NLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLharARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 988 QHNVLFDILTVEEHVWFYGRM-KGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
909-1116 |
1.69e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.36 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKGAK--LAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRT 982
Cdd:PRK11153 4 LKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQHnvlFDIL---TVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGM-QRklsVAIAFIGGS 1058
Cdd:PRK11153 84 IGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQkQR---VAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1059 --KVVVLDEPTAGVDPYSRRGIWDLLLKY-RE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11153 158 npKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
907-1116 |
2.28e-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: 109.27 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1893-2113 |
5.96e-26 |
|
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: 114.62 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG----DTRITyGEAFLSNQSVLTEMEKVH- 1967
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphGGRIS-GEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 QLMGYCPQ-FDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:COG1123 83 RRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
907-1116 |
1.57e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.17 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY--KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIR 980
Cdd:COG1135 2 IELENLSKTFptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVCPQH-NvLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGM-QRklsVAIA--FIG 1056
Cdd:COG1135 82 RKIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQkQR---VGIAraLAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1057 GSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1893-2115 |
1.73e-25 |
|
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: 107.36 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKagRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-LTEMEKVHQL-M 1970
Cdd:TIGR04406 1 TLVAENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDItHLPMHERARLgI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQFDAIIDLLTGREHLEFYARLRG-VPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
907-1116 |
1.83e-25 |
|
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: 106.52 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLF-----DILTV------EEHVWFYGRMKGMSlEEVNKEMNSLLEDVGlqhkrfEQTKNLSGGMQRKLSVAIAF 1054
Cdd:cd03245 83 VPQDVTLFygtlrDNITLgapladDERILRAAELAGVT-DFVNKHPNGLDLQIG------ERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLgDRIAIISQGKL 1116
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1896-2104 |
1.99e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSkvYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQLMGYCP 1974
Cdd:COG4619 3 LEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1975 Q----FDAIIdlltgREHLEFYARLRGVPESYvEKVAQWgVQKLGLSQ-YADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:COG4619 81 QepalWGGTV-----RDNLPFPFQLRERKFDR-ERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
907-1125 |
2.90e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRRTLGV 985
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQ--HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:PRK13647 84 VFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLK-YREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFL 1125
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
907-1132 |
2.97e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 114.84 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDiiRRTlgVC 986
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH--RRA--VC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQ---------HNvLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQhkRFE--QTKNLSGGMQRKLSVAIAFI 1055
Cdd:NF033858 76 PRiaympqglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLA--PFAdrPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1056 GGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGR---TIILSTHYMDEADLLgDRIAIISQGKLCCCGTPLFLKARLGTG 1132
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
907-1122 |
3.56e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.63 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI---RSDMDIIRRTL 983
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQH--NVLFDIlTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:PRK13636 85 GMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
908-1115 |
3.97e-25 |
|
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: 106.22 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDM---DIIRRTLG 984
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLpphRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEH--VWFYGRMKGMSLEEVnkemnslLEDVG-----LQHKRFEQTKNLSGGMQRKLSVAIAFIGG 1057
Cdd:COG0410 82 YVPEGRRIFPSLTVEENllLGAYARRDRAEVRAD-------LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1058 SKVVVLDEPTAGVDPYSRRGIWDLL--LKyREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
907-1116 |
5.21e-25 |
|
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: 104.05 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLvkiykkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLG 984
Cdd:cd03215 5 LEVRGL------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCP---QHNVLFDILTVEEhvwfygrmkgmsleevNKEMNSLLedvglqhkrfeqtknlSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:cd03215 79 YVPedrKREGLVLDLSVAE----------------NIALSSLL----------------SGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
907-1122 |
5.24e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.02 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDI--IRRTLG 984
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVwdVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGmqRKLSVAIAFIGGS--KVV 1061
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGG--QKQRVAIAGVLALqpDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEAdLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
910-1137 |
1.39e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRRTLGVCPQ 988
Cdd:PRK13652 7 RDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 H--NVLFDIlTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:PRK13652 86 NpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP--LFLKARLGTGYYLTL 1137
Cdd:PRK13652 165 TAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDL 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
907-1116 |
1.77e-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: 104.89 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKG--AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI-IRRTL 983
Cdd:COG1124 2 LEVRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKaFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQH-----NVLFdilTVEEHVwfygR--MKGMSLEEVNKEMNSLLEDVGLQ----HKRFEQtknLSGG-MQRklsVA 1051
Cdd:COG1124 82 QMVFQDpyaslHPRH---TVDRIL----AepLRIHGLPDREERIAELLEQVGLPpsflDRYPHQ---LSGGqRQR---VA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1052 I--AFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG1124 149 IarALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
888-1122 |
1.96e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 888 PREEQDARIEAEPTnlilgVSIRNLVKIYKkgAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYV 967
Cdd:PRK11607 6 PRPQAKTRKALTPL-----LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 968 KGMDIrSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRK 1047
Cdd:PRK11607 79 DGVDL-SHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1048 LSVAIAFIGGSKVVVLDEPTAGVDPYSRR----GIWDLLlkYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
908-1122 |
2.29e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVkiYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIR--RTLGV 985
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVL-FDiLTVEEHVwfygRMKGMSLEEVNKEMNSL----LEDVGLQH--KRFEQTknLSGG-MQRklsVAIAFI-- 1055
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVV----AMGRAPHGLSRAEDDALvaaaLAQVDLAHlaGRDYPQ--LSGGeQQR---VQLARVla 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1056 ------GGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
907-1116 |
2.65e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG--MDIRSDMDIIRRTLG 984
Cdd:COG1129 5 LEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFyGRMKG----MSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGmQRKLsVAI--AFIGGS 1058
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFL-GREPRrgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGIWDLL--LKyREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
907-1122 |
4.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTA---GTIYVKGMDIRSD-MDIIRRT 982
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADlLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1896-2108 |
4.84e-24 |
|
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: 102.23 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltemEKVHQLMGYCPQ 1975
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FdAIID----------LLTGRE-HLEFyarLRGVPESYVEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGA 2044
Cdd:cd03235 76 R-RSIDrdfpisvrdvVLMGLYgHKGL---FRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2045 APVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRmAIMVNGRFQCLG 2108
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
907-1122 |
5.03e-24 |
|
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: 102.57 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLF--------DILTV--EEHVWfygrmkgMSLEEVN-KEMNSLLEDvGLQHKRFEQTKNLSGGmQRKL-SVAIA 1053
Cdd:cd03244 83 IPQDPVLFsgtirsnlDPFGEysDEELW-------QALERVGlKEFVESLPG-GLDTVVEEGGENLSVG-QRQLlCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDE-ADLlgDRIAIISQGKLCCCGTP 1122
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
912-1116 |
5.12e-24 |
|
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: 101.86 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 912 LVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTAGTIYVKGmdIRSDMDIIRRTLGVCPQH 989
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING--RPLDKRSFRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 990 NVLFDILTVEEHVWFYGRMKGmsleevnkemnslledvglqhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAG 1069
Cdd:cd03213 91 DILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1070 VDPYSRRGIWDLLLKYR-EGRTIILSTHYM-DEADLLGDRIAIISQGKL 1116
Cdd:cd03213 142 LDSSSALQVMSLLRRLAdTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
887-1122 |
6.46e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.10 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 887 APREEQDARIEAEPTNLILGVSIRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY 966
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 967 VKGMDIRS-DMDIIRRTLGVCPQHNVLFDiLTVEEHVwFYGRmKGMSLEEVNK--EMNSLLEDV-----GLQHKRFEQTK 1038
Cdd:COG1132 399 IDGVDIRDlTLESLRRQIGVVPQDTFLFS-GTIRENI-RYGR-PDATDEEVEEaaKAAQAHEFIealpdGYDTVVGERGV 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1039 NLSGGmQR-KLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTII-----LSThyMDEAdllgDRIAIIS 1112
Cdd:COG1132 476 NLSGG-QRqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIviahrLST--IRNA----DRILVLD 548
|
250
....*....|
gi 1207110406 1113 QGKLCCCGTP 1122
Cdd:COG1132 549 DGRIVEQGTH 558
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1896-2115 |
6.55e-24 |
|
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: 102.58 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL----TEMEKVHQLMG 1971
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFDAIIDLLTGREHLEFYARLRGV-PESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
905-1116 |
7.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 905 LGVSIRNLVKIYKKGA---KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD-----M 976
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DIIRRTLGVCPQ--HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKLSVAIA 1053
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFE-NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
919-1122 |
1.16e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.38 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLGVCPQHNVLFDIL 996
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIARMGVVRTFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEE--------HV---WFYGRMKGMSLEEvnKEMNSL------LEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSK 1059
Cdd:PRK11300 96 TVIEnllvaqhqQLktgLFSGLLKTPAFRR--AESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1060 VVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1893-2111 |
1.21e-23 |
|
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: 102.43 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEM--EKVHQLM 1970
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-LASLsrRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQFDAIIDLLTGRE--------HLEFYARLRgvPESyvEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALI 2042
Cdd:COG1120 78 AYVPQEPPAPFGLTVRElvalgrypHLGLFGRPS--AED--REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2043 GAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQ 2111
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1894-2103 |
1.23e-23 |
|
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: 101.41 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAG--RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVH-- 1967
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 -QLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEEcEALCTRMAIMVNGR 2103
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1893-2103 |
1.57e-23 |
|
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: 102.04 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMeKVHQL--- 1969
Cdd:COG0411 4 LLEVRGLTKRF-GGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGL-PPHRIarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 -MGYCPQFDAIIDLLTGREHLEFyARLRGVPESYVEKVAQWGVQK----------------LGLSQYADREAGGYSGGNK 2032
Cdd:COG0411 80 gIARTFQNPRLFPELTVLENVLV-AAHARLGRGLLAALLRLPRARreereareraeellerVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2033 RKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1893-2113 |
1.86e-23 |
|
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: 101.12 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRK--PAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT----EMEKV 1966
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 HQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1896-2103 |
2.02e-23 |
|
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: 101.25 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRK-------------------PAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAflsn 1956
Cdd:cd03267 3 VSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1957 qsvltemekvhQLMGYCP-----QFDAIIDLLTG-----------REHLEFYARLRGVPES-YVEKVAQWgVQKLGLSQY 2019
Cdd:cd03267 79 -----------RVAGLVPwkrrkKFLRRIGVVFGqktqlwwdlpvIDSFYLLAAIYDLPPArFKKRLDEL-SELLDLEEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2020 ADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAI 2098
Cdd:cd03267 147 LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLV 226
|
....*
gi 1207110406 2099 MVNGR 2103
Cdd:cd03267 227 IDKGR 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1911-2084 |
2.36e-23 |
|
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: 100.81 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1911 VNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG---DTRITYGEAFLSNQSVltEMEKVHQLMGYCPQFDAIIDLLTGRE 1987
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1988 HLEFYARLRGvPESYVEKVAQWGVQKLGLSQYADREAGGY-----SGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPkak 2062
Cdd:cd03234 101 TLTYTAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS--- 176
|
170 180
....*....|....*....|....*.
gi 1207110406 2063 rFLWNCILSVVKE----GRSVVLTSH 2084
Cdd:cd03234 177 -FTALNLVSTLSQlarrNRIVILTIH 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
917-1116 |
3.94e-23 |
|
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: 99.91 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 917 KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmDIRSDMDIirrTLGVCPQhnvlfdiL 996
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL---GGGFNPE-------L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRR 1076
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207110406 1077 GIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03220 180 KCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1894-2108 |
5.14e-23 |
|
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: 99.25 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYC 1973
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLG 2108
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1894-2103 |
6.74e-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: 99.43 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLMG 1971
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFDAIIDLLTGREHLEFYARLRGvpesyvEKVAQWGVQKL-----GLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
921-1116 |
8.27e-23 |
|
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: 98.91 E-value: 8.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 921 KLAVNHLNIKF-YEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG---MDIRSDMDI--IRRTLGVCPQHNVLFD 994
Cdd:cd03297 9 RLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKINLppQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 995 ILTVEEHVWFygRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYS 1074
Cdd:cd03297 89 HLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 1075 RRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:cd03297 167 RLQLLPELkqIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
917-1122 |
8.79e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 917 KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMD-----IIRRTLGVCPQHNV 991
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelreVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 992 LFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1072 PYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK10070 197 PLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
907-1130 |
9.24e-23 |
|
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: 99.22 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRsDMDII--RRTLG 984
Cdd:cd03254 3 IEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKslRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDiLTVEEHVwFYGRmKGMSLEEVNKE-----MNSLLEDV--GLQHKRFEQTKNLSGGMQRKLSVAIAFIGG 1057
Cdd:cd03254 81 VVLQDTFLFS-GTIMENI-RLGR-PNATDEEVIEAakeagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1058 SKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTII-----LSThyMDEAdllgDRIAIISQGKLCCCGTPLFLKARLG 1130
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIiiahrLST--IKNA----DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
907-1116 |
9.74e-23 |
|
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: 97.38 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC 986
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDiltveehvwfygrmkgmsleevnkemNSLLEDVGLQhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03247 81 NQRPYLFD--------------------------TTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYREGRTIILSTHYmdeadLLG----DRIAIISQGKL 1116
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKI 174
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1891-2115 |
1.28e-22 |
|
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: 98.90 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1891 GDILI-LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT----EMEK 1965
Cdd:COG1127 2 SEPMIeVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 VHQLMGYCPQFDAIIDLLTGREHLEFYAR-LRGVPESYVEKVAQWGVQKLGLSQYADReaggY----SGGNKRKLSTAIA 2040
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADK----MpselSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1893-2103 |
1.45e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKagRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTE--MEKVHQL- 1969
Cdd:COG1137 3 TLEAENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKRARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIgAAP-VI 2048
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA-TNPkFI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2049 FLDEPTTGMDPKA----KRFlwncILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
923-1101 |
2.80e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirsdmdiiRRTLGVCPQHNVLFDIL--TVEE 1000
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HV----W----FYGRMKGMSLEEVNKEmnslLEDVGLQHKRFEQTKNLSGG-MQRKLsVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:NF040873 77 LVamgrWarrgLWRRLTRDDRAAVDDA----LERVGLADLAGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 1207110406 1072 PYSRRGIWDLLLKY-REGRTIILSTHYMDEA 1101
Cdd:NF040873 152 AESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1877-2134 |
2.93e-22 |
|
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: 103.44 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1877 VARERERVKNGRALGDILI-LSDLSKVY---KAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEA 1952
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLeVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1953 FLSNQSVLT----EMEKVHQLMGYCPQ--FDAIIDLLTGREHLEFYARLRGV-PESYVEKVAQWGVQKLGLS-QYADREA 2024
Cdd:COG1123 323 LFDGKDLTKlsrrSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2025 GGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260 270
....*....|....*....|....*....|.
gi 1207110406 2104 FQCLGSVQHLKNRFGDGYTIILRLSTPSAEP 2134
Cdd:COG1123 483 IVEDGPTEEVFANPQHPYTRALLAAVPSLDP 513
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
907-1148 |
2.97e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1067 TAGVDpYSRRGIWDLLLKY--RE-GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPlflkarlgtgyyltlvkREMH 1143
Cdd:PRK09452 172 LSALD-YKLRKQMQNELKAlqRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP-----------------REIY 233
|
....*
gi 1207110406 1144 RTPSN 1148
Cdd:PRK09452 234 EEPKN 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1983-2148 |
3.04e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 100.96 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1983 LTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAK 2062
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2063 RFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGdGYTIILRLSTPSAEPCPVDAYIQ 2142
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMVGAIAQ 259
|
....*.
gi 1207110406 2143 NAFPGI 2148
Cdd:NF000106 260 AGLDGI 265
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1896-2108 |
5.71e-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: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSkvYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTemekvhqlmgycpq 1975
Cdd:cd03214 2 VENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 fdaiidlLTGREhlefYARLRGVpesyvekVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:cd03214 66 -------LSPKE----LARKIAY-------VPQA-LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2056 GMDPKAKRFLwnciLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLG 2108
Cdd:cd03214 127 HLDIAHQIEL----LELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
874-1096 |
1.10e-21 |
|
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: 101.59 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 874 GGVPLELGLPIPPAPreeqdarieaeptnlILGVSIRNLVKIYKkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSI 953
Cdd:TIGR02857 304 APRPLAGKAPVTAAP---------------ASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 954 LTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVEEHVWFYgrMKGMSLEEVNK-----EMNSLLEDV 1027
Cdd:TIGR02857 368 LLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAENIRLA--RPDASDAEIREaleraGLDEFVAAL 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1028 --GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTH 1096
Cdd:TIGR02857 445 pqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
906-1283 |
1.79e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 98.65 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 906 GVSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTmSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGV 985
Cdd:NF000106 13 AVEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 C-PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:NF000106 90 HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKARLGTgyyLTLVKREMH 1143
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG---RTLQIRPAH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1144 RTPSNTSSGKIPSAaspkdsdssvsddtglgseenGFDVAALMALAQQyvpdaqlvedigrEAVINLPNAASEDgtLALF 1223
Cdd:NF000106 247 AAELDRMVGAIAQA---------------------GLDGIAGATADHE-------------DGVVNVPIVSDEQ--LSAV 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1224 LNELDKRQgeFGVVSYGLSDTTLEEIFLRVAEET---GVDADPEDPPvsQEPQGApsEDRDAE 1283
Cdd:NF000106 291 VGMLGERG--FTISGHQHPSAQL*EVFLAITGQKtseAADGGPQDGP--QDQQGV--QDKQYE 347
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
923-1121 |
1.86e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRrtLGVC-----PqhNVlFDI 995
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtgLDEHEIAR--LGIGrkfqkP--TV-FEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 996 LTVEEH----------VW--FYGRMKGmsleEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:COG4674 100 LTVFENlelalkgdrgVFasLFARLTA----EERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGT 1121
Cdd:COG4674 176 DEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
907-1116 |
1.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKL---AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD-------- 975
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 976 --MDI---------------IRRTLGVCPQ--HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQ 1036
Cdd:PRK13651 83 vlEKLviqktrfkkikkikeIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1037 TK-NLSGGMQRKlsVAIAFIGG--SKVVVLDEPTAGVDPYSRRGIWDLLLK-YREGRTIILSTHYMDEADLLGDRIAIIS 1112
Cdd:PRK13651 162 SPfELSGGQKRR--VALAGILAmePDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 1207110406 1113 QGKL 1116
Cdd:PRK13651 240 DGKI 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
879-1096 |
2.43e-21 |
|
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: 100.51 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 879 ELGLPIPPAPREEqdARIEAEPTNLILGVSIRnlvkiyKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLF 958
Cdd:TIGR02868 314 AGPVAEGSAPAAG--AVGLGKPTLELRDLSAG------YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 959 PPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVEEHVWFyGRmkgmslEEV-NKEMNSLLEDVGL------- 1029
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL-AR------PDAtDEELWAALERVGLadwlral 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1030 ----QHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTH 1096
Cdd:TIGR02868 458 pdglDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
907-1128 |
2.67e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGA-KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmDIRSDMDI--IRRTL 983
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVwdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEAdLLGDRIAIISQGKLCCCGTPLFLKAR 1128
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
927-1114 |
2.75e-21 |
|
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: 94.84 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIrrtlgVCPQHNVLFDILTVEEHVWFY 1005
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRM-----VVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1006 GR--MKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLL 1083
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 1207110406 1084 KYRE--GRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:TIGR01184 159 QIWEehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1906-2103 |
2.98e-21 |
|
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: 93.77 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTR--ITYGEAFLSNQSVltEMEKVHQLMGYCPQFDAIIDLL 1983
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1984 TGREHLEFYARLRGVpesyvekvaqwgvqklglsqyadreaggySGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKR 2063
Cdd:cd03213 98 TVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207110406 2064 FLWNCILSVVKEGRSVVLTSHSM-EECEALCTRMAIMVNGR 2103
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
923-1122 |
3.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI-----------------IRRTLGV 985
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNhelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 C---PQHNVLFDilTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKlsVAIAFIGG--SK 1059
Cdd:PRK13631 121 VfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRR--VAIAGILAiqPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1060 VVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
907-1115 |
3.86e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.54 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKG---AKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-------RSDM 976
Cdd:COG1101 2 LELKNLSKTFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 diIRR-----TLGVCPQhnvlfdiLTVEEHV---WFYGRMKGMSL------EEVNKEMNSLLeDVGLQHKRFEQTKNLSG 1042
Cdd:COG1101 82 --IGRvfqdpMMGTAPS-------MTIEENLalaYRRGKRRGLRRgltkkrRELFRELLATL-GLGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1043 GmQRK-LSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:COG1101 152 G-QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
916-1122 |
3.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQH----- 989
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQNpdnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 990 ---NVLFDI-LTVEEHVWFYGRMKgmslEEVNKemnsLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:PRK13648 97 vgsIVKYDVaFGLENHAVPYDEMH----RRVSE----ALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKYREGR--TIILSTHYMDEAdLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1894-2103 |
4.14e-21 |
|
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: 92.64 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQL---M 1970
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQFDAIIDLLTGREHLEFyarlrgvpesyvekvaqwgvqklglsqyadreagGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
908-1114 |
4.19e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIY--KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDiirRtlG 984
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpGAD---R--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHkrFEQTK--NLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLAD--FARRRiwQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKY--REGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
907-1122 |
5.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLG 984
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLLLK-YREGRTIILSTHYMDEADlLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
919-1116 |
6.01e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.79 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRTLGVCPQ-HNVLF 993
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQdHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 994 DiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY 1073
Cdd:PRK10908 93 D-RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 1074 SRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK10908 172 LSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
907-1137 |
8.47e-21 |
|
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: 99.41 E-value: 8.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDIlTVEEHVwFYGRMKGMSLEEVNK--EMNSLLEDV-----GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGS 1058
Cdd:TIGR02203 411 VSQDVVLFND-TIANNI-AYGRTEQADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADlLGDRIAIISQGKLCCCGTPLFLKARlgTGYYLTL 1137
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELLAR--NGLYAQL 564
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1893-2103 |
8.99e-21 |
|
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: 93.34 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVY--KAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQL- 1969
Cdd:cd03257 1 LLEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 ---MGYCPQfDAIIDL---LTGREHLE--FYARLRGVPESYVEKVAQWGVQKLGLS-QYADREAGGYSGGNKRKLSTAIA 2040
Cdd:cd03257 81 rkeIQMVFQ-DPMSSLnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDPKAKRflwnCILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQA----QILDLLKKlqeelGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
907-1122 |
9.03e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS---DMDIIRRTL 983
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQHNVLFDILTVEEHVWFyG--RMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMF-GplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1062 VLDEPTAGVDPYSR----RGIWDLLlkyREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK09493 159 LFDEPTSALDPELRhevlKVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1906-2084 |
9.15e-21 |
|
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: 92.42 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTG 1985
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1986 REHLEFYARLRGVPESYVEKvaqwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFL 2065
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 1207110406 2066 WNCILSVVKEGRSVVLTSH 2084
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTH 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
916-1135 |
1.80e-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: 92.93 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFD 994
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 995 iLTVEEHVWFYGrmKGMSLEEVnkEMNSLLEDV---------GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03252 90 -RSIRDNIALAD--PGMSMERV--IEAAKLAGAhdfiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMdEADLLGDRIAIISQGKLCCCGTPLFLKARLGTGYYL 1135
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1896-2102 |
2.06e-20 |
|
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: 91.55 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEaFLSNQSVLTEMEKVhQLMGYCPQ 1975
Cdd:cd03226 2 IENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS-ILLNGKPIKAKERR-KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 fDAIIDLLTGREHLEFYARLRGVPESY--VEKVaqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03226 79 -DVDYQLFTDSVREELLLGLKELDAGNeqAETV----LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2102
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1896-2113 |
2.19e-20 |
|
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: 92.75 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL-TEMEKVHQLMGYCP 1974
Cdd:cd03295 3 FENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1975 QFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGL--SQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
907-1110 |
2.23e-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: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKL--AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TAGTIYVKGMDI----RSDMD 977
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 978 IIR-RTLGVCPQhnvlfD-------ILTVEEHVW-FYGRMKGMSLEEVNKEMNSLLEDVGLQH-----KRF--EqtknLS 1041
Cdd:COG0444 82 KIRgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDperrlDRYphE----LS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1042 GGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHymdeaDL-----LGDRIAI 1110
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITH-----DLgvvaeIADRVAV 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
907-1116 |
2.79e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKgaKLAVNHLNIKFYEGQITSFLGHNGAGKTT---TMSILTGLFP--PTAGTIYVKGMDI---RSDMDI 978
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 IRRTLGVCPQHNVLFDiLTVEEHVWFYGRMKGMSLEEVnkeMNSLLEDVGLQHKRFEQTKN--------LSGGMQRKLSV 1050
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
906-1100 |
3.07e-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: 92.45 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 906 GVSIRnlvkiykKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAG-TIYVKGMDI-RSDMDIIRRTL 983
Cdd:COG1119 8 NVTVR-------RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCpqHNVLFDILTVEEHVW------FYGrmkgmSL---EEVNKEM----NSLLEDVGLQHKRFEQTKNLSGGMQRKLSV 1050
Cdd:COG1119 81 GLV--SPALQLRFPRDETVLdvvlsgFFD-----SIglyREPTDEQreraRELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDE 1100
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1894-2118 |
3.30e-20 |
|
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: 97.53 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEmEKVHQLMG 1971
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdLDE-DDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQfdaiidlltgREHLeFYARLR-----GVPESYVEKVaqWGV-QKLGLSQYADREAGGY-----------SGGNKRK 2034
Cdd:COG4987 413 VVPQ----------RPHL-FDTTLRenlrlARPDATDEEL--WAAlERVGLGDWLAALPDGLdtwlgeggrrlSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2035 LSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKeGRSVVLTSHSMEECEAlCTRMAIMVNGRFQCLGSVQHLK 2114
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
....
gi 1207110406 2115 NRFG 2118
Cdd:COG4987 558 AQNG 561
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
907-1122 |
4.31e-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: 96.80 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY---KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIR--- 980
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 -----RTLGVCPQHNVLFDILTVEEHVwfygrMKGMSLeEVNKEMNSL-----LEDVGLQHKRFEQ-----TKNLSGGMQ 1045
Cdd:TIGR03269 360 rgrakRYIGILHQEYDLYPHRTVLDNL-----TEAIGL-ELPDELARMkavitLKMVGFDEEKAEEildkyPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1046 RKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1910-2103 |
4.45e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.89 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-LTEMEkVHQLMGYCPQFDAIIDLLTGREH 1988
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIA-TRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1989 LEFYARLRGVPESYVEK-VAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWN 2067
Cdd:NF033858 360 LELHARLFHLPAAEIAArVAEM-LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207110406 2068 CI--LSvVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2103
Cdd:NF033858 439 LLieLS-REDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
923-1123 |
5.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDII------RRTLGVC---PQHNVLF 993
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 994 DilTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTK-NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDP 1072
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1073 YSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPL 1123
Cdd:PRK13645 184 KGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
907-1122 |
1.87e-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: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYK--------------------KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY 966
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 967 VKGmDIRSDMDIirrTLGVCPQhnvlfdiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLE--DVGlqhkRFEQT--KNLSG 1042
Cdd:COG1134 85 VNG-RVSALLEL---GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELG----DFIDQpvKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1043 GMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY----SRRGIWDLLlkyREGRTIILSTHYMDEADLLGDRIAIISQGKLCC 1118
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
....
gi 1207110406 1119 CGTP 1122
Cdd:COG1134 227 DGDP 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1896-2103 |
2.19e-19 |
|
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: 89.13 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEaflsnqsvLTEMEKVHQLMGYCPQ 1975
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT--------VTVRGRVSSLLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FDAIidlLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:cd03220 95 FNPE---LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2056 GMDP----KAKRFlwncILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03220 172 VGDAafqeKCQRR----LRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1894-2099 |
2.29e-19 |
|
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: 89.07 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVY--KAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltemEKVHQLMG 1971
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADReaggY----SGGNKRKLSTAIALIGAAPV 2047
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENA----YphqlSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2048 IFLDEPTTGMDPKAKRFLWNCILSVV-KEGRSVVLTSHSMEECEALCTRMAIM 2099
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1894-2117 |
2.48e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.06 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYC 1973
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL----KNRF 2117
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELydrpANLF 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
925-1140 |
2.78e-19 |
|
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: 89.14 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 925 NHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVEEHVw 1003
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1004 FYGRMKGMSLE--EVNKEMN-----SLLED-----VGlqhkrfEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:cd03249 98 RYGKPDATDEEveEAAKKANihdfiMSLPDgydtlVG------ERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1072 PYSRRGIWDLLLKYREGRTIILSTHYMD---EAdllgDRIAIISQGKLCCCGTPLFLKARlgTGYYLTLVKR 1140
Cdd:cd03249 172 AESEKLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGTHDELMAQ--KGVYAKLVKA 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
907-1120 |
3.08e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIR--SDMDIIRRTLG 984
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDILTVEEHVwFYGRMKGMSLEEVN----KEMNS----LLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIG 1056
Cdd:PRK09700 84 IIYQELSVIDELTVLENL-YIGRHLTKKVCGVNiidwREMRVraamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1057 GSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKLCCCG 1120
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
921-1130 |
3.30e-19 |
|
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: 89.21 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 921 KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDIlTVE 999
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1000 EHVwFYGRMKGmSLEEVNK---------EMNSLLEdvGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGV 1070
Cdd:cd03253 93 YNI-RYGRPDA-TDEEVIEaakaaqihdKIMRFPD--GYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1071 DPYSRRGIWDLLLKYREGRTIILSTHYMDEAdLLGDRIAIISQGKLCCCGTPLFLKARLG 1130
Cdd:cd03253 169 DTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
919-1122 |
3.76e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMD-IIRRTLGVCPQHNVLFDILT 997
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHV------W--FYGRMKGMSLEEVNKEMnsllEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAG 1069
Cdd:PRK11231 93 VRELVaygrspWlsLWGRLSAEDNARVNQAM----EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1070 VDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK11231 169 LDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1893-2109 |
4.08e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKaGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQ--SVLTEMEKVHQLM 1970
Cdd:PRK10895 3 TLTAKNLAKAYK-GRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQFDAIIDLLTGREHLEFYARLR-GVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGS 2109
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
907-1115 |
4.62e-19 |
|
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: 88.44 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDIlTVEEHVwFYGRmKGMSLEEVNK--EMNSLLE-----DVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGS 1058
Cdd:cd03251 81 VSQDVFLFND-TVAENI-AYGR-PGATREEVEEaaRAANAHEfimelPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTII-----LSThyMDEAdllgDRIAIISQGK 1115
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
890-1116 |
4.65e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 890 EEQDARIEAEPTNLILgvSIRNLvkiykkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG 969
Cdd:COG1129 242 EDLFPKRAAAPGEVVL--EVEGL------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 970 --MDIRSDMDII----------RRTLGVCPQHNVLFDI-LTVEEHvwfYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQ 1036
Cdd:COG1129 314 kpVRIRSPRDAIragiayvpedRKGEGLVLDLSIRENItLASLDR---LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1037 -TKNLSGGMQRKlsVAIA--FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEadLLG--DRIAI 1110
Cdd:COG1129 391 pVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILV 466
|
....*.
gi 1207110406 1111 ISQGKL 1116
Cdd:COG1129 467 MREGRI 472
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
907-1122 |
5.85e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVC 986
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQ--HKRFeqTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAgfEDRY--VDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1065 EPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1896-2117 |
9.25e-19 |
|
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: 87.68 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvltemekVHQLMGYCPQ 1975
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-------ITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FD------AIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:cd03300 74 VNtvfqnyALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL----KNRF 2117
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1871-2104 |
9.95e-19 |
|
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: 92.17 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1871 GMEDEDVAR------ERERVKNGRALGDILILSDLSKVYKA---GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRML 1941
Cdd:TIGR03269 251 GTPDEVVAVfmegvsEVEKECEVEVGEPIIKVRNVSKRYISvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1942 TGDTRITYGEAFLSNQSVLTEMEK---------------VHQLMGYCPQFDaIIDLLTGREHLEF---YARLRGVpesYV 2003
Cdd:TIGR03269 331 AGVLEPTSGEVNVRVGDEWVDMTKpgpdgrgrakryigiLHQEYDLYPHRT-VLDNLTEAIGLELpdeLARMKAV---IT 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2004 EKVAQWGVQKLG--LSQYADReaggYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVV 2080
Cdd:TIGR03269 407 LKMVGFDEEKAEeiLDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFI 482
|
250 260
....*....|....*....|....
gi 1207110406 2081 LTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:TIGR03269 483 IVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
908-1116 |
1.08e-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: 85.73 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVC 986
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDiltveehvwfygrmkgmsleevnkemNSLLEDVglqhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03246 82 PQDDELFS--------------------------GSIAENI------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1067 TAGVDPYSRRGIWDLL--LKYReGRTIILSTHYMdEADLLGDRIAIISQGKL 1116
Cdd:cd03246 124 NSHLDVEGERALNQAIaaLKAA-GATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
919-1096 |
1.14e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRT-LGvcpQHNVLFDILT 997
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG---HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHVWFYGRMKG---MSLEEVnkemnslLEDVGLQ---HKRFeqtKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PRK13539 90 VAENLEFWAAFLGgeeLDIAAA-------LEAVGLAplaHLPF---GYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*.
gi 1207110406 1072 PYSRRGIWDLLLKYRE-GRTIILSTH 1096
Cdd:PRK13539 160 AAAVALFAELIRAHLAqGGIVIAATH 185
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1887-2103 |
1.19e-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: 88.47 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1887 GRALGDILILSDLSKVYKA-GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT---- 1961
Cdd:cd03294 15 QKAFKLLAKGKSKEEILKKtGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1962 --------EMEKVHQLMGYCPQfdaiidlLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKR 2033
Cdd:cd03294 95 elrelrrkKISMVFQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2034 KLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
934-1115 |
1.19e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFyGRMKGMSL 1013
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQENNLFPHLTVAQNIGL-GLRPGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1014 EEVNKE-MNSLLEDVGLQHkrFEQTK--NLSGG-MQRklsVAIA--FIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKY 1085
Cdd:COG3840 103 TAEQRAqVEQALERVGLAG--LLDRLpgQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDLVdeLCR 177
|
170 180 190
....*....|....*....|....*....|
gi 1207110406 1086 REGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:COG3840 178 ERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1893-2117 |
1.62e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.77 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL-TEMEKVHqlMG 1971
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTgLPPEKRN--VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNK-RklsTAIA--LIGAAPVI 2048
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VALAraLAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL----KNRF 2117
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATRF 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1913-2084 |
3.14e-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: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1913 RLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGREHLEFY 1992
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1993 ARLRGvPESYVEKVAQwgvqkLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSV 2072
Cdd:cd03231 98 HADHS-DEQVEEALAR-----VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 1207110406 2073 VKEGRSVVLTSH 2084
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1896-2103 |
5.26e-18 |
|
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: 85.31 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG------DTRITyGEAFLSNQSVLTEMEKVHQL 1969
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDE-GEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 ---MGYCPQ----FDAIIdlltgREHLEFYARLRGV-PESYVEKVAQWGVQKLGLSQYADREAGGY--SGGNKRKLSTAI 2039
Cdd:cd03260 80 rrrVGMVFQkpnpFPGSI-----YDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHALglSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2040 ALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEgRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
888-1138 |
6.32e-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: 90.57 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 888 PREEQDARIEAEPTNLILGVSIRNLVKIYKKGAKlAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYV 967
Cdd:TIGR01193 455 DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 968 KGMDIRS-DMDIIRRTLGVCPQHNVLFD--IL----------TVEEHVWfygrmKGMSLEEVNKEMNSLleDVGLQHKRF 1034
Cdd:TIGR01193 534 NGFSLKDiDRHTLRQFINYLPQEPYIFSgsILenlllgakenVSQDEIW-----AACEIAEIKDDIENM--PLGYQTELS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1035 EQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREgRTIILSTHYMDEADLLgDRIAIISQG 1114
Cdd:TIGR01193 607 EEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHG 684
|
250 260
....*....|....*....|....
gi 1207110406 1115 KLCCCGTPLFLKARlgTGYYLTLV 1138
Cdd:TIGR01193 685 KIIEQGSHDELLDR--NGFYASLI 706
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
923-1116 |
1.11e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS--DMDIIRRTLGVCPQHNVLFDILTVEE 1000
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HVwfygRMKGMSLEEvnKEMNSLLEDV-----GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSR 1075
Cdd:PRK11614 100 NL----AMGGFFAER--DQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 1076 RGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11614 174 QQIFDTIEQLReQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
930-1122 |
1.30e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 930 KFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TAGTIYVKGMDIRSDMdiIRRTLGVCPQHNVLFDILTVEEHVWFYG 1006
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1007 --RMKGMSLEEVNKEM-NSLLEDVGL---QHKRF---EQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRG 1077
Cdd:TIGR00955 125 hlRMPRRVTKKEKRERvDEVLQALGLrkcANTRIgvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 1078 IWDLLLKY-REGRTIILSTHyMDEADL--LGDRIAIISQGKLCCCGTP 1122
Cdd:TIGR00955 205 VVQVLKGLaQKGKTIICTIH-QPSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
926-1096 |
1.35e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 926 HLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFY 1005
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1006 GRMKGMSLEEvnkEMNSLLEDVGLQhkRFEQ--TKNLSGGMQRKlsVAIA--FIGGSKVVVLDEP-----TAGVDPYSRR 1076
Cdd:PRK13538 99 QRLHGPGDDE---ALWEALAQVGLA--GFEDvpVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQGVARLEAL 171
|
170 180
....*....|....*....|
gi 1207110406 1077 giwdLLLKYREGRTIILSTH 1096
Cdd:PRK13538 172 ----LAQHAEQGGMVILTTH 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1893-2103 |
1.35e-17 |
|
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: 84.26 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEMeKVHQL--- 1969
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-ITGL-PPHRIarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 -MGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQwgVQKL--GLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:COG0410 79 gIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLER--VYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
890-1117 |
1.91e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 890 EEQDARIEAEPTNLILGVSirNLvkiykKGAklAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG 969
Cdd:PRK10762 243 EDQYPRLDKAPGEVRLKVD--NL-----SGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 970 MDIRSdmdiirrtlgVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEvNKEMNSLLE----DVGLQHKRFEQT-------- 1037
Cdd:PRK10762 314 HEVVT----------RSPQDGLANGIVYISEDRKRDGLVLGMSVKE-NMSLTALRYfsraGGSLKHADEQQAvsdfirlf 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1038 -----------KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEadLLG 1105
Cdd:PRK10762 383 niktpsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPE--VLG 460
|
250
....*....|....
gi 1207110406 1106 --DRIAIISQGKLC 1117
Cdd:PRK10762 461 msDRILVMHEGRIS 474
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
907-1116 |
2.64e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYK-----KGAKLAVNhlnikfyEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI--- 978
Cdd:PRK11264 4 IEVKNLVKKFHgqtvlHGIDLEVK-------PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 ------IRRTLGVCPQHNVLFDILTVEEHVwFYGRM--KGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSV 1050
Cdd:PRK11264 77 kglirqLRQHVGFVFQNFNLFPHRTVLENI-IEGPVivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVDPysrRGIWDLLLKYR----EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
927-1122 |
3.38e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI---RSDMDIIRRTLGVC---PQHNVLFDilTVEE 1000
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYT--DIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWD 1080
Cdd:PRK13638 98 DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207110406 1081 LLLK-YREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK13638 178 IIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1892-2110 |
3.40e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1892 DILILSDLSKVYKAGRKP--------------------AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGe 1951
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1952 aflsnqSVLTEMeKVHQL----MGYCPQfdaiidlLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGY 2027
Cdd:COG1134 82 ------RVEVNG-RVSALlelgAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2028 SGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP----KAKRFlwncILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*..
gi 1207110406 2104 FQCLGSV 2110
Cdd:COG1134 224 LVMDGDP 230
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
923-1122 |
3.49e-17 |
|
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: 83.19 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TAGTIYVKGMDIrSDMDIIRRTLGVCPQH--NVLFDIL 996
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKR-------FEqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAG 1069
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlkkypFQ----LSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1070 VDPYSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1881-2169 |
3.76e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1881 RERVKNGRALGDILILSDLSKVYKAgrKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvL 1960
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1961 TEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIA 2040
Cdd:PRK11607 84 SHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGS----VQHLKN 2115
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTT 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2116 RFgdgytiilrlstpSAEpcpvdaYIQ--NAFPGIqLKERHQNVLQYQLPSQTCSL 2169
Cdd:PRK11607 244 RY-------------SAE------FIGsvNVFEGV-LKERQEDGLVIDSPGLVHPL 279
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1893-2103 |
4.81e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAG--RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVH- 1967
Cdd:COG1136 4 LLELRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 --QLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAA 2045
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2046 PVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSmEECEALCTRMAIMVNGR 2103
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
907-1116 |
4.92e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKL-AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD-MDIIRRTLG 984
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQH-NVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVL 1063
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1064 DEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEAdLLGDRIAIISQGKL 1116
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1899-2103 |
6.32e-17 |
|
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: 82.62 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1899 LSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK-----------VH 1967
Cdd:cd03256 6 LSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqigmIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 QLMGYCPQFDAIIDLLTGR--EHLEFYARLRGVPESYVEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAA 2045
Cdd:cd03256 85 QQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2046 PVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
925-1122 |
6.43e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 925 NHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGVCPQHNVLFDILTVEEHVWF 1004
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1005 ----YGRMKGMSLEEVNKEMNSLLEDVGLQH--KRFeqTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGI 1078
Cdd:PRK10851 98 gltvLPRRERPNAAAIKAKVTQLLEMVQLAHlaDRY--PAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1079 WDLL------LKYregrTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK10851 176 RRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
914-1116 |
7.55e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 914 KIYKKGAKLA------VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTAGTIYVKGMDI-RSDMDIIRR 981
Cdd:PRK14247 3 KIEIRDLKVSfgqvevLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLGVCPQHNVLFDILTVEEHVWFygrmkGMSLEEVNKEMNSLLEDV--GLQHKR-FEQTKN--------LSGGMQRKLSV 1050
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVAL-----GLKLNRLVKSKKELQERVrwALEKAQlWDEVKDrldapagkLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1904-2123 |
7.60e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1904 KAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTS-----TFRMLTGdtrITYGEAFLSNQSVLtEMEKVHQLMGYCPQFDA 1978
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKG---VKGSGSVLLNGMPI-DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1979 IIDLLTGREHLEFYARLRgVPESYVEKVAQWGV----QKLGLSQYADREAG------GYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLR-MPRRVTKKEKRERVdevlQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2049 FLDEPTTGMDPkakrFLWNCILSVVKE----GRSVVLTSH--SMEECEaLCTRMAIMVNGRFQCLGSVQHLKNRFGD-GY 2121
Cdd:TIGR00955 189 FCDEPTSGLDS----FMAYSVVQVLKGlaqkGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGH 263
|
..
gi 1207110406 2122 TI 2123
Cdd:TIGR00955 264 PC 265
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1893-2103 |
7.69e-17 |
|
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: 82.44 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFlsnqSVL------TEMEKV 1966
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFgerrggEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 HQLMGY--------CPQFDAIID-LLTGrehleFYA---RLRGVPESYVEKVAQWgVQKLGLSQYADREAGGYSGGNKRK 2034
Cdd:COG1119 77 RKRIGLvspalqlrFPRDETVLDvVLSG-----FFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2035 LSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEG-RSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1894-2102 |
8.41e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKvhQLMGYC 1973
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQ-------FDAIID--LLTGRE-HLEFYARlrgvPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIG 2043
Cdd:PRK15056 84 PQseevdwsFPVLVEdvVMMGRYgHMGWLRR----AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2044 AAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTrMAIMVNG 2102
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1894-2111 |
8.55e-17 |
|
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: 82.00 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNrlcLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLsNQSVLTEMEKVHQLMGYC 1973
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVS---LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-NGKDITNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVL-TSHSMEECEALCTRMAIMVNGRFQCLGSVQ 2111
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1894-2104 |
9.20e-17 |
|
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: 80.43 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYC 1973
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQfdaiidlltgREHLeFYARLRgvpesyvekvaqwgvQKLGLSqyadreaggYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03247 81 NQ----------RPYL-FDTTLR---------------NNLGRR---------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEgRSVVLTSHSMEECEALcTRMAIMVNGRF 2104
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1921-2085 |
9.94e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPE 2000
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLGGEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2001 SYVEKVAQwgvqKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVV 2080
Cdd:PRK13539 106 LDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVI 181
|
....*
gi 1207110406 2081 LTSHS 2085
Cdd:PRK13539 182 AATHI 186
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
927-1096 |
1.45e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMD-----IIRRT-LGVCPQHNVLFDILTVEE 1000
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-ATLDadalaQLRREhFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWD 1080
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170
....*....|....*..
gi 1207110406 1081 LLLKYRE-GRTIILSTH 1096
Cdd:PRK10535 186 ILHQLRDrGHTVIIVTH 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
910-1105 |
2.83e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKKGaKLAVNHL-NIKFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG-----MDIRSDMDIIRR 981
Cdd:PRK11629 9 DNLCKRYQEG-SVQTDVLhNVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmskLSSAAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLGVCPQ-HNVLFDiLTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:PRK11629 88 KLGFIYQfHHLLPD-FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLG 1105
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
887-1116 |
2.99e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 887 APREEQDARIEAEPT----NLILgvSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTA 962
Cdd:COG0488 294 PPRRDKTVEIRFPPPerlgKKVL--ELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 963 GTIYVkGMDIRsdmdiirrtLGVCPQHNVLFDI-LTVEEHVWfyGRMKGMSLEEVnkemNSLLEDVGL----QHKRfeqT 1037
Cdd:COG0488 370 GTVKL-GETVK---------IGYFDQHQEELDPdKTVLDELR--DGAPGGTEQEV----RGYLGRFLFsgddAFKP---V 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1038 KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYrEGrTIILSTHymDEA--DLLGDRIAIISQGK 1115
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSH--DRYflDRVATRILEFEDGG 506
|
.
gi 1207110406 1116 L 1116
Cdd:COG0488 507 V 507
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1910-2103 |
3.53e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltEMEKVHQL--MGYCPQFD---------A 1978
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIarMGVVRTFQhvrlfremtV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1979 IIDLLTGR-EHLE--FYARLRGVPeSY-------VEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:PRK11300 98 IENLLVAQhQQLKtgLFSGLLKTP-AFrraeseaLDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
919-1114 |
3.67e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdIRSDMDIIRRtlGVCPQHNVLFDILTV 998
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 999 EEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQ--HKRFeqTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRR 1076
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEgaEKRY--IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207110406 1077 GIWDLLLK--YREGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:PRK11248 166 QMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1926-2084 |
4.28e-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: 78.82 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1926 LLGVNGAGKTSTFRMLTG--DTRITYGEAFLSNQSVLTEMEKVhqlMGYCPQFDAIIDLLTGREHLEFYARLRGvpesyv 2003
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALLRG------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2004 ekvaqwgvqkLGLSQyadreaggysggnKRKLSTAIALIgAAPVI-FLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLT 2082
Cdd:cd03232 109 ----------LSVEQ-------------RKRLTIGVELA-AKPSIlFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCT 164
|
..
gi 1207110406 2083 SH 2084
Cdd:cd03232 165 IH 166
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1893-2104 |
5.10e-16 |
|
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: 78.24 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSkvykagRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLM 1970
Cdd:cd03215 4 VLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCP---QFDAIIDLLTGREHLEFYARLrgvpesyvekvaqwgvqklglsqyadreaggySGGNKRKLSTAIALIGAAPV 2047
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2048 IFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1896-2103 |
5.22e-16 |
|
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: 77.47 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltemekvhqlmgycpQ 1975
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------S 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FDAIIDlltgrehlefyARLRGVpesyvEKVAQwgvqklglsqyadreaggYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:cd03216 66 FASPRD-----------ARRAGI-----AMVYQ------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1913-2084 |
5.99e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1913 RLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGREHLEFY 1992
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1993 ARLRGVPESyvEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSV 2072
Cdd:PRK13538 99 QRLHGPGDD--EALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQH 175
|
170
....*....|..
gi 1207110406 2073 VKEGRSVVLTSH 2084
Cdd:PRK13538 176 AEQGGMVILTTH 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
936-1122 |
6.27e-16 |
|
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: 81.70 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 936 ITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-----DMDIIRRTLGVCPQHNVLFDILTVEEHVwFYGRMKG 1010
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNL-RYGMKRA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1011 MSlEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--G 1088
Cdd:TIGR02142 104 RP-SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAefG 182
|
170 180 190
....*....|....*....|....*....|....
gi 1207110406 1089 RTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
908-1096 |
8.77e-16 |
|
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: 78.17 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLvkIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCP 987
Cdd:TIGR01189 2 AARNL--ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 988 QHNVLFDILTVEEHVWFYGRMKG---MSLEEvnkemnsLLEDVGLQHkrFEQT--KNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGgaqRTIED-------ALAAVGLTG--FEDLpaAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTH 1096
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLArGGIVLLTTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1893-2103 |
1.43e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTF----RMLTGDT-RITYGE---------------A 1952
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLkcfaRLLTPQSgTVFLGDkpismlssrqlarrlA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1953 FLSNQSVLTEMEKVHQLMGYcpqfdaiidlltGRE-HLEFYARLRGVPESYVekvaQWGVQKLGLSQYADREAGGYSGGN 2031
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAY------------GRSpWLSLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2032 KRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
876-1117 |
2.26e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 876 VPLELGLPIPPAPREEQDarieaeptnlilgVSIRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILT 955
Cdd:PRK10522 305 APYKAEFPRPQAFPDWQT-------------LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLT 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 956 GLFPPTAGTIYVKGMDIRS-DMDIIRRtlgvcpqhnvLFDilTVEEHVWFYGRMKGMSLEEVNKEM-NSLLEDVGLQHK- 1032
Cdd:PRK10522 371 GLYQPQSGEILLDGKPVTAeQPEDYRK----------LFS--AVFTDFHLFDQLLGPEGKPANPALvEKWLERLKMAHKl 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1033 RFEQTK----NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-RE-GRTIILSTH---YMDEAdl 1103
Cdd:PRK10522 439 ELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLlQEmGKTIFAISHddhYFIHA-- 516
|
250
....*....|....
gi 1207110406 1104 lgDRIAIISQGKLC 1117
Cdd:PRK10522 517 --DRLLEMRNGQLS 528
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
918-1122 |
2.65e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 918 KGAKLAVNhlnikfyEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIR--SDMD------------IIRRTL 983
Cdd:PRK10619 22 KGVSLQAN-------AGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvRDKDgqlkvadknqlrLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 984 GVCPQHNVLFDILTVEEHVWFYG-RMKGMSLEEVNKEMNSLLEDVGLQHK-RFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1897-2109 |
2.81e-15 |
|
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: 77.76 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1897 SDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYCPQF 1976
Cdd:cd03296 6 RNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1977 DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKL----GLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGS 2109
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1893-2103 |
2.86e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV------LTEMEKV 1966
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 ---------HQLmgycpqFDAIIdlltgREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLST 2037
Cdd:PRK13636 84 vgmvfqdpdNQL------FSASV-----YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2038 AIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1898-2113 |
3.39e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1898 DLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTE-MEKVHQLMGYCPQF 1976
Cdd:PRK13652 8 DLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1977 -DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:PRK13652 87 pDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1894-2103 |
4.38e-15 |
|
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: 75.11 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQLMGY 1972
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQ----FDAIIdlltgREHLefyarlrgvpesyvekvaqwgvqklglsqyadreaggYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:cd03228 81 VPQdpflFSGTI-----RENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSvVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2103
Cdd:cd03228 119 ILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1910-2159 |
5.03e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLMGYCPQFDAIIDLLTGRE 1987
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1988 HLeFYARLR-----GVP---ESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP 2059
Cdd:PRK09700 100 NL-YIGRHLtkkvcGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2060 KAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNrfgDGytiILRLStpsaepcpVDA 2139
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN---DD---IVRLM--------VGR 244
|
250 260
....*....|....*....|
gi 1207110406 2140 YIQNAFPGiqLKERHQNVLQ 2159
Cdd:PRK09700 245 ELQNRFNA--MKENVSNLAH 262
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
934-1096 |
6.23e-15 |
|
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: 75.61 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFYGRMKGMS- 1012
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1013 LEEVNKEMNSlledVGLQHKRFEQtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTI 1091
Cdd:cd03231 106 VEEALARVGL----NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCArGGMV 178
|
....*
gi 1207110406 1092 ILSTH 1096
Cdd:cd03231 179 VLTTH 183
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1892-2090 |
8.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1892 DILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG--------DTRITYGEAFLSNQSVLTEM 1963
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1964 EKV--------HQLMGycpqfdAII--DLLTGREHlefyarlRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKR 2033
Cdd:PRK13640 84 EKVgivfqnpdNQFVG------ATVgdDVAFGLEN-------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2034 KLSTAIALIGAAPVIFLDEPTTGMDPKAKrflwNCILSVVKE-----GRSVVLTSHSMEECE 2090
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1896-2054 |
1.00e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSN----------------QSV 1959
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1960 LTEMEKVHQ-LMGYCPQFDAIIDLL-TGREHLEFYARLRGV--------PESYVEKVAqwgvQKLGLSQ-YADREAGGYS 2028
Cdd:COG0488 79 LDTVLDGDAeLRALEAELEELEAKLaEPDEDLERLAELQEEfealggweAEARAEEIL----SGLGFPEeDLDRPVSELS 154
|
170 180
....*....|....*....|....*.
gi 1207110406 2029 GGNKRKLSTAIALIGAAPVIFLDEPT 2054
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
907-1116 |
1.04e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTT---TMSILTGLFPP--TAGTIYVKGMDIRS-DMDII- 979
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGEDIYDpDVDVVe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 -RRTLGVCPQH----------NVLfdiltveehvwfYG-RMKGM-SLEEVNKEMNSLLEDVGLqhkrFEQTKN------- 1039
Cdd:COG1117 90 lRRRVGMVFQKpnpfpksiydNVA------------YGlRLHGIkSKSELDEIVEESLRKAAL----WDEVKDrlkksal 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1040 -LSGGMQRKLSVA--IAFigGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG1117 154 gLSGGQQQRLCIAraLAV--EPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
934-1096 |
1.16e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.59 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRT------LGVCPQHNVLFDILTVEEHVWFYGR 1007
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEEARAklrakhVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1008 MKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKY 1085
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNR 194
|
170
....*....|.
gi 1207110406 1086 REGRTIILSTH 1096
Cdd:PRK10584 195 EHGTTLILVTH 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
907-1114 |
1.42e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKfyEGQITSFLGHNGAGKTTTMSILTGLF-----PPT-----AGTIYVKGM---DIR 973
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIH--HGEMVALLGPSGSGKSTLLRHLSGLItgdksAGShiellGRTVQREGRlarDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 974 SDmdiiRRTLGVCPQHNVLFDILTVEEHV----------------WFYGRMKGMSLEEVNKemnslledVGLQHKRFEQT 1037
Cdd:PRK09984 83 KS----RANTGYIFQQFNLVNRLSVLENVligalgstpfwrtcfsWFTREQKQRALQALTR--------VGMVHFAHQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1038 KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
906-1125 |
1.48e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 906 GVSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGV 985
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGmQRKlSVAIA--FIGGSKVVVL 1063
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGG-QRQ-RVAIGrtLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1064 DEPTAGVDPYSR---RgIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFL 1125
Cdd:PRK11000 158 DEPLSNLDAALRvqmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
907-1140 |
1.50e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLF-----DILTveehvwfygrmkgMSLEEVNKE-MNSLLEDVGLQhKRFEQTKNL-----------SGGMQRKL 1048
Cdd:PRK11160 419 VSQRVHLFsatlrDNLL-------------LAAPNASDEaLIEVLQQVGLE-KLLEDDKGLnawlgeggrqlSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1049 SVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHymdeaDLLG----DRIAIISQGKLCCCGTPLF 1124
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*.
gi 1207110406 1125 LKARLgtGYYLTLVKR 1140
Cdd:PRK11160 560 LLAQQ--GRYYQLKQR 573
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1893-2103 |
1.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.27 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFL-------SNQSVLtemeK 1965
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgepikyDKKSLL----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 VHQLMGYCPQF-DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGA 2044
Cdd:PRK13639 76 VRKTVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2045 APVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1893-2103 |
1.74e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG-----DTRITYGEAFLSNQSVLTEMEKV- 1966
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlllpeAGTITVGGMVLSEETVWDVRRQVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 -------HQLMGycpqfdaiidlLTGREHLEFYARLRGVP-ESYVEKVaQWGVQKLGLSQYADREAGGYSGGNKRKLstA 2038
Cdd:PRK13635 85 mvfqnpdNQFVG-----------ATVQDDVAFGLENIGVPrEEMVERV-DQALRQVGMEDFLNREPHRLSGGQKQRV--A 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2039 IA-LIGAAP-VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2103
Cdd:PRK13635 151 IAgVLALQPdIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1921-2105 |
1.82e-14 |
|
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: 74.64 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLsNQSVLTEMEK-----VHQL-MGYCPQFDAIIDLLTGREHLEFYAR 1994
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTVLFDSRKkinlpPQQRkIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1995 L--RGVPESYVEKVaqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSV 2072
Cdd:cd03297 102 RkrNREDRISVDEL----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....
gi 1207110406 2073 VKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1896-2103 |
2.33e-14 |
|
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: 74.55 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNqsvlTEMEKVH-----QLM 1970
Cdd:cd03245 5 FRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQLDpadlrRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQfDAiidlltgreHLeFYARLR-----GVPESYVEKVAQwGVQKLGLSQYADREAGGY-----------SGGNKRK 2034
Cdd:cd03245 81 GYVPQ-DV---------TL-FYGTLRdnitlGAPLADDERILR-AAELAGVTDFVNKHPNGLdlqigergrglSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2035 LSTAIALIGAAPVIFLDEPTTGMDPKA-KRFLWNciLSVVKEGRSVVLTSH--SMEEceaLCTRMAIMVNGR 2103
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
909-1116 |
2.90e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmDIRsdmdiirrtLGVCPQ 988
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 HNVLFDILTVEEHVW--FYGRMKGMS-LEEVNKEM---NSLLEDVGLQHKRFE--------------------------- 1035
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgDAELRALEAeLEELEAKLaepDEDLERLAELQEEFEalggweaearaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1036 QTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRgiW--DLLLKYReGrTIILSTH---YMDEadlLGDRIAI 1110
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSHdryFLDR---VATRILE 221
|
....*.
gi 1207110406 1111 ISQGKL 1116
Cdd:COG0488 222 LDRGKL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1894-2108 |
2.96e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-LTEMEKVHQLMGY 1972
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQ-------FD--AIIDLltGRE-HLEFYARLRGVPESYVEKvaqwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALI 2042
Cdd:PRK09536 82 VPQdtslsfeFDvrQVVEM--GRTpHRSRFDTWTETDRAAVER----AMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2043 GAAPVIFLDEPTTGMD-PKAKRFLwNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLG 2108
Cdd:PRK09536 156 QATPVLLLDEPTASLDiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
907-1116 |
3.02e-14 |
|
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: 75.23 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIY-------KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSD 975
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 976 MDIIRRTL---------GVCPQHNVLFDILTVEEHvwfygrMKGMSLEEVNKEMNSLLEDVGLQHKRFEQ-TKNLSGGMQ 1045
Cdd:TIGR02769 83 RRAFRRDVqlvfqdspsAVNPRMTVRQIIGEPLRH------LTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1046 RKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
921-1121 |
3.16e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.08 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 921 KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI-------IRRTLGVCPQHNVLF 993
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidaikLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 994 DILTVEEHVWFYGRMKGMSLE-EVNKEMNSLLEDVGLQHKRFEQ----TKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1069 GVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGT 1121
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
907-1116 |
3.30e-14 |
|
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: 74.87 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDiRSDMDII------R 980
Cdd:TIGR02323 4 LQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRS-GAELELYqlseaeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTL-----GVCPQH-------------NVLFDILTV-EEHvwfYGRMKgmsleevnKEMNSLLEDVGLQHKRFE-QTKNL 1040
Cdd:TIGR02323 81 RRLmrtewGFVHQNprdglrmrvsagaNIGERLMAIgARH---YGNIR--------ATAQDWLEEVEIDPTRIDdLPRAF 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1041 SGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1920-2103 |
4.11e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1920 RGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLMGYCP---QFDAIIDLLTGRE-----HL 1989
Cdd:COG1129 277 AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDAIRAGIAYVPedrKGEGLVLDLSIREnitlaSL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 EFYARLRGVPESYVEKVAQWGVQKLGL-SQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNC 2068
Cdd:COG1129 357 DRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
170 180 190
....*....|....*....|....*....|....*
gi 1207110406 2069 ILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1129 437 IRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
907-1116 |
4.22e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.49 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTAGTIYVKGMDIRS-DMDII- 979
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 -RRTLGVCPQHNVLFDILTVEEHVWFYGRMKGM--SLEEVNKEMNSLLEDVGL----QHKRFEQTKNLSGGMQRKLSVAI 1052
Cdd:PRK14267 83 vRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1053 AFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1893-2087 |
4.62e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.55 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRkPAVNRLCLGIPRGE-CFgLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEM--EKVHQL 1969
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLkrREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 ---MGYCPQfdaiiD--LLTGR---EHLEFYARLRGVPESYVEK-VAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIA 2040
Cdd:COG2884 78 rrrIGVVFQ-----DfrLLPDRtvyENVALPLRVTGKSRKEIRRrVREV-LDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSME 2087
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
940-1116 |
4.98e-14 |
|
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: 73.62 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 940 LGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMD------IIRRTLGVCPQHNVLFDILTVEEHVwfygrmkGMSL 1013
Cdd:COG4181 44 VGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALDedararLRARHVGFVFQSFQLLPTLTALENV-------MLPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1014 EEVN-----KEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYR 1086
Cdd:COG4181 116 ELAGrrdarARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRE 195
|
170 180 190
....*....|....*....|....*....|.
gi 1207110406 1087 EGRTIILSTHymDEADLL-GDRIAIISQGKL 1116
Cdd:COG4181 196 RGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
911-1127 |
5.42e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 911 NLVKI----YKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDMDIIRRT 982
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQHNVLFDILTVEEHVWFYGRMKGMSLEEVNKEMNSL-LEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1062 VLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFLKA 1127
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
908-1122 |
6.91e-14 |
|
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: 72.56 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNL-VKIykkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGlFP---PTAGTIYVKGMDIrSDMDI---IR 980
Cdd:cd03217 2 EIKDLhVSV---GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVCPQHNVlfdiltveehvwfygRMKGMSLEEVNKEMNslledvglqhkrfeqtKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:cd03217 77 LGIFLAFQYPP---------------EIPGVKNADFLRYVN----------------EGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLL-GDRIAIISQGKLCCCGTP 1122
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1898-2110 |
7.03e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1898 DLSKVYKAG---RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAF-----LSNQSV-LTEMEKV-- 1966
Cdd:PRK13637 7 NLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdITDKKVkLSDIRKKvg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 -------HQLmgycpqFDAIIDlltgrEHLEFYARLRGVPESYVEKVAQWGVQKLGLS--QYADREAGGYSGGNKRKLST 2037
Cdd:PRK13637 87 lvfqypeYQL------FEETIE-----KDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2038 AIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSV 2110
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
900-1116 |
8.07e-14 |
|
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: 72.89 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 900 PTNLILGVSIRNLVKIYK-KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMD 977
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 978 IIRRTLGVCPQHNVLFDiLTVEEHVwFYGrMKGMSLEEVNKEMN--------SLLEDvGLQHKRFEQTKNLSGGMQRKLS 1049
Cdd:cd03248 85 YLHSKVSLVGQEPVLFA-RSLQDNI-AYG-LQSCSFECVKEAAQkahahsfiSELAS-GYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1050 VAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADlLGDRIAIISQGKL 1116
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
928-1116 |
8.73e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 928 NIKF--YEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG--MDIRSDMD-------IIRRTLGVCPQhnvlfdiL 996
Cdd:PRK11288 22 DISFdcRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAalaagvaIIYQELHLVPE-------M 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEEHVW---FYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVdpy 1073
Cdd:PRK11288 95 TVAENLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL--- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 1074 SRRGIWDLL-----LKyREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11288 172 SAREIEQLFrvireLR-AEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
933-1122 |
1.43e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 933 EGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVL---FDILTVEE-----HVw 1003
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLsfeFDVRQVVEmgrtpHR- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1004 fyGRMKGMSlEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDpySRRGIWDLLL 1083
Cdd:PRK09536 107 --SRFDTWT-ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--INHQVRTLEL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 1084 KYR---EGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK09536 182 VRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
919-1122 |
1.61e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIR--SDMDIIRRtLGVCPQHNVLFDIL 996
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARR-IGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 TVEE--------HVWFYGRMKGMSLEEVNKEMNSlledVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:PRK10253 97 TVQElvargrypHQPLFTRWRKEDEEAVTKAMQA----TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1069 GVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTP 1122
Cdd:PRK10253 173 WLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
927-1116 |
1.74e-13 |
|
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: 75.60 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRrtlgvcpQH-------NVLFDilt 997
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYR-------QLfsavfsdFHLFD--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 veehvwfygRMKGMSLEEVNKEMNSLLEDVGLQHK-RFEQ----TKNLSGGmQRK-LSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:COG4615 420 ---------RLLGLDGEADPARARELLERLELDHKvSVEDgrfsTTDLSQG-QRKrLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1072 PYSRRgiW---DLL--LKyREGRTIILSTH---YMDEAdllgDRIAIISQGKL 1116
Cdd:COG4615 490 PEFRR--VfytELLpeLK-ARGKTVIAISHddrYFDLA----DRVLKMDYGKL 535
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1896-2110 |
1.80e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKP--AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT----EMEKVHQL 1969
Cdd:PRK11153 4 LKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQ-FDaiidLLTGR---EHLEFYARLRGVPESYVEKvaqwGVQKL----GLSQYADREAGGYSGGNKRKLSTAIAL 2041
Cdd:PRK11153 84 IGMIFQhFN----LLSSRtvfDNVALPLELAGTPKAEIKA----RVTELlelvGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2042 IGAAPVIFLDEPTTGMDPKAKRflwnCILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSV 2110
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1894-2085 |
2.13e-13 |
|
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: 75.47 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG--DTRitYGEAFLSNQSVLTEME-KVHQLM 1970
Cdd:TIGR02868 335 LELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGllDPL--QGEVTLDGVPVSSLDQdEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCPQ----FDAIIdlltgREHLEFyarlrGVPESYVEKVAqWGVQKLGLSQYADREAGGY-----------SGGNKRKL 2035
Cdd:TIGR02868 412 SVCAQdahlFDTTV-----RENLRL-----ARPDATDEELW-AALERVGLADWLRALPDGLdtvlgeggarlSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2036 STAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVkEGRSVVLTSHS 2085
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1906-2088 |
2.46e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGeaflsnqsvlTEMEKVHQLMGYCPQFDAIIDLL-- 1983
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG----------TVRRAGGARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1984 TGRE--------HLEFYARLRGVPESYVEKVaqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:NF040873 73 TVRDlvamgrwaRRGLWRRLTRDDRAAVDDA----LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|...
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEE 2088
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
934-1096 |
2.88e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDiiRRTLGVCPQ-HNVLFDILTVEEHVWFYGRMKGMS 1012
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYVPQsEEVDWSFPVLVEDVVMMGRYGHMG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1013 LEEVNKE-----MNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYR- 1086
Cdd:PRK15056 111 WLRRAKKrdrqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRd 190
|
170
....*....|
gi 1207110406 1087 EGRTIILSTH 1096
Cdd:PRK15056 191 EGKTMLVSTH 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1918-2172 |
3.09e-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: 73.61 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1918 IPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLsNQSVLTEMEKVHQL------MGYCPQFDAIIDLLTGREHLEf 1991
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL-NGRTLFDSRKGIFLppekrrIGYVFQEARLFPHLSVRGNLR- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1992 YARLRGVPEsyvEKVAQWG--VQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCI 2069
Cdd:TIGR02142 98 YGMKRARPS---ERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2070 LSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNR-------FGD-GYTIILRLstpsAEPCPVDAY 2140
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASpdlpwlaREDqGSLIEGVV----AEHDQHYGL 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 1207110406 2141 IQNAFPGI-----QLKERHQNVLQYQLPSQTCSLARV 2172
Cdd:TIGR02142 251 TALRLGGGhlwvpENLGPTGARLRLRVPARDVSLALQ 287
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
910-1115 |
3.29e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTAGTIYVKGMDI---------RSDMDI 978
Cdd:PRK13549 9 KNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELqasnirdteRAGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 IRRTLGVCPQhnvlfdiLTVEEHVwFYGR--MKG--MSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAF 1054
Cdd:PRK13549 87 IHQELALVKE-------LSVLENI-FLGNeiTPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKyREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1894-2113 |
3.59e-13 |
|
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: 74.79 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEM--EKVHQLMG 1971
Cdd:COG4988 337 IELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSDLdpASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQ----FDAIIdlltgREHLEFYArlrgvPESYVEKVAQWgVQKLGLSQYADREAGGY-----------SGGNKRKLS 2036
Cdd:COG4988 415 WVPQnpylFAGTI-----RENLRLGR-----PDASDEELEAA-LEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2037 TAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSvVKEGRSVVLTSHSMEECeALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1898-2103 |
4.44e-13 |
|
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: 70.51 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1898 DLSKVYKAGrKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL----TEMEKVHQLMGYC 1973
Cdd:cd03292 5 NVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2054 TTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
918-1115 |
4.79e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 918 KGAKLAVnhlnikfYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIR---------SDMDIIRRTLGVCPQ 988
Cdd:PRK10762 21 SGAALNV-------YPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeAGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 hnvlfdiLTVEEHVW----FYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:PRK10762 94 -------LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1894-2099 |
5.12e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 71.43 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGR--KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTemekvhqlmg 1971
Cdd:COG4525 4 LTVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 ycP--------QFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIG 2043
Cdd:COG4525 74 --PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2044 AAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIM 2099
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
886-1121 |
5.24e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 886 PAPREEQDARieaEPTNLILGVSIRNLVKIYKkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTI 965
Cdd:PRK13657 317 PDVRDPPGAI---DLGRVKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 966 YVKGMDIRS-DMDIIRRTLGVCPQHNVLFDiLTVEEHVWFyGRmKGMSLEEVNK--EMNSLLEDVGLQHKRF-----EQT 1037
Cdd:PRK13657 393 LIDGTDIRTvTRASLRRNIAVVFQDAGLFN-RSIEDNIRV-GR-PDATDEEMRAaaERAQAHDFIERKPDGYdtvvgERG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1038 KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRT--II---LSThyMDEAdllgDRIAIIS 1112
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFD 543
|
....*....
gi 1207110406 1113 QGKLCCCGT 1121
Cdd:PRK13657 544 NGRVVESGS 552
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
919-1109 |
5.25e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSI---LTGLFPP--TAGTIYVKGMDIR-SDMDI--IRRTLGVCPQHN 990
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYaPDVDPveVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 991 VLFDiLTVEEHVWFYGRMKGMsleevNKEMNSLLEDVGLQHKRFEQTKN--------LSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:PRK14243 101 NPFP-KSIYDNIAYGARINGY-----KGDMDELVERSLRQAALWDEVKDklkqsglsLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIA 1109
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1904-2121 |
5.93e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1904 KAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-------LTEMEKVHQLMGYcpQF 1976
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaeLREVRRKKIAMVF--QS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1977 DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTG 2056
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2057 MDPKAKRFLWNCILSV-VKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGDGY 2121
Cdd:PRK10070 195 LDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1872-2054 |
6.14e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1872 MEDEDVARERERVK----NGRALGDILI-LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDT- 1945
Cdd:COG0488 289 LEREEPPRRDKTVEirfpPPERLGKKVLeLEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELe 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1946 ----RITYGeaflsnqsvltemEKVHqlMGYCPQFDAIIDL-LTGREHLEfyarlRGVPESYVEKVAQWgVQKLGLS-QY 2019
Cdd:COG0488 367 pdsgTVKLG-------------ETVK--IGYFDQHQEELDPdKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDD 425
|
170 180 190
....*....|....*....|....*....|....*
gi 1207110406 2020 ADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPT 2054
Cdd:COG0488 426 AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
907-1115 |
8.02e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGaKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNV-----LFDILTV-----EEHVWfygrmkgMSLEEVnkEMNSLLEDV--GLQHKRFEQTKNLSGGMQRKLSVAIA 1053
Cdd:PRK10790 420 VQQDPVvladtFLANVTLgrdisEEQVW-------QALETV--QLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMD---EAD--LLGDRIAIISQGK 1115
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEADtiLVLHRGQAVEQGT 557
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1893-2127 |
8.32e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRkpAVNRLCLGIPRGECFGLLGVNGAGKTSTFR----MLTGDTRITYGEAFLSNQ-----SVLTEM 1963
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvqregRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1964 EKVHQLMGYCPQFDAIIDLLTGREHLEFYArLRGVP------ESYVEKVAQWGVQKL---GLSQYADREAGGYSGGNKRK 2034
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTPfwrtcfSWFTREQKQRALQALtrvGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2035 LSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVK-EGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*
gi 1207110406 2114 KN-RFGDGYTIILRL 2127
Cdd:PRK09984 241 DNeRFDHLYRSINRV 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1893-2101 |
9.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.94 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV----LTEMEK--- 1965
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKhig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 ------VHQLMGYCPQFDAIIDLltgREHLefyarlrgVP-ESYVEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTA 2038
Cdd:PRK13648 87 ivfqnpDNQFVGSIVKYDVAFGL---ENHA--------VPyDEMHRRVSE-ALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2039 IALIGAAPVIFLDEPTTGMDPKAKRFLWNCIlSVVKEGRSVVLTSHSMEECEALCTRMAIMVN 2101
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLV-RKVKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
879-1116 |
1.08e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 879 ELGLPIPPAPREEQDARIEAEptnlilGVSIRNlvkiykKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLF 958
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVE------NLSVRD------DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 959 PPTAGTIYVKGMDI--RSDMDIIRRTLGVCPqhnvlfdiltvEEhvwfygRMK-----GMSLEEvnkemNSLLEDVG--- 1028
Cdd:COG3845 309 PPASGSIRLDGEDItgLSPRERRRLGVAYIP-----------ED------RLGrglvpDMSVAE-----NLILGRYRrpp 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1029 ------LQHKRFEQ-------------------TKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLL 1083
Cdd:COG3845 367 fsrggfLDRKAIRAfaeelieefdvrtpgpdtpARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL 446
|
250 260 270
....*....|....*....|....*....|....
gi 1207110406 1084 KYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG3845 447 ELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1916-2088 |
1.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLTG-----DTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQF-DAIIDLLTGREHL 1989
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 EFYARLRGVPESYVEKVAQWGVQKLGLS-QYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNC 2068
Cdd:PRK13643 107 AFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180
....*....|....*....|
gi 1207110406 2069 ILSVVKEGRSVVLTSHSMEE 2088
Cdd:PRK13643 187 FESIHQSGQTVVLVTHLMDD 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1893-2117 |
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 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL---TEMEKVHQL 1969
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MgycpQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:PRK09452 92 F----QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL----KNRF 2117
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1896-2131 |
1.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGrKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLMGYC 1973
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 pqFDAIIDLLTGR---EHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:PRK13644 83 --FQNPETQFVGRtveEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFQCLGSVQhlkNRFGDGYTIILRLSTP 2130
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE---NVLSDVSLQTLGLTPP 236
|
.
gi 1207110406 2131 S 2131
Cdd:PRK13644 237 S 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
924-1117 |
1.30e-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: 72.94 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPT-AGTIYVKG--MDIRSDMDII----------RRTLGVCPQ-- 988
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQAIragiamvpedRKRHGIVPIlg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 989 --HNVLFDILTveehvwfygRMKGMSLEEVNKEMNSLLEDVGLQHKR----FEQTKNLSGGMQRKLSVAIAFIGGSKVVV 1062
Cdd:TIGR02633 356 vgKNITLSVLK---------SFCFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKLC 1117
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1921-2084 |
1.50e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.60 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTR---ITYGEAfLSNQSVLTEmeKVHQLMGYCPQFDAIIDLLTGREHLEFYARLR- 1996
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDR-LVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRq 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1997 --GVPES----YVEKVaqwgVQKLGLSQYADREAG----GYSGGNKRKLSTAIALIgAAP--VIFLDEPTTGMDPKAKRF 2064
Cdd:TIGR00956 866 pkSVSKSekmeYVEEV----IKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELV-AKPklLLFLDEPTSGLDSQTAWS 940
|
170 180
....*....|....*....|
gi 1207110406 2065 LWNCILSVVKEGRSVVLTSH 2084
Cdd:TIGR00956 941 ICKLMRKLADHGQAILCTIH 960
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
905-1116 |
2.54e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 905 LGVSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGM--DIRSDMDI---- 978
Cdd:COG4161 1 MSIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 979 -IRRTLGVCPQHNVLFDILTVEEH-VWFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIG 1056
Cdd:COG4161 79 lLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1057 GSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
908-1115 |
2.84e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDiRSDMDII------RR 981
Cdd:PRK11701 8 SVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaeRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TL-----GVCPQH-------------NVLFDILTV-EEHvwfYGRMKGMSLEevnkemnsLLEDVGLQHKRF-EQTKNLS 1041
Cdd:PRK11701 85 RLlrtewGFVHQHprdglrmqvsaggNIGERLMAVgARH---YGDIRATAGD--------WLERVEIDAARIdDLPTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1042 GGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1896-2118 |
3.01e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAflsnqSVL-TEM------EKVHQ 1968
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLgGDMadarhrRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1969 LMGYCPQfdaiiDL-------LTGREHLEFYARLRGVPESyvEKvaQWGVQKL----GLSQYADREAGGYSGGNKRKLST 2037
Cdd:NF033858 77 RIAYMPQ-----GLgknlyptLSVFENLDFFGRLFGQDAA--ER--RRRIDELlratGLAPFADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2038 AIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE--GRSVVLTSHSMEECEAlCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLA 226
|
...
gi 1207110406 2116 RFG 2118
Cdd:NF033858 227 RTG 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1888-2103 |
3.50e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1888 RALGDILIlsDLSKVYKAGRKPAVNrlcLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL--TEMEK 1965
Cdd:PRK11288 251 RPLGEVRL--RLDGLKGPGLREPIS---FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 VHQLMGYCPQ---FDAIIDLLTGREHLEFYARLRGVPESYV------EKVAQWGVQKLGL-SQYADREAGGYSGGNKRK- 2034
Cdd:PRK11288 326 IRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAGCLinnrweAENADRFIRSLNIkTPSREQLIMNLSGGNQQKa 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2035 -----LSTAIAligaapVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11288 406 ilgrwLSEDMK------VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
907-1115 |
3.59e-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: 65.93 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIyvkgmdirsdmdiirrtlgvc 986
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 pqhnvlfdiltveehvwfygrmkgmsleevnkemnSLLEDVGLQHkrFEQtknLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:cd03221 58 -----------------------------------TWGSTVKIGY--FEQ---LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKYRegRTIILSTHymDEA--DLLGDRIAIISQGK 1115
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
923-1115 |
3.73e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPptAGT----IYVKGM-----DIRSDMD----IIRRTLGVCPQh 989
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSyegeILFDGEvcrfkDIRDSEAlgivIIHQELALIPY- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 990 nvlfdiLTVEEHVwFYG--RMKG--MSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFiggSKVV---V 1062
Cdd:NF040905 93 ------LSIAENI-FLGneRAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL---SKDVkllI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1063 LDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
897-1116 |
4.02e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 897 EAEPTNLIlgvSIRNlvkIYKKGAKLAV-NHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD 975
Cdd:PRK15439 5 DTTAPPLL---CARS---ISKQYSGVEVlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 976 MDIIRRTLGV--CPQHNVLFDILTVEEHVWFygrmkGMSLEEVNKE-MNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAI 1052
Cdd:PRK15439 79 TPAKAHQLGIylVPQEPLLFPNLSVKENILF-----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1053 AFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1908-2119 |
4.43e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.99 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQsVLTE---MEKVHQL-MGY-CP--QF-DAI 1979
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEenvWDIRHKIgMVFqNPdnQFvGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1980 I--DLLTGREHlefyarlRGVP-ESYVEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTG 2056
Cdd:PRK13650 99 VedDVAFGLEN-------KGIPhEEMKERVNE-ALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2057 MDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGRFQCLGSVQHLKNRFGD 2119
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1894-2113 |
5.32e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.01 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKvhqlmgyc 1973
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA-------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 pQFDAIIDLLTGREHLeFYARLR-----GVPESYVEKVAQwGVQKLGLSQYADREA--------GG--YSGGNKRKLSTA 2038
Cdd:PRK11160 411 -ALRQAISVVSQRVHL-FSATLRdnlllAAPNASDEALIE-VLQQVGLEKLLEDDKglnawlgeGGrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2039 IALIGAAPVIFLDEPTTGMDPKAKRFlwncILSVVKE---GRSVVLTSH---SMEECEALCtrmaIMVNGRFQCLGSVQH 2112
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQ----ILELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQE 559
|
.
gi 1207110406 2113 L 2113
Cdd:PRK11160 560 L 560
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1894-2103 |
5.39e-12 |
|
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: 66.47 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-LTEMEKVHQLMGY 1972
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQFDaiiDLLTGrehlefyarlrgvpeSYVEKVaqwgvqklglsqyadreaggYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:cd03246 81 LPQDD---ELFSG---------------SIAENI--------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2103
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
901-1109 |
7.18e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 901 TNLILGVSIRNLVKIYKkgAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLfPPTAGTIYVKG---------MD 971
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqniYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 972 IRSDMDIIRRTLG-VCPQHNvLFDiLTVEEHVWFYGRMKGMSLE-EVNKEMNSLLEDVGL----QHKRFEQTKNLSGGMQ 1045
Cdd:PRK14258 79 RRVNLNRLRRQVSmVHPKPN-LFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1046 RKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIA 1109
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1910-2103 |
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 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG-------DTRITYGEAFLSNQSVLTEMEK----VHQLMGYCPQFDA 1978
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYWSGSPLKASNIRDTERAgiviIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1979 IIDLLTGREhlefyARLRGVPESYVEKV--AQWGVQKLGLSQYAD-REAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:TIGR02633 96 AENIFLGNE-----ITLPGGRMAYNAMYlrAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1997-2087 |
8.22e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1997 GVPESYVEKVAQWGVQKLGL-SQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE 2075
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90
....*....|..
gi 1207110406 2076 GRSVVLTSHSME 2087
Cdd:PRK13631 226 NKTVFVITHTME 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1887-2083 |
1.03e-11 |
|
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: 66.13 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1887 GRALGDILILSDLSKVYKAGRKpavnRLCLGIPRGECFGLLGVnGAGKTSTFRMLTGDtrITYGeaflsNQSVLTEMEKV 1966
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEM----VLVLGRPGSGCSTLLKA-LANRTEGNVSVEGD--IHYN-----GIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 HQLMGYCPQFDAIIDLLTGREHLEFYARLRGvpesyvekvaqwgvqklglsqyaDREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207110406 2047 VIFLDEPTTGMDPK-AKRFLwNCILSVVKEGRSVVLTS 2083
Cdd:cd03233 139 VLCWDNSTRGLDSStALEIL-KCIRTMADVLKTTTFVS 175
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
907-1071 |
1.04e-11 |
|
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: 66.13 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLA--VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTA---GTIYVKGMDIRSDMDIIRR 981
Cdd:cd03233 4 LSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLGVCPQHNVLFDILTVEEHVWFYGRMKGmsleevnkemNSLLedvglqhkrfeqtKNLSGGMQRKLSVAIAFIGGSKVV 1061
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCKG----------NEFV-------------RGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 1207110406 1062 VLDEPTAGVD 1071
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1876-2103 |
1.08e-11 |
|
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: 70.25 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1876 DVARERERVKNGRALGDIlILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLS 1955
Cdd:COG2274 457 EREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1956 NQSvLTEMEK--VHQLMGYCPQfDaiIDLLTG--REHLEFYARlrGVPESYVEKVAQwgvqKLGLSQYADREAGGY---- 2027
Cdd:COG2274 536 GID-LRQIDPasLRRQIGVVLQ-D--VFLFSGtiRENITLGDP--DATDEEIIEAAR----LAGLHDFIEALPMGYdtvv 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2028 -------SGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKeGRSVVLTSHSMeECEALCTRMAIMV 2100
Cdd:COG2274 606 geggsnlSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLD 683
|
...
gi 1207110406 2101 NGR 2103
Cdd:COG2274 684 KGR 686
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1893-2104 |
1.25e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKtSTF-RMLTGDTRITYGEAFLSNQSVL----TEMEK-- 1965
Cdd:COG1129 4 LLEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVRfrspRDAQAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 ---VHQLMGYCPQFDAIIDLLTGREhlefYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALI 2042
Cdd:COG1129 81 iaiIHQELNLVPNLSVAENIFLGRE----PRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2043 GAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
924-1120 |
1.26e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.03 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TAGTIYVKGMDIrSDMDIIRRTLGVCPQH--NVLFDILT 997
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV-APCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHVWFYGRMKGmsLEEVNKEMNSLLEDVGLQHKR-------FEqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGV 1070
Cdd:PRK10418 98 MHTHARETCLALG--KPADDATLTAALEAVGLENAArvlklypFE----MSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1071 DPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCG 1120
Cdd:PRK10418 172 DVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
924-1116 |
1.40e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI--RSDMDIIRRTLGVCPQH---NVLFDILTV 998
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 999 EEHVWFY-----GRMKG-MSLEEVNKEM---NSLLEDVGLQHKRFEQTKN-LSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:PRK09700 359 AQNMAISrslkdGGYKGaMGLFHEVDEQrtaENQRELLALKCHSVNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1069 GVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
907-1115 |
1.81e-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: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTAGTIYVKGMDI---------RSD 975
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkasnirdteRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 976 MDIIRRTLGVCPQHNVLFDILTVEEHVWFYGRmkgMSLEEVNKEMNSLLEDVGLQHKRFEQ-TKNLSGGMQRKLSVAIAF 1054
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKyREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1893-2087 |
2.89e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKagRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAF-------LSNQSVLTEMEK 1965
Cdd:PRK13638 1 MLATSDLWFRYQ--DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 VHQLMGYCPQ--FDAIIDlltgrEHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIG 2043
Cdd:PRK13638 79 VATVFQDPEQqiFYTDID-----SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 2044 AAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSME 2087
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1906-2103 |
2.89e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQL-----MGYcPQFDaII 1980
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeagMVF-QQFY-LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1981 DLLTGREHLEFYA-RLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP 2059
Cdd:PRK09493 90 PHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 2060 KAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
923-1115 |
4.11e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrsDMDIIRRTL--GVCPQHNVLFDIL--TV 998
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEALenGISMVHQELNLVLqrSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 999 EEHVWFyGR--MKGMSLEE--VNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYS 1074
Cdd:PRK10982 91 MDNMWL-GRypTKGMFVDQdkMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 1075 RRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK10982 170 VNHLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1864-2084 |
4.38e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 68.72 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1864 GFVLP--PLGMEDEDVA----RERERVKNGRALGDILILSDLSKVYKAGRKPAvnrlclgiprgecfgLLGVNGAGKTST 1937
Cdd:PLN03140 858 GMVLPftPLAMSFDDVNyfvdMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTA---------------LMGVSGAGKTTL 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1938 FRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPE-------SYVEKVAQWg 2010
Cdd:PLN03140 923 MDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEvskeekmMFVDEVMEL- 1001
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2011 vqkLGLSQYADREAG-----GYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:PLN03140 1002 ---VELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1893-2103 |
4.53e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGR---KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEME----- 1964
Cdd:COG1101 1 MLELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1965 ---KVHQ--LMGYCPQfdaiidlLTGREHLEFyARLRGVP------------ESYVEKVAQWGvqkLGLSQYADREAGGY 2027
Cdd:COG1101 81 yigRVFQdpMMGTAPS-------MTIEENLAL-AYRRGKRrglrrgltkkrrELFRELLATLG---LGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2028 SGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFlwncILS----VVKEGRsvvLTS----HSMEECEALCTRMAIM 2099
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAAL----VLEltekIVEENN---LTTlmvtHNMEQALDYGNRLIMM 222
|
....
gi 1207110406 2100 VNGR 2103
Cdd:COG1101 223 HEGR 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
907-1116 |
4.55e-11 |
|
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: 68.24 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDIlTVEEHVwfyGRMKGMSLEEVNK--------EMNSLLED-----VGlqhkrfEQTKNLSGG-MQRkLSVA 1051
Cdd:COG4618 411 LPQDVELFDG-TIAENI---ARFGDADPEKVVAaaklagvhEMILRLPDgydtrIG------EGGARLSGGqRQR-IGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1052 IAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMdeaDLLG--DRIAIISQGKL 1116
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1894-2111 |
4.56e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.56 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSkvYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV----LTEMEKVHQL 1969
Cdd:PRK13548 3 LEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MgycPQ-----FD----AIIDLltGRE-HLEFYARLRGVPESYVEKVaqwgvqklGLSQYADREAGGYSGGNKRKLSTAI 2039
Cdd:PRK13548 81 L---PQhsslsFPftveEVVAM--GRApHGLSRAEDDALVAAALAQV--------DLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2040 ALI------GAAPVIFLDEPTTGMDPK--------AKRFLWNCILSVVkegrsVVLtsHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAhqhhvlrlARQLAHERGLAVI-----VVL--HDLNLAARYADRIVLLHQGRLV 220
|
....*.
gi 1207110406 2106 CLGSVQ 2111
Cdd:PRK13548 221 ADGTPA 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1893-2116 |
4.65e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK-VHQLMG 1971
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQF-DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:PRK13647 83 LVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNR 2116
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1896-2103 |
4.76e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 66.64 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKP--AVNRLCLGIPRGECFGLLGVNGAGKtSTF-RMLTGDTRITYGEAFLSNQSV--LTEME--KVHQ 1968
Cdd:COG1135 4 LENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGVDLtaLSERElrAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1969 LMGYCPQ-FDaiidLLTGR---EHLEFYARLRGVPESYVEKVaqwgVQKL----GLSQYADReaggY----SGGNKRKLS 2036
Cdd:COG1135 83 KIGMIFQhFN----LLSSRtvaENVALPLEIAGVPKAEIRKR----VAELlelvGLSDKADA----YpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2037 TAIALIGAAPVIFLDEPTTGMDPKAKRflwnCILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTR----SILDLLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1896-2115 |
5.57e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.40 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKtSTF-RMLTGDTRITYGEAFLS----NQSVLTEMEKVHQLM 1970
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDgitiSKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1971 GYCP--QFDAIidllTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:PRK13632 89 FQNPdnQFIGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
923-1116 |
5.84e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.22 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirsDMDIIRRTLGVCPQhnvlfdiLTVEEHV 1002
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 WFYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL 1082
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1207110406 1083 LKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK13546 187 YEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
904-1144 |
6.04e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.82 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 904 ILGVSIRNLvkIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGM---DIRsdMDIIR 980
Cdd:PRK10789 313 ELDVNIRQF--TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltKLQ--LDSWR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGVCPQHNVLFDIlTVEEHVWFyGRMKGMS--LEEVNKeMNSLLEDV-----GLQHKRFEQTKNLSGGMQRKLSVAIA 1053
Cdd:PRK10789 389 SRLAVVSQTPFLFSD-TVANNIAL-GRPDATQqeIEHVAR-LASVHDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMD---EAdllgDRIAIISQGKLCCCGTPLFLKARlg 1130
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSaltEA----SEILVMQHGHIAQRGNHDQLAQQ-- 539
|
250
....*....|....
gi 1207110406 1131 TGYYltlvkREMHR 1144
Cdd:PRK10789 540 SGWY-----RDMYR 548
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
927-1138 |
6.84e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.83 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDiLTVEEHVwFY 1005
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFS-GSVRENI-AY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1006 GRMKGMSLEEVNKEMNSLLEDV------GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIW 1079
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFimefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1080 DllLKYREGRTIILSTHYMDEADlLGDRIAIISQGKLCCCGTPLFLKARlgTGYYLTLV 1138
Cdd:TIGR00958 658 E--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1916-2102 |
7.94e-11 |
|
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: 64.41 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEM--EKVHQLMGYcpqfdAIIDLLTGREH--LEF 1991
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPgpDRMVVFQNY-----SLLPWLTVRENiaLAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1992 YARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILS 2071
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 1207110406 2072 VVKEGR-SVVLTSHSMEECEALCTRMAIMVNG 2102
Cdd:TIGR01184 160 IWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1908-2084 |
8.83e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGRE 1987
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1988 H----LEFYARLRGVPESyvekvaqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKR 2063
Cdd:PRK13540 94 NclydIHFSPGAVGITEL---------CRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|.
gi 1207110406 2064 FLWNCILSVVKEGRSVVLTSH 2084
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
927-1125 |
1.01e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDILTVEEHV--- 1002
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 ---WF--YGRMKGMSLEEVnKEMNSLledVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRG 1077
Cdd:PRK10575 110 rypWHgaLGRFGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1078 IWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPLFL 1125
Cdd:PRK10575 186 VLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
907-1116 |
1.24e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG--MDIRSDMDI-----I 979
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkaireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 RRTLGVCPQHNVLFDILTVEEH-VWFYGRMKGMSLEEVNKEMNSLLEDVGLQHK--RFEQtkNLSGGMQRKLSVAIAFIG 1056
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYadRFPL--HLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1057 GSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
907-1133 |
1.27e-10 |
|
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: 67.28 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTttmSILTGLF---PPTAGTIYVKGMDI-RSDMDIIRRT 982
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 983 LGVCPQHNVLF--------DILT--VEEHVWfygrmkgMSLEEVN-KEMNSLLEDvGLQHKRFEQTKNLSGGMQRKLSVA 1051
Cdd:TIGR00957 1362 ITIIPQDPVLFsgslrmnlDPFSqySDEEVW-------WALELAHlKTFVSALPD-KLDHECAEGGENLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1052 IAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTH----YMDEAdllgdRIAIISQGKLCCCGTPLFLKA 1127
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHrlntIMDYT-----RVIVLDKGEVAEFGAPSNLLQ 1508
|
....*.
gi 1207110406 1128 RLGTGY 1133
Cdd:TIGR00957 1509 QRGIFY 1514
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
919-1116 |
2.06e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.96 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY-----VKGMDIRSDMDII--RRTLGVCPQHNV 991
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRDVLefRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 992 LFDILTVEEHVWFYGRMKGMSLEEVNKEMNSLLEDVGL----QHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPT 1067
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1068 AGVDPYSRRGIWDLLLKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
880-1116 |
2.38e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 880 LGLPIPPAPREEQDArieaePTNLILGVSIRNLVkIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGlFP 959
Cdd:PRK11174 328 LETPLAHPQQGEKEL-----ASNDPVTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 960 PTAGTIYVKGMDIRS-DMDIIRRTL---GVCPQ-------HNVLF-DILTVEEHVWfygrmkgMSLEEVN-KEMNSLLED 1026
Cdd:PRK11174 401 PYQGSLKINGIELRElDPESWRKHLswvGQNPQlphgtlrDNVLLgNPDASDEQLQ-------QALENAWvSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1027 vGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDeaDLLG- 1105
Cdd:PRK11174 474 -GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQw 550
|
250
....*....|.
gi 1207110406 1106 DRIAIISQGKL 1116
Cdd:PRK11174 551 DQIWVMQDGQI 561
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
926-1116 |
2.52e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 926 HLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVC------PQHNVLFDI---- 995
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 996 ----LTVEEHVWFYGRMKGMS-LEEVNKEMNSLLEDVglqhkrfEQT-KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAG 1069
Cdd:PRK15439 361 nvcaLTHNRRGFWIKPARENAvLERYRRALNIKFNHA-------EQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 1070 VDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK15439 434 VDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
900-1116 |
2.65e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 900 PTNLILG--VSIRNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGM---DIRS 974
Cdd:PRK11247 4 TARLNQGtpLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 975 DMDIIRRTLGVCPQHNVLFDI---LTveehvwfyGRMKGMSLEEvnkemnslLEDVGLQHKRFEQTKNLSGGMQRKLSVA 1051
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVglgLK--------GQWRDAALQA--------LAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1052 IAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1916-2105 |
2.74e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEM--EKVHQL----MGYCPQFDAIIDLLTGREHL 1989
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMdeEARAKLrakhVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 EFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCI 2069
Cdd:PRK10584 110 ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207110406 2070 LSVVKE-GRSVVLTSHSmEECEALCTRMAIMVNGRFQ 2105
Cdd:PRK10584 190 FSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
934-1096 |
2.76e-10 |
|
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: 61.88 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSIL-----TGLfppTAGTIYVKGMDIRSDmdiIRRTLGVCPQHNVLFDILTVEEHVWFYGRM 1008
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1009 KGMSLEEvnkemnslledvglqhkrfeqtknlsggmQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-RE 1087
Cdd:cd03232 107 RGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDS 157
|
....*....
gi 1207110406 1088 GRTIILSTH 1096
Cdd:cd03232 158 GQAILCTIH 166
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1894-2087 |
3.11e-10 |
|
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: 65.39 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKV-HQLMGY 1972
Cdd:TIGR02857 322 LEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQ----FDAIIdlltgREHLEFYARlrGVPESYVEKVAQW-GVQKL--GLSQYADREAG----GYSGGNKRKLSTAIAL 2041
Cdd:TIGR02857 401 VPQhpflFAGTI-----AENIRLARP--DASDAEIREALERaGLDEFvaALPQGLDTPIGeggaGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207110406 2042 IGAAPVIFLDEPTTGMDPKAKRFLwNCILSVVKEGRSVVLTSHSME 2087
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLA 518
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
887-1116 |
3.12e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 887 APREEQDARIEAEptnlilGVSIRNLvkiyKKGAKLAVNhlnikfyEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY 966
Cdd:PRK11288 249 RPRPLGEVRLRLD------GLKGPGL----REPISFSVR-------AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 967 VKG--MDIRSDMDIIRRTLGVCPQ---HNVLFDILTVEEHVWFYGRMK----GMSLEEVNKEMNSLLEDVGLQHK---RF 1034
Cdd:PRK11288 312 LDGkpIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARRHhlraGCLINNRWEAENADRFIRSLNIKtpsRE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1035 EQTKNLSGGMQRKlsvaiAFIG-----GSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTHymDEADLLG--D 1106
Cdd:PRK11288 392 QLIMNLSGGNQQK-----AILGrwlseDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSS--DLPEVLGvaD 464
|
250
....*....|
gi 1207110406 1107 RIAIISQGKL 1116
Cdd:PRK11288 465 RIVVMREGRI 474
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
921-1096 |
3.29e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 921 KLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEE 1000
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HVWFygrmkGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWD 1080
Cdd:PRK13540 94 NCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*..
gi 1207110406 1081 LLLKYR-EGRTIILSTH 1096
Cdd:PRK13540 169 KIQEHRaKGGAVLLTSH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1893-2122 |
4.26e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.79 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL---TEMEKVHQL 1969
Cdd:PRK11248 1 MLQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQFDAIidlltgrEHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:PRK11248 79 EGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2050 LDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQClgsVQHLKNRFGDGYT 2122
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
927-1122 |
4.42e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFpPTAGTIYVKGMDIR----SDMDIIRRTLgvCPQHNVLFDIltveeHV 1002
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaAELARHRAYL--SQQQTPPFAM-----PV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 WFYGRM---KGMSLEEVNKEMNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIG-------GSKVVVLDEPTAGVDp 1072
Cdd:PRK03695 87 FQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1073 YSRRGIWDLLLKY--REGRTIILSTHymdeaDL-----LGDRIAIISQGKLCCCGTP 1122
Cdd:PRK03695 166 VAQQAALDRLLSElcQQGIAVVMSSH-----DLnhtlrHADRVWLLKQGKLLASGRR 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
919-1122 |
5.95e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIyvkgmdIRSDmdiiRRTLGVCPQhNVLFDI--- 995
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNG----KLRIGYVPQ-KLYLDTtlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 996 LTVEehvwfygrmKGMSLEEVNKEMNSL--LEDVGLQHKRFEQTKNLSGG-MQRKLsVAIAFIGGSKVVVLDEPTAGVDP 1072
Cdd:PRK09544 84 LTVN---------RFLRLRPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1073 YSRRGIWDLLLKYRE--GRTIILSTHYMDEADLLGDRIAIISQgKLCCCGTP 1122
Cdd:PRK09544 154 NGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1893-2103 |
8.20e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEK---VHQL 1969
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQFDAIIDLLTGREHLE---FYARlrgvPESYVEKVAQwgVQKL--GLSQYADREAGGYSGGNKRKLSTAIALIGA 2044
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggFFAE----RDQFQERIKW--VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2045 APVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1875-2108 |
8.47e-10 |
|
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: 64.00 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1875 EDVARERERVKNGRALGDiLILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFL 1954
Cdd:COG4618 313 AAVPAEPERMPLPRPKGR-LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1955 SNQSVLT-EMEKVHQLMGYCPQfDaiIDLLTG--REHLefyARLRGVPESYVEKVAQW-GVQK--LGLSQ-YADR-EAGG 2026
Cdd:COG4618 392 DGADLSQwDREELGRHIGYLPQ-D--VELFDGtiAENI---ARFGDADPEKVVAAAKLaGVHEmiLRLPDgYDTRiGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2027 Y--SGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMeecEAL--CTRMAIMVNG 2102
Cdd:COG4618 466 ArlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDG 542
|
....*.
gi 1207110406 2103 RFQCLG 2108
Cdd:COG4618 543 RVQAFG 548
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1921-2130 |
9.29e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDT---------RITYgeaflsNQSVLTEMEKvhQLMG---YCPQFDAIIDLLTGREH 1988
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTdgfhigvegVITY------DGITPEEIKK--HYRGdvvYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1989 LEFYARLRGVP--------ESYVEKVAQWGVQKLGLSQYADREAG-----GYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:TIGR00956 159 LDFAARCKTPQnrpdgvsrEEYAKHIADVYMATYGLSHTRNTKVGndfvrGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKEGRSVVLTS--HSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGD-GYTIILRLSTP 2130
Cdd:TIGR00956 239 GLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKmGFKCPDRQTTA 316
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1907-2103 |
9.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.03 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1907 RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTE--MEKVHQLMGYC---P--QFDAI 1979
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenLWDIRNKAGMVfqnPdnQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1980 I---DLLTGREHLefyarlrGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTG 2056
Cdd:PRK13633 102 IveeDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 2057 MDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGR 2103
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1893-2103 |
1.01e-09 |
|
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: 62.38 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKP--AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG---DTRITYGEAFLSNQSVLT----EM 1963
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1964 EKV-HQLMGYCPQfdaiiD-------LLTGREHL-EFYARLRGVPESYVEKVAQWGVQKLGLSQYADReAGGY----SGG 2030
Cdd:COG0444 81 RKIrGREIQMIFQ-----DpmtslnpVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPERR-LDRYphelSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2031 NKRKLSTAIALIGAAPVIFLDEPTTGMDP--KAKrflwncILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVtiQAQ------ILNLLKDlqrelGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1916-2115 |
1.15e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRML-------TGDTRITyGEAF-LSNQSVLTEMEKVHQLMGYCPQFDAIIDLLTGRE 1987
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIA-GNHFdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTVQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1988 HL-EFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKakrfLW 2066
Cdd:PRK11124 102 NLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----IT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2067 NCILSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:PRK11124 178 AQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1913-2103 |
1.19e-09 |
|
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: 60.58 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1913 RLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYCPQFDAIIDLLTGREHLEF- 1991
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1992 ---YARLRGVPESYVEKVAQwgvqKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNC 2068
Cdd:cd03298 95 lspGLKLTAEDRQAIEVALA----RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207110406 2069 ILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
884-1109 |
1.20e-09 |
|
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: 63.42 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 884 IPPAPREeQDARIEAEptnlilgvsirNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAG 963
Cdd:TIGR03719 312 IPPGPRL-GDKVIEAE-----------NLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 964 TI---------YVKGMdiRSDMDiirrtlgvcPQHNVL------FDILTVEehvwfygrmkgmsleevNKEMNSLLEdVG 1028
Cdd:TIGR03719 378 TIeigetvklaYVDQS--RDALD---------PNKTVWeeisggLDIIKLG-----------------KREIPSRAY-VG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1029 L-------QHKRfeqTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYrEGRTIILStHymDEA 1101
Cdd:TIGR03719 429 RfnfkgsdQQKK---VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRW 501
|
....*...
gi 1207110406 1102 DLlgDRIA 1109
Cdd:TIGR03719 502 FL--DRIA 507
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
940-1116 |
1.26e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.75 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 940 LGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSdMDIIRRTLGVCPQHNVLFDILTVEEHVWFyGRMKGMSLEEVNKE 1019
Cdd:PRK10771 31 LGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRPVSMLFQENNLFSHLTVAQNIGL-GLNPGLKLNAAQRE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1020 -MNSLLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGR--TIILSTH 1096
Cdd:PRK10771 109 kLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSH 188
|
170 180
....*....|....*....|
gi 1207110406 1097 YMDEADLLGDRIAIISQGKL 1116
Cdd:PRK10771 189 SLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1891-2109 |
1.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1891 GDIlILSDLSKVYkAGRKP----AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKV 1966
Cdd:PRK13645 5 KDI-ILDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 HQL------MGYCPQF-------DAI-IDLLTGREHL-----EFYARlrgVPEsyVEKVAQWGvqklglSQYADREAGGY 2027
Cdd:PRK13645 83 KEVkrlrkeIGLVFQFpeyqlfqETIeKDIAFGPVNLgenkqEAYKK---VPE--LLKLVQLP------EDYVKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2028 SGGNKRKLSTA--IALIGAAPVifLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:PRK13645 152 SGGQKRRVALAgiIAMDGNTLV--LDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
....*
gi 1207110406 2105 QCLGS 2109
Cdd:PRK13645 230 ISIGS 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1921-2104 |
1.97e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMEKVHQLMGYCPQ--------FDA-----IIDLLTG 1985
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnVCALTHN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1986 RehLEFY---ARLRGVPESYVekvaqwgvQKLGLS-QYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKA 2061
Cdd:PRK15439 369 R--RGFWikpARENAVLERYR--------RALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207110406 2062 KRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
925-1114 |
2.09e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 925 NHLNIKFYEGQITSFLGHNGAGKTTTMSILTG--LFPPTAGTIYVKGMDIRSDMDIIrrtlgvcpqhnvlfdiltveEHV 1002
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI--------------------DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 WFYGRMKgMSLEEVNkemNSLLEDVGLQHKRFeqtKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDP-YSRRG--IW 1079
Cdd:COG2401 107 GRKGDFK-DAVELLN---AVGLSDAVLWLRRF---KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRVarNL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207110406 1080 DLLLKyREGRTIILSTHYMD-EADLLGDRIAIISQG 1114
Cdd:COG2401 180 QKLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
883-1116 |
2.42e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 883 PIPPAPREEQDARIEAEPtnlILGVsiRNLVKIYKKGAKL---------AVNHLNIKFYEGQITSFLGHNGAGKTTTMSI 953
Cdd:PRK10261 295 PAKQEPPIEQDTVVDGEP---ILQV--RNLVTRFPLRSGLlnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 954 LTGLFPPTAGTIYVKGMDIR----SDMDIIRRTL---------GVCPQHNVLFDILtveEHVWFYGRMKGmslEEVNKEM 1020
Cdd:PRK10261 370 LLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIqfifqdpyaSLDPRQTVGDSIM---EPLRVHGLLPG---KAAAARV 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1021 NSLLEDVGLQHKR-FEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYRE--GRTIILSTHY 1097
Cdd:PRK10261 444 AWLLERVGLLPEHaWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHD 523
|
250
....*....|....*....
gi 1207110406 1098 MDEADLLGDRIAIISQGKL 1116
Cdd:PRK10261 524 MAVVERISHRVAVMYLGQI 542
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1893-2103 |
2.63e-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: 59.76 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYK----AGRK-PAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK-- 1965
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 ---VHQL----MGYCPQFdaiidlltgrehlefyarLRGVPE-SYVEKVAQ----WGVQKlglsQYADREAGG------- 2026
Cdd:COG4778 84 preILALrrrtIGYVSQF------------------LRVIPRvSALDVVAEplleRGVDR----EEARARAREllarlnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2027 -----------YSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTR 2095
Cdd:COG4778 142 perlwdlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
....*...
gi 1207110406 2096 MAIMVNGR 2103
Cdd:COG4778 222 VVDVTPFS 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
907-1122 |
2.86e-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: 59.35 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDiLTVEEHVWFYGRmkgMSLEEVnkeMNSLledvglqhKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:cd03369 87 IPQDPTLFS-GTIRSNLDPFDE---YSDEEI---YGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDE-ADLlgDRIAIISQGKLCCCGTP 1122
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
924-1116 |
2.95e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTAGTIYVKG--MDIRSDMDII----------RRTLGVCPQHN 990
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAIaqgiamvpedRKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 991 VLFDI-LTVeehvwfYGRMKGMSLEEVNKEMNSLLEDVGLQHKR----FEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:PRK13549 358 VGKNItLAA------LDRFTGGSRIDDAAELKTILESIQRLKVKtaspELAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
934-1095 |
2.98e-09 |
|
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: 62.14 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLF-DilTVEEHVWfYGRmKGM 1011
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGR-PDA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1012 SLEEVNK--EMNSL------LED-----VGlqhkrfEQTKNLSGG-MQRklsVAIA--FIGGSKVVVLDEPTAGVDPYSR 1075
Cdd:COG5265 460 SEEEVEAaaRAAQIhdfiesLPDgydtrVG------ERGLKLSGGeKQR---VAIArtLLKNPPILIFDEATSALDSRTE 530
|
170 180
....*....|....*....|....*
gi 1207110406 1076 RGIWDLLLKYREGRT--II---LST 1095
Cdd:COG5265 531 RAIQAALREVARGRTtlVIahrLST 555
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1916-2084 |
3.31e-09 |
|
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: 60.07 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPR-GECFGLLGVNGAGKTSTFRMLTGdtritygeaflsnqsvltemEKVHQLMGYC--PQFDAIIDLLTGREHLEFY 1992
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAG--------------------KLKPNLGKFDdpPDWDEILDEFRGSELQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1993 ARLRG------VPESYV---------------EKVAQWG-----VQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:cd03236 80 TKLLEgdvkviVKPQYVdlipkavkgkvgellKKKDERGkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1896-2103 |
4.06e-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: 59.08 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQL---MGY 1972
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQfdaiidlltgreHLEFYARL-------------RGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAI 2039
Cdd:cd03262 81 VFQ------------QFNLFPHLtvlenitlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2040 ALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1894-2084 |
4.47e-09 |
|
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: 57.07 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEaflsnqsvLTEMEKVHqlMGYC 1973
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--------VTWGSTVK--IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFdaiidlltgrehlefyarlrgvpesyvekvaqwgvqklglsqyadreaggySGGNKRKLSTAIALIGAAPVIFLDEP 2053
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 1207110406 2054 TTGMDPKAKRFLWNCILsvvKEGRSVVLTSH 2084
Cdd:cd03221 98 TNHLDLESIEALEEALK---EYPGTVILVSH 125
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
907-1071 |
4.64e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKL---------AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----- 972
Cdd:COG4608 8 LEVRDLKKHFPVRGGLfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 973 ------RSDMDII----------RRTLGvcpqhnvlfDILtvEEHVWFYGRMKGmslEEVNKEMNSLLEDVGL--QHK-R 1033
Cdd:COG4608 88 relrplRRRMQMVfqdpyaslnpRMTVG---------DII--AEPLRIHGLASK---AERRERVAELLELVGLrpEHAdR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207110406 1034 F--EqtknLSGGmQR-KLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:COG4608 154 YphE----FSGG-QRqRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1921-2096 |
4.83e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHqlMGYCPQFDAIIDLLTGREHLEFYARLRGvpe 2000
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF--MAYLGHLPGLKADLSTLENLHFLCGLHG--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2001 SYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVV 2080
Cdd:PRK13543 112 RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAAL 191
|
170
....*....|....*.
gi 1207110406 2081 LTSHSMEECEALCTRM 2096
Cdd:PRK13543 192 VTTHGAYAAPPVRTRM 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1911-2105 |
5.03e-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: 61.38 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1911 VNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITY-GEAFLSNQSVLTE--MEKVHQLMGYCPQ---FDAII-DLL 1983
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRnpAQAIRAGIAMVPEdrkRHGIVpILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1984 TGRE----HLEFYARLRGVPESYVEKVAQWGVQKLGLSQYA-DREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMD 2058
Cdd:TIGR02633 356 VGKNitlsVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207110406 2059 PKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
910-1104 |
5.68e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNL---VKIyKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSIL-----TGLFppTAGTIYVKGMDIRSDMdiiRR 981
Cdd:TIGR00956 763 RNLtyeVKI-KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSF---QR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 982 TLGVCPQHNVLFDILTVEEHVWFYGRM---KGMSLEEVNK---------EMNSLLEDV------GLQhkrFEQTKnlsgg 1043
Cdd:TIGR00956 837 SIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEyveevikllEMESYADAVvgvpgeGLN---VEQRK----- 908
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1044 mqrKLSVAIAFIGGSKVVV-LDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILSTH-----YMDEADLL 1104
Cdd:TIGR00956 909 ---RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHqpsaiLFEEFDRL 973
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1911-2103 |
5.90e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1911 VNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQ--SVLTEMEKVHQLMGYC----------PQFD- 1977
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdiSPRSPLDAVKKGMAYItesrrdngffPNFSi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1978 ----AIIDLLTGrehlefyARLRG----VPESYVEKVAQWGVQKLGLSQYA-DREAGGYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:PRK09700 359 aqnmAISRSLKD-------GGYKGamglFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
907-1130 |
6.14e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDIlTVEEHVwFYGRMKGMSLEEVNK--EMNSLLE-----DVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGS 1058
Cdd:PRK11176 422 VSQNVHLFND-TIANNI-AYARTEQYSREQIEEaaRMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1059 KVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTII-----LSThyMDEAdllgDRIAIISQGKLCCCGTPLFLKARLG 1130
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLviahrLST--IEKA----DEILVVEDGEIVERGTHAELLAQNG 570
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1896-2103 |
6.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYKAG---RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG-----DTRITYGEAFLSNQSVLTEMEKVH 1967
Cdd:PRK13649 5 LQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlhvptQGSVRVDDTLITSTSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 QLMGYCPQF-DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQ-YADREAGGYSGGNKRKLSTAIALIGAA 2045
Cdd:PRK13649 85 KKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2046 PVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
916-1148 |
6.39e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI-RSDMDIIRRTLGVCPQHNVLFD 994
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 995 iLTVEEHVWFYGRMKGMSLEEVNKEMNslLEDV------GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:PLN03232 1324 -GTVRFNIDPFSEHNDADLWEALERAH--IKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1069 GVDPYSRRGIWDLLLKYREGRTIILSTHYMDEAdLLGDRIAIISQGKLCCCGTPLFLKARLGTGYYltlvkREMHRT-PS 1147
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF-----RMVHSTgPA 1474
|
.
gi 1207110406 1148 N 1148
Cdd:PLN03232 1475 N 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
918-1114 |
9.82e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 918 KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVkgmdirsdmdiIRRTLGVCPQHNVLFDIlT 997
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHVWF--------YGRmkGMSLEEVNKEMNSL----LEDVGlqhkrfEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDE 1065
Cdd:PLN03232 695 VRENILFgsdfeserYWR--AIDVTALQHDLDLLpgrdLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1066 PTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLgDRIAIISQG 1114
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1921-2084 |
9.91e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGdtRItYGEAF----LSNQSVLTEmeKVHQLMGYCPQFDAIIDLLTGREHLEFYARLR 1996
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG--RI-QGNNFtgtiLANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1997 gVPESYVEK----VAQWGVQKLGLSQYADREAG-----GYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWN 2067
Cdd:PLN03211 169 -LPKSLTKQekilVAESVISELGLTKCENTIIGnsfirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*..
gi 1207110406 2068 CILSVVKEGRSVVLTSH 2084
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMH 264
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1892-2113 |
1.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1892 DIlILSDLSKVYKAG---RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG-----DTRITYGEAFLSNQSVLTEM 1963
Cdd:PRK13634 2 DI-TFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1964 EKVHQLMGYCPQFDaiidlltgrEHLEFYARLR----------GVPESYVEKVAQWGVQKLGLSQ-YADREAGGYSGGNK 2032
Cdd:PRK13634 81 KPLRKKVGIVFQFP---------EHQLFEETVEkdicfgpmnfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2033 RKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQ 2111
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
..
gi 1207110406 2112 HL 2113
Cdd:PRK13634 232 EI 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
908-1116 |
1.08e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIY-------KKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDI----RSDM 976
Cdd:PRK10419 5 NVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DIIRRTL---------GVCPQHNVLFDILTVEEHvwfygrMKGMSLEEVNKEMNSLLEDVGLQ----HKRFEQtknLSGG 1043
Cdd:PRK10419 85 KAFRRDIqmvfqdsisAVNPRKTVREIIREPLRH------LLSLDKAERLARASEMLRAVDLDdsvlDKRPPQ---LSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1044 MQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
919-1114 |
1.14e-08 |
|
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: 57.83 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHlNIKF--YEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDM------DII---RRTLGVCP 987
Cdd:COG4778 21 GKRLPVLD-GVSFsvAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqasprEILalrRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 988 QH-NVL-----FDIltVEEHVwfygRMKGMSLEEVNKEMNSLLEdvglqhkRFEQTKNL--------SGGMQRKLSVAIA 1053
Cdd:COG4778 100 QFlRVIprvsaLDV--VAEPL----LERGVDREEARARARELLA-------RLNLPERLwdlppatfSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1054 FIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1894-2087 |
1.16e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.44 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLmgyc 1973
Cdd:PRK10619 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDA-IIDLLTGR-----EHLEFYARLrgvpeSYVEKVAQWGVQKLGLSQYADRE---------------AGGY----S 2028
Cdd:PRK10619 80 KVADKnQLRLLRTRltmvfQHFNLWSHM-----TVLENVMEAPIQVLGLSKQEAREravkylakvgideraQGKYpvhlS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2029 GGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSME 2087
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
907-1123 |
1.18e-08 |
|
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: 60.20 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKiyKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTAG-TIYVKGM------------- 970
Cdd:TIGR03269 1 IEVKNLTK--KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGrIIYHVALcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 971 ---------------------------DIRSDMDII-RRTLGVCPQHNVLFDILTVEEHVwfygrmkGMSLEEVNKEMNS 1022
Cdd:TIGR03269 79 gepcpvcggtlepeevdfwnlsdklrrRIRKRIAIMlQRTFALYGDDTVLDNVLEALEEI-------GYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1023 LLEDVGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLK--YREGRTIILSTHYMDE 1100
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|...
gi 1207110406 1101 ADLLGDRIAIISQGKLCCCGTPL 1123
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPD 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
916-1100 |
1.26e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLF- 993
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 994 DilTVEEHVWFYGRMKGMSLEEvnKEMNSLLEDVGLQHKRFEQTKN-LSGGMQRKLSVA--IAFIggSKVVVLDEPTAGV 1070
Cdd:PRK10247 95 D--TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIrnLQFM--PKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1207110406 1071 DPYSRRGIWDLLLKYREGRTI--ILSTHYMDE 1100
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIavLWVTHDKDE 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1908-2113 |
1.26e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRML------------TGDTRITyGEAFLSNQSVLTEMEKVHQLMGYCPQ 1975
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDVLLG-GRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FDAII--DLLTGREHLEFYAR--LRGVPESYVEKVAQWGVQKLGLSQYADReaggYSGGNKRKLSTAIALIGAAPVIFLD 2051
Cdd:PRK14271 113 FPMSImdNVLAGVRAHKLVPRkeFRGVAQARLTEVGLWDAVKDRLSDSPFR----LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2052 EPTTGMDPKAKRFLWNCILSVVkEGRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1872-2084 |
1.46e-08 |
|
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: 59.95 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1872 MEDEDVARERER----VKNGRALGDILI-LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG--- 1943
Cdd:TIGR03719 296 LLSQEFQKRNETaeiyIPPGPRLGDKVIeAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqeq 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1944 -DT-RITYGEAflsnqsvltemekVHqlMGYCPQF-DAIIDLLT-------GREHL-----EFYARlrgvpeSYVEKVAQ 2008
Cdd:TIGR03719 374 pDSgTIEIGET-------------VK--LAYVDQSrDALDPNKTvweeisgGLDIIklgkrEIPSR------AYVGRFNF 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2009 WGV--QKLglsqyadreAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVvkeGRSVVLTSH 2084
Cdd:TIGR03719 433 KGSdqQKK---------VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1893-2104 |
1.61e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkAGRKpAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK------- 1965
Cdd:PRK10762 4 LLQLKGIDKAF-PGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 --VHQLMGYCPQFDAIIDLLTGRehlEFYARLRGV--PESYVEkvAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIAL 2041
Cdd:PRK10762 82 giIHQELNLIPQLTIAENIFLGR---EFVNRFGRIdwKKMYAE--ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2042 IGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1918-2104 |
2.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1918 IPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVL--TEMEK-------VHQLMGYCPQFDAIIDLLTGReh 1988
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAAlaagvaiIYQELHLVPEMTVAENLYLGQ-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1989 leFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNC 2068
Cdd:PRK11288 105 --LPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRV 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207110406 2069 ILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:PRK11288 183 IRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
927-1115 |
2.22e-08 |
|
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: 56.71 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirsdmdiirrTLGVCPQ----------HNVLFDil 996
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQepwiqngtirENILFG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 997 tveehvwfygrmkgmslEEVNKEM-NSLLEDVGLQH--KRFE---QTK------NLSGGMQRKLSVAIAFIGGSKVVVLD 1064
Cdd:cd03250 90 -----------------KPFDEERyEKVIKACALEPdlEILPdgdLTEigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1065 EPTAGVDPYSRRGIWDLLL--KYREGRTIILSTH---YMDEAdllgDRIAIISQGK 1115
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
927-1096 |
2.78e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 927 LNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSdmdiIRRTLGVCPQHNVLFDI-LTVEEHVWFY 1005
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPYCTYIGHNLGLKLeMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1006 GRMKGmSLEEVNKEMNSLledvGLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL-LK 1084
Cdd:PRK13541 95 SEIYN-SAETLYAAIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvMK 169
|
170
....*....|..
gi 1207110406 1085 YREGRTIILSTH 1096
Cdd:PRK13541 170 ANSGGIVLLSSH 181
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1908-2084 |
3.02e-08 |
|
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: 56.46 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK-VHQLMGYCPQfDAIIDLLTGR 1986
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQ-DTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1987 EHLEfYARLRGVPESYVEKVAQWG----VQKL--GLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPK 2060
Cdd:cd03254 95 ENIR-LGRPNATDEEVIEAAKEAGahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180
....*....|....*....|....
gi 1207110406 2061 AKRFLWNCILSvVKEGRSVVLTSH 2084
Cdd:cd03254 174 TEKLIQEALEK-LMKGRTSIIIAH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1896-2111 |
3.60e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.79 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYCPQ 1975
Cdd:PRK10851 5 IANIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 FDAIIDLLTGREHLEFYARL---RGVPESYV--EKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFL 2050
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlprRERPNAAAikAKVTQL-LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2051 DEPTTGMDPKAKRFLWNCILSVVKEGR--SVVLTsHSMEECEALCTRMAIMVNGRFQCLGSVQ 2111
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKftSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
888-1096 |
4.37e-08 |
|
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: 59.15 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 888 PREEQDARIEAEPTNLILGVSIRN--LVKIYKKGAKLAVNHLNIKFYE---------------GQITSFLGHNGAGKTTT 950
Cdd:TIGR01271 1182 PQEEPRPSGGGGKYQLSTVLVIENphAQKCWPSGGQMDVQGLTAKYTEagravlqdlsfsvegGQRVGLLGRTGSGKSTL 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 951 MSILTGLFPpTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFD----------ILTVEEHVWFYGRMKGMS--LEEVN 1017
Cdd:TIGR01271 1262 LSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVFIFSgtfrknldpyEQWSDEEIWKVAEEVGLKsvIEQFP 1340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1018 KEMNSLLEDVGLQhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTH 1096
Cdd:TIGR01271 1341 DKLDFVLVDGGYV---------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
907-1116 |
4.74e-08 |
|
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: 56.79 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPpTAGTIYVKGMDIRS-DMDIIRRTLGV 985
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDiLTVEEHVWFYGRMKgmsleevNKEMNSLLEDVGLQH--KRFEQTKN---------LSGGMQRKLSVAIAF 1054
Cdd:cd03289 82 IPQKVFIFS-GTFRKNLDPYGKWS-------DEEIWKVAEEVGLKSviEQFPGQLDfvlvdggcvLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1055 IGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMdEADLLGDRIAIISQGKL 1116
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1907-2103 |
4.94e-08 |
|
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: 55.55 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1907 RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQsvltemekvhqlMGYCPQFdAIIDLLTGR 1986
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQE-PWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1987 EHLEFYARLRgvPESYvEKVaqwgVQKLGLSQYADREAGG-----------YSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:cd03250 84 ENILFGKPFD--EERY-EKV----IKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 2056 GMDPKAKRFLW-NCILSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2103
Cdd:cd03250 157 AVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1908-2116 |
6.34e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTST----FRMLTGDTRITYGEAFLSNQSVLTEM---EKVHQLMgYCPQfDAII 1980
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCAlrgRKIATIM-QNPR-SAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1981 DLLTGREHLEFYARLRGVPESyvEKVAQWGVQKLGLSQyADREAGGY----SGGNKRKLSTAIALIGAAPVIFLDEPTTG 2056
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPAD--DATLTAALEAVGLEN-AARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2057 MDPKAK-RFLwNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNR 2116
Cdd:PRK10418 171 LDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1909-2103 |
6.36e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1909 PAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEmekvhqlmgyCPQ------------- 1975
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR----------SPQdglangivyised 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1976 --FDAIIDLLTGREH-----LEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREA--GGYSGGNKRKLSTAIALIGAAP 2046
Cdd:PRK10762 336 rkRDGLVLGMSVKENmsltaLRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQaiGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1896-2103 |
6.41e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1896 LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRML-------TGDTRITyGEAF-LSNQSVLTEMEKVH 1967
Cdd:COG4161 5 LKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIA-GHQFdFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1968 QLMGYCPQFDAIIDLLTGREHL-EFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAP 2046
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 2047 VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1916-2085 |
8.35e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRM------LTGDTRITyGEAFLSNQSVLTEME---KVHQLMGYCPQFDAIIDLLTGR 1986
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVE-GEVRLFGRNIYSPDVdpiEVRREVGMVFQYPNPFPHLTIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1987 EHLEFYARLRGVPESYVE--KVAQWGVQKLGL-SQYADR---EAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPK 2060
Cdd:PRK14267 104 DNVAIGVKLNGLVKSKKEldERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPV 183
|
170 180
....*....|....*....|....*
gi 1207110406 2061 AKRFLWNCILSvVKEGRSVVLTSHS 2085
Cdd:PRK14267 184 GTAKIEELLFE-LKKEYTIVLVTHS 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2004-2103 |
9.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2004 EKVAQWgVQKLGLS-QYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLT 2082
Cdd:PRK13641 123 EKALKW-LKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILV 201
|
90 100
....*....|....*....|.
gi 1207110406 2083 SHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13641 202 THNMDDVAEYADDVLVLEHGK 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
941-1071 |
1.02e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 941 GHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSD--MDIiRRTLGVCPQHNVLF------DILTVEEH----VWfygrm 1008
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDL-RKVLGIIPQAPVLFsgtvrfNLDPFNEHndadLW----- 1345
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1009 kgMSLEEVNkemnslLEDV------GLQHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PLN03130 1346 --ESLERAH------LKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1921-2102 |
1.05e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1921 GECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV--LTEMeKVHQLMGY-CPQFDAIIDLLTGREHLEFyaRLRG 1997
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPA-KAHQLGIYlVPQEPLLFPNLSVKENILF--GLPK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1998 VPESYvEKVAQWgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGR 2077
Cdd:PRK15439 114 RQASM-QKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGV 191
|
170 180
....*....|....*....|....*
gi 1207110406 2078 SVVLTSHSMEECEALCTRMAIMVNG 2102
Cdd:PRK15439 192 GIVFISHKLPEIRQLADRISVMRDG 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1872-2104 |
1.13e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1872 MEDEDVARERERVKngRALGD-ILILSDLSkVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYG 1950
Cdd:COG3845 237 MVGREVLLRVEKAP--AEPGEvVLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1951 EAFLSNQSVltEMEKVHQL--------------MGYCPQFDAIIDLLTGREHLEFYARL----RGVPESYVEK-VAQWGV 2011
Cdd:COG3845 314 SIRLDGEDI--TGLSPRERrrlgvayipedrlgRGLVPDMSVAENLILGRYRRPPFSRGgfldRKAIRAFAEElIEEFDV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2012 QKLGlsqyADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEA 2091
Cdd:COG3845 392 RTPG----PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILA 467
|
250
....*....|...
gi 1207110406 2092 LCTRMAIMVNGRF 2104
Cdd:COG3845 468 LSDRIAVMYEGRI 480
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
934-1096 |
1.17e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDIIRRTlGVCPQHNVLFDILTVEEHVWFYGRM---KG 1010
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1011 MSLEEVNKEMNSLLEDVGLqhKRFEQT-------KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSR-RGIWDLL 1082
Cdd:PLN03211 173 LTKQEKILVAESVISELGL--TKCENTiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLG 250
|
170
....*....|....
gi 1207110406 1083 LKYREGRTIILSTH 1096
Cdd:PLN03211 251 SLAQKGKTIVTSMH 264
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
924-1102 |
1.19e-07 |
|
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: 54.64 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIY----VKGMDIRSDMDIIRR-TLGVCPQHNVLFDIlTV 998
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRySVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 999 EEHVWFYGRMKGMSLEEVNkEMNSLLEDVGL-----QHKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY 1073
Cdd:cd03290 96 EENITFGSPFNKQRYKAVT-DACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207110406 1074 -----SRRGIWDLLLKyrEGRTIILSTH---YMDEAD 1102
Cdd:cd03290 175 lsdhlMQEGILKFLQD--DKRTLVLVTHklqYLPHAD 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1916-2103 |
1.19e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLT------------GDTRITYGEAfLSNQSVLteMEKVHQLMGYCPQFdaiIDLL 1983
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARS-LSQQKGL--IRQLRQHVGFVFQN---FNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1984 TGREHLEFYAR----LRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP 2059
Cdd:PRK11264 98 PHRTVLENIIEgpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 2060 KAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1887-2123 |
1.24e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1887 GRALGDILilsDLSKVYKAGRKPAVNR-LCLGIPRGECFGLLGVNGAGKTSTFRMLTG-----DTRITY-GEAFLSNQSV 1959
Cdd:PRK14246 4 GKSAEDVF---NISRLYLYINDKAILKdITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKIKVdGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1960 L-TEMEKVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESY-VEKVAQWGVQKLGL-SQYADR---EAGGYSGGNKR 2033
Cdd:PRK14246 81 FqIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2034 KLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEgRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|....
gi 1207110406 2114 ----KNRFGDGYTI 2123
Cdd:PRK14246 240 ftspKNELTEKYVI 253
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
907-1131 |
1.36e-07 |
|
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: 57.26 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 907 VSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirsdmdiirrTLGVC 986
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 987 PQHNVLFDIlTVEEHVWFygrmkGMSLEE----VNKEMNSLLEDV-----GLQHKRFEQTKNLSGGMQRKLSVAIAFIGG 1057
Cdd:TIGR00957 705 PQQAWIQND-SLRENILF-----GKALNEkyyqQVLEACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1058 SKVVVLDEPTAGVDPYSRRGIWDLLLKYR---EGRTIILSTH---YMDEADLlgdrIAIISQGKLCCCGTPLFLKARLGT 1131
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQRDGA 854
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1892-2063 |
1.51e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1892 DILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlteMEKVHQLMG 1971
Cdd:PRK11432 5 NFVVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1972 YCPQFD--AIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIF 2049
Cdd:PRK11432 80 ICMVFQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170
....*....|....
gi 1207110406 2050 LDEPTTGMDPKAKR 2063
Cdd:PRK11432 160 FDEPLSNLDANLRR 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1920-2103 |
2.17e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1920 RGECFGLLGVNGAGKTSTFRMLTGDTRITY-GEAFLSNQSVLTE--MEKVHQLMGYCPQ---FDAIIDLLTGREH----- 1988
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRnpQQAIAQGIAMVPEdrkRDGIVPVMGVGKNitlaa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1989 LEFYARLRGVPESYVEKVAQWGVQKLGL-SQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWN 2067
Cdd:PRK13549 367 LDRFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207110406 2068 CILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK13549 447 LINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1897-2102 |
3.34e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.40 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1897 SDLSKVYKAG---RKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYG-----EAFLSNQSVLTEMEKVHQ 1968
Cdd:PRK13646 6 DNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKTKDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1969 LMGYCPQF--DAIIDLLTGREhLEFYARLRGVPESYVEKVAQWGVQKLGLSQ-YADREAGGYSGGNKRKLSTAIALIGAA 2045
Cdd:PRK13646 86 RIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2046 PVIFLDEPTTGMDPKAKRFLWNCILSV-VKEGRSVVLTSHSMEECEALCTRMAIMVNG 2102
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
909-1116 |
3.97e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYKKGAKL-------AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGM-----DIRSDM 976
Cdd:PRK15112 7 VRNLSKTFRYRTGWfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DIIRR-----TLGVCPQHNV--LFDI---LTVEehvwfygrmkgMSLEEVNKEMNSLLEDVGL--QHKRFEQTKNLSGGM 1044
Cdd:PRK15112 87 QRIRMifqdpSTSLNPRQRIsqILDFplrLNTD-----------LEPEQREKQIIETLRQVGLlpDHASYYPHMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1045 QRkLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTI--ILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK15112 156 QR-LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1893-2084 |
4.91e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGRKP--AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV-------LTEM 1963
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadaLAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1964 EKVHqlMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIG 2043
Cdd:PRK10535 84 RREH--FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207110406 2044 AAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
908-1116 |
5.27e-07 |
|
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: 54.69 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNL-VKIYK-KGAKLAVNHLNIKFYEGQITSFLGHNGAGKT-TTMSILtGLFPPTA----GTIYVKGMDI----RSDM 976
Cdd:COG4172 8 SVEDLsVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAahpsGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DIIR-RTLGVCPQH-----NVLFdilTVEE--------HvwfygrmKGMSLEEVNKEMNSLLEDVGLQH--KRFE----Q 1036
Cdd:COG4172 87 RRIRgNRIAMIFQEpmtslNPLH---TIGKqiaevlrlH-------RGLSGAAARARALELLERVGIPDpeRRLDayphQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1037 tknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHymdeaDL-----LGDRIA 1109
Cdd:COG4172 157 ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH-----DLgvvrrFADRVA 228
|
....*..
gi 1207110406 1110 IISQGKL 1116
Cdd:COG4172 229 VMRQGEI 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
918-1126 |
5.46e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 918 KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVkgmdirsdmdiIRRTLGVCPQHNVLFDIlT 997
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEEHVWFygrmkGMSLEEVnkEMNSLLEDVGLQH-----------KRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEP 1066
Cdd:PLN03130 695 VRDNILF-----GSPFDPE--RYERAIDVTALQHdldllpggdltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 1067 TAGVDPYSRRGIWDLLLKyRE--GRTIILST---HYMDEAdllgDRIAIISQGKLCCCGT--------PLFLK 1126
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIK-DElrGKTRVLVTnqlHFLSQV----DRIILVHEGMIKEEGTyeelsnngPLFQK 835
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
648-849 |
5.49e-07 |
|
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: 54.32 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 648 LPLFMTLAWIYSVAMIIKGVVYEKEARLKETMRIMGLGSGMLWFSWFISSYLPFLFSAALLIAALKwGDILPYSDPAVVF 727
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLF-GIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 728 FFLAAFATATIMLCFLISTFFSR---ANLAAACGGLIYFTLYLPYVLcvawREYLTSTHRILASFLSPVAFGFGceyfsq 804
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNsedAQSIIGIVILLLSGFFGGLFP----LEDPPSFLQWIFSIIPFFSPIDG------ 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207110406 805 yeeqgvgiqwfnLKSSPMEGDTYSFNTSIMMLYADALIYALATWY 849
Cdd:pfam12698 313 ------------LLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1906-2058 |
5.86e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK-VHQLMGYCPQF-----DAI 1979
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNattpgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1980 IDLLTGR---EHLEFYARLRGVPESYVEKvaqwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTG 2056
Cdd:PRK10253 98 VQELVARgryPHQPLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 1207110406 2057 MD 2058
Cdd:PRK10253 174 LD 175
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1874-2058 |
6.28e-07 |
|
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: 54.75 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1874 DEDVARERERVKNGRALGDILIlSDLSKVYKAGRkPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAF 1953
Cdd:TIGR01193 455 DSEFINKKKRTELNNLNGDIVI-NDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1954 LsNQSVLTEMEK--VHQLMGYCPQ----FDAII--DLLTG-REHLEFYARLRGVpeSYVEKVAQWGVQKLGLSQYADREA 2024
Cdd:TIGR01193 533 L-NGFSLKDIDRhtLRQFINYLPQepyiFSGSIleNLLLGaKENVSQDEIWAAC--EIAEIKDDIENMPLGYQTELSEEG 609
|
170 180 190
....*....|....*....|....*....|....
gi 1207110406 2025 GGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMD 2058
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2025-2103 |
7.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 7.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2025 GGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
908-1115 |
8.55e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 908 SIRNLVKIYKKGAKL--AVNHLNIKFYEGQITSFLGHNGAGKT-TTMSILTGLfpPTAGTIYVKGmDIR--------SDM 976
Cdd:PRK15134 7 AIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DIIRRTLG-------------VCPQHNV---LFDILTVEehvwfygrmKGMSLEEVNKEMNSLLEDVGLQH--KRFEQ-T 1037
Cdd:PRK15134 84 QTLRGVRGnkiamifqepmvsLNPLHTLekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIRQaaKRLTDyP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1038 KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
923-1100 |
9.00e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIyvkgmDIRSDMDIIRRTLGVCPQhnvlfdiLTVEEHV 1002
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 WFYGRMKGMSLEEVNKEMNSLLE--DVGlqhKRFEQ-TKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIW 1079
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEfaDIG---KFIYQpVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180
....*....|....*....|..
gi 1207110406 1080 DLLLKYRE-GRTIILSTHYMDE 1100
Cdd:PRK13545 184 DKMNEFKEqGKTIFFISHSLSQ 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1040-1111 |
1.36e-06 |
|
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: 50.44 E-value: 1.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1040 LSGGMQRKLSVAIAF----IGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYR-EGRTIILSTHYMDEADLLgDRIAII 1111
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELA-DKLIHI 153
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
916-1071 |
1.56e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 916 YKKGAKL-AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMD-----------IRSDMDII---- 979
Cdd:PRK15079 28 WQPPKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgmkddewraVRSDIQMIfqdp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 ------RRTLGvcpqhnvlfDILTvEEHVWFYGRmkgMSLEEVNKEMNSLLEDVGL---QHKRFEQtkNLSGGMQRKLSV 1050
Cdd:PRK15079 108 laslnpRMTIG---------EIIA-EPLRTYHPK---LSRQEVKDRVKAMMLKVGLlpnLINRYPH--EFSGGQCQRIGI 172
|
170 180
....*....|....*....|.
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALD 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1902-2102 |
1.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1902 VYKAGRKPAVNRL---CLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTE-MEKVHQLMGYCPQF- 1976
Cdd:PRK13642 11 VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1977 DAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAiALIGAAP-VIFLDEPTT 2055
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA-GIIALRPeIIILDESTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207110406 2056 GMDPKAKRFLWNCILSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNG 2102
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1894-2087 |
1.58e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRK---PAVNRLCLGIPRGECFGLLGVNGAGKTSTFRML-------TGDTRITYGEAFLSNQSVLTE- 1962
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdTGTIEWIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1963 --------------MEKVHQL---MGYCPQFdAIIDLL--TGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQ-YADR 2022
Cdd:PRK13651 83 vleklviqktrfkkIKKIKEIrrrVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 2023 EAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSME 2087
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1916-2084 |
1.59e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.84 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLT------GDTRITyGEAFLSNQSV----LTEMEKVHQLMGYCPQfdaIIDLLTG 1985
Cdd:PRK14247 24 LEIPDNTITALMGPSGSGKSTLLRVFNrlielyPEARVS-GEVYLDGQDIfkmdVIELRRRVQMVFQIPN---PIPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1986 REHLEFYARLRGVPESYVE--KVAQWGVQKLGL-SQYADR---EAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP 2059
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKElqERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180
....*....|....*....|....*
gi 1207110406 2060 KAKRFLWNCILSVVKEgRSVVLTSH 2084
Cdd:PRK14247 180 ENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1910-2084 |
2.18e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKtSTFRM-LTGDTRITYGEAFLSNQSVLTEmekvhQLMGYCPQFDAII-DLltgre 1987
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGK-STLAMlLTGLYQPQSGEILLDGKPVTAE-----QPEDYRKLFSAVFtDF----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1988 HLefYARLRGvPE---SYVEKVAQWgVQKLGLSQYADREAG-----GYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDP 2059
Cdd:PRK10522 407 HL--FDQLLG-PEgkpANPALVEKW-LERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180
....*....|....*....|....*.
gi 1207110406 2060 KAKRFLWNCILSVVKE-GRSVVLTSH 2084
Cdd:PRK10522 483 HFRREFYQVLLPLLQEmGKTIFAISH 508
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1893-2105 |
2.21e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGR--KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSvLTEM------E 1964
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-MSKLssaakaE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1965 KVHQLMGYCPQFDAIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGA 2044
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2045 APVIFLDEPTTGMDPKAKRFLWNCILSV-VKEGRSVVLTSHSMEECEALcTRMAIMVNGRFQ 2105
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
931-1071 |
2.23e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 931 FYEGQITSFLGHNGAGKTTTMSILTGlfPPTAGtiYVKGmDIR-----SDMDIIRRTLGVCPQHNVLFDILTVEEHVWFY 1005
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRisgfpKKQETFARISGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207110406 1006 GRMKgmSLEEVNKEMNSLLEDVGLQHKRFEQTKN----------LSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:PLN03140 978 AFLR--LPKEVSKEEKMMFVDEVMELVELDNLKDaivglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1894-2110 |
2.33e-06 |
|
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: 50.60 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSkvYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG--DTRITYGEAFLSNQSvLTEM---EKVHQ 1968
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGED-ITDLppeERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1969 LMGYCPQFDAIIDLLTgrehLEFYarLRGVPEsyvekvaqwgvqklglsqyadreagGYSGGNKRKLSTAIALIGAAPVI 2048
Cdd:cd03217 78 GIFLAFQYPPEIPGVK----NADF--LRYVNE-------------------------GFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2049 FLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEAL-CTRMAIMVNGRFQCLGSV 2110
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1894-2084 |
2.90e-06 |
|
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: 50.69 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRkPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQLMGY 1972
Cdd:cd03253 1 IEFENVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1973 CPQ----FDAIIdlltgrEHLEFYARLRGVPESYVE--KVAQWGVQKLGLSQ-YADR--EAGGY-SGGNKRKLSTAIALI 2042
Cdd:cd03253 80 VPQdtvlFNDTI------GYNIRYGRPDATDEEVIEaaKAAQIHDKIMRFPDgYDTIvgERGLKlSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 2043 GAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKeGRSVVLTSH 2084
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
884-1067 |
2.92e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 884 IPPAPREeQDARIEAEptnlilgvsirNLVKIYkkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAG 963
Cdd:PRK11819 314 IPPGPRL-GDKVIEAE-----------NLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 964 TI---------YVKGMdiRSDMDiirrtlgvcPQHNVL------FDILTVeehvwfyGrmkgmsleevNKEMNSLLEdVG 1028
Cdd:PRK11819 380 TIkigetvklaYVDQS--RDALD---------PNKTVWeeisggLDIIKV-------G----------NREIPSRAY-VG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207110406 1029 lqhkRF-----EQTK---NLSGGMQRKLSVAIAFIGGSKVVVLDEPT 1067
Cdd:PRK11819 431 ----RFnfkggDQQKkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1887-2103 |
3.32e-06 |
|
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: 52.41 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1887 GRALGDILIlSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNqsvltemekv 1966
Cdd:TIGR02203 325 ERARGDVEF-RNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1967 HQLMGYCPQ-FDAIIDLLTGREHLeF---------YARLRGVPESYVEKVAQWG-----VQKL--GLSQYADREAGGYSG 2029
Cdd:TIGR02203 394 HDLADYTLAsLRRQVALVSQDVVL-FndtianniaYGRTEQADRAEIERALAAAyaqdfVDKLplGLDTPIGENGVLLSG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2030 GNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRfLWNCILSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2103
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGR 544
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1916-2103 |
4.00e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.14 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1916 LGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEME----KV------HQLmgycpqFDaiidlltg 1985
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPpaerPVsmlfqeNNL------FP-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1986 reHLEFYA----------RLRGVPESYVEKVAQwgvqKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTT 2055
Cdd:COG3840 85 --HLTVAQniglglrpglKLTAEQRAQVEQALE----RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2056 GMDPkAKRFLwncILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG3840 159 ALDP-ALRQE---MLDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
936-1115 |
4.29e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 936 ITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG---MDIRSDMDII--RRTLGVCPQHNVLFDILTVEehvwfyGRMK- 1009
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGICLPpeKRRIGYVFQDARLFPHYKVR------GNLRy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1010 GMSleevnKEMNSLLEDV----GLQH--KRFEQTknLSGG-MQRklsVAI--AFIGGSKVVVLDEPTAGVD-PYSRRgiw 1079
Cdd:PRK11144 100 GMA-----KSMVAQFDKIvallGIEPllDRYPGS--LSGGeKQR---VAIgrALLTAPELLLMDEPLASLDlPRKRE--- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 1080 dlLLKY-----REGRTIIL-STHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK11144 167 --LLPYlerlaREINIPILyVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1893-2102 |
4.53e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.54 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKtSTF-----RM--------LTGDtrITY-GEAFLSNQS 1958
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGK-STLlrsinRMndlnpevtITGS--IVYnGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1959 VLTEMEK----VHQLMGYCPqfdaiidlLTGREHLEFYARLRGVPESYV--EKVAQWGVQKLGLSQYADR---EAGGYSG 2029
Cdd:PRK14239 80 DTVDLRKeigmVFQQPNPFP--------MSIYENVVYGLRLKGIKDKQVldEAVEKSLKGASIWDEVKDRlhdSALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2030 GNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSvVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2102
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1918-2058 |
4.93e-06 |
|
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: 50.10 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1918 IPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVltemekvhqlmGYCPQFdaIIDLLTGRehleFYARLRG 1997
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQY--IKADYEGT----VRDLLSS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1998 VPESYVEKvAQWGV---QKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMD 2058
Cdd:cd03237 85 ITKDFYTH-PYFKTeiaKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
923-1115 |
7.61e-06 |
|
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: 51.22 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTT-MSILtGLFPpTAGTIYVKGMDI-----------RSDMDII----------R 980
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLdglsrralrplRRRMQVVfqdpfgslspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 981 RTLGvcpqhnvlfDIltVEE----HvwfygrMKGMSLEEVNKEMNSLLEDVGLQhkrfEQTKN-----LSGGmQR-KLSV 1050
Cdd:COG4172 379 MTVG---------QI--IAEglrvH------GPGLSAAERRARVAEALEEVGLD----PAARHrypheFSGG-QRqRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1051 AIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHymdeaDL-----LGDRIAIISQGK 1115
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLrdLQREHGLAYLFISH-----DLavvraLAHRVMVMKDGK 503
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
890-1108 |
8.72e-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: 50.94 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 890 EEQDARIEAEPTNLilgVSIRNLVKIYKkGAKLAVNHLNIkfYEGQITSFLGHNGAGKTTTMSILTGLFPPTAG------ 963
Cdd:COG1245 328 EVHAPRREKEEETL---VEYPDLTKSYG-GFSLEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedl 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 964 TIYVKGMDIRSDMDIirrtlgvcpqhnvlfdilTVEEHvwfygrmkgmsLEEVNKEM-------NSLLEDVGLqHKRFEQ 1036
Cdd:COG1245 402 KISYKPQYISPDYDG------------------TVEEF-----------LRSANTDDfgssyykTEIIKPLGL-EKLLDK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207110406 1037 T-KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGR--TIILSTH--YMdeADLLGDRI 1108
Cdd:COG1245 452 NvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHdiYL--IDYISDRL 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
933-1111 |
1.02e-05 |
|
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: 50.94 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 933 EGQITSFLGHNGAGKTTTMSILTGLFPPTAGtIYVKGMDIRsdmDIIRRTLGvcpqhNVLFDILT--VEEHV-------- 1002
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG-DYDEEPSWD---EVLKRFRG-----TELQDYFKklANGEIkvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1003 ------WFYGRMKGMsLEEVN--KEMNSLLEDVGLQHKRFEQTKNLSGG-MQRkLSVAIAFIGGSKVVVLDEPTAGVDPY 1073
Cdd:COG1245 169 vdlipkVFKGTVREL-LEKVDerGKLDELAEKLGLENILDRDISELSGGeLQR-VAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207110406 1074 SR----RGIWDLLlkyREGRTIILSTHymDEA--DLLGDRIAII 1111
Cdd:COG1245 247 QRlnvaRLIRELA---EEGKYVLVVEH--DLAilDYLADYVHIL 285
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
899-1116 |
1.04e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 899 EPTNLILGVsiRNLVKIYKKgaklAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKG--MDIRSDM 976
Cdd:PRK10982 245 KPGEVILEV--RNLTSLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkINNHNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 977 DII----------RRTLGVCPQHNVLFD--ILTVEEHVWFYGRMKgmsleevNKEMNSLLEDV--GLQHKRFEQTKN--- 1039
Cdd:PRK10982 319 EAInhgfalvteeRRSTGIYAYLDIGFNslISNIRNYKNKVGLLD-------NSRMKSDTQWVidSMRVKTPGHRTQigs 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1040 LSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKY-REGRTIILSTHYMDEadLLG--DRIAIISQGKL 1116
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2028-2157 |
1.14e-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: 50.57 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2028 SGGNKRKLSTAIALIgAAPVIFL-DEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:TIGR03269 170 SGGEKQRVVLARQLA-KEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 2106 CLGSVQHLKNRFGDGYTI------------ILRLSTPSAEPCPVDAYIQNAFPGIQLKERHQNV 2157
Cdd:TIGR03269 249 EEGTPDEVVAVFMEGVSEvekecevevgepIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEI 312
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2021-2104 |
1.22e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2021 DREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMV 2100
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
....
gi 1207110406 2101 NGRF 2104
Cdd:NF040905 479 EGRI 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
910-1096 |
1.36e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 910 RNLVKIYKKgaklavnhLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIRSDMDI--IRRTLGVCP 987
Cdd:PTZ00265 395 RKDVEIYKD--------LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLkwWRSKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 988 QHNVLF----------------DILTVEEH-------------------VWFYGRMKGMS-------LEEVNKEMNS--- 1022
Cdd:PTZ00265 467 QDPLLFsnsiknnikyslyslkDLEALSNYynedgndsqenknkrnscrAKCAGDLNDMSnttdsneLIEMRKNYQTikd 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1023 ----------LLED-VGLQHKRFE-----QTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LK 1084
Cdd:PTZ00265 547 sevvdvskkvLIHDfVSALPDKYEtlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLK 626
|
250
....*....|..
gi 1207110406 1085 YREGRTIILSTH 1096
Cdd:PTZ00265 627 GNENRITIIIAH 638
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
874-1122 |
1.49e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 874 GGVPLELGLPIPPAPREEQDARIEAEptnlilGVSIRnlvkiYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSI 953
Cdd:PTZ00243 1287 GTVVIEPASPTSAAPHPVQAGSLVFE------GVQMR-----YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLT 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 954 LTGLFPPTAGTIYVKGMDIRS-DMDIIRRTLGVCPQHNVLFDiLTVEEHVWFYgrmkgmsLEEVNKEMNSLLEDVGLQHK 1032
Cdd:PTZ00243 1356 FMRMVEVCGGEIRVNGREIGAyGLRELRRQFSMIPQDPVLFD-GTVRQNVDPF-------LEASSAEVWAALELVGLRER 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1033 R-----------FEQTKNLSGGMQRKLSVAIAFIG-GSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTIILSTHYMDE 1100
Cdd:PTZ00243 1428 VasesegidsrvLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHT 1507
|
250 260
....*....|....*....|..
gi 1207110406 1101 ADLLgDRIAIISQGKLCCCGTP 1122
Cdd:PTZ00243 1508 VAQY-DKIIVMDHGAVAEMGSP 1528
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1893-2103 |
1.81e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTE---------- 1962
Cdd:COG3845 5 ALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsprdaialgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1963 -MekVHQlmgycpQFdAIIDLLT-------GREHLEFYARLRGVPESYVEKVAQwgvqKLGLSQYADREAGGYSGGNKRK 2034
Cdd:COG3845 83 gM--VHQ------HF-MLVPNLTvaenivlGLEPTKGGRLDRKAARARIRELSE----RYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2035 LSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2028-2087 |
1.88e-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: 48.93 E-value: 1.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2028 SGGNKRKLSTAIALIGAAP---VIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSHSME 2087
Cdd:pfam13304 238 SDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1880-2118 |
2.48e-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: 49.94 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1880 ERERVKNGRalGDILILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLtgdtritygeaflsnqsv 1959
Cdd:TIGR00957 625 ERRTIKPGE--GNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL------------------ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1960 LTEMEKV--HQLM----GYCPQfDAIIDLLTGREHLEFYARLRgvpESYVEKVAQWG--VQKLGLSQYADR----EAG-G 2026
Cdd:TIGR00957 685 LAEMDKVegHVHMkgsvAYVPQ-QAWIQNDSLRENILFGKALN---EKYYQQVLEACalLPDLEILPSGDRteigEKGvN 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2027 YSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSV--VKEGRSVVLTSHSMEECEALcTRMAIMVNGRF 2104
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
250
....*....|....
gi 1207110406 2105 QCLGSVQHLKNRFG 2118
Cdd:TIGR00957 840 SEMGSYQELLQRDG 853
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
900-1115 |
3.10e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 900 PTNLILGVSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIR------ 973
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 974 --------SDMDIIRRT-LGVCPQHNV--LFDILTVEEHVWFYGRM-KGMSLEEVNKEMNSLLEDVGLQHKRFEQTK--- 1038
Cdd:PRK10261 88 ielseqsaAQMRHVRGAdMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 1039 NLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQGK 1115
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
934-1116 |
3.67e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILTGLFPPTAGTI------------------------YVkgMDIRSDMDIIRRTLGVCPQH 989
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalpqpaleYV--IDGDREYRQLEAQLHDANER 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 990 NVLFDILTVeehvwfYGRMKGMSLEEVNKEMNSLLEDVGLQHKRFEQ-TKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTA 1068
Cdd:PRK10636 105 NDGHAIATI------HGKLDAIDAWTIRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1069 GVDPYSRrgIW-DLLLKYREGrTIILSTHYMDEADLLGDRIAIISQGKL 1116
Cdd:PRK10636 179 HLDLDAV--IWlEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1910-2119 |
3.70e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKvhqlmGYCPQfdaiidlLTGREHL 1989
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS-----GLNGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 EFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDpkaKRFLWNCI 2069
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207110406 2070 --LSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGD 2119
Cdd:PRK13545 184 dkMNEFKEqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1894-2090 |
4.85e-05 |
|
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: 48.75 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTF----RMLTGDTRITYGEafLSNQSVltEMEKVHQL 1969
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIQIDG--VSWNSV--TLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQfdaIIDLLTG--REHLEFYARLRgvpESYVEKVAQWGVQKLGLSQYADR-----EAGGY--SGGNKRKLSTAIA 2040
Cdd:TIGR01271 1294 FGVIPQ---KVFIFSGtfRKNLDPYEQWS---DEEIWKVAEEVGLKSVIEQFPDKldfvlVDGGYvlSNGHKQLMCLARS 1367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2041 LIGAAPVIFLDEPTTGMDP--------KAKRFLWNCilsvvkegrSVVLTSHSME---ECE 2090
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPvtlqiirkTLKQSFSNC---------TVILSEHRVEallECQ 1419
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1906-2086 |
4.86e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEaflsnqsvlteMEKVHQL-MGYCPQ---FDAIID 1981
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-----------IKRNGKLrIGYVPQklyLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1982 LLTGRehlefYARLR-GVPESYV---------EKVAQWGVQKLglsqyadreaggySGGNKRKLSTAIALIGAAPVIFLD 2051
Cdd:PRK09544 84 LTVNR-----FLRLRpGTKKEDIlpalkrvqaGHLIDAPMQKL-------------SGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207110406 2052 EPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSM 2086
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
885-1096 |
5.44e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 885 PPAPREEQDARIEAEPTNLILGVSIrnlvkiykkgaklavnhlniKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGT 964
Cdd:PTZ00243 657 AKTPKMKTDDFFELEPKVLLRDVSV--------------------SVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 965 IYVKgmdirsdmdiirRTLGVCPQHNVLFDIlTVEEHVWFYGRMKGMSLEEVNKeMNSLLEDV-----GLQHKRFEQTKN 1039
Cdd:PTZ00243 717 VWAE------------RSIAYVPQQAWIMNA-TVRGNILFFDEEDAARLADAVR-VSQLEADLaqlggGLETEIGEKGVN 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 1040 LSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPY-SRRGIWDLLLKYREGRTIILSTH 1096
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATH 840
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1906-2115 |
6.44e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1906 GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSV----LTEMEKVHQLMGYCPQFDAIID 1981
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1982 LLTGREHLEFYARLRG-VPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRK--LSTAIALigAAPVIFLDEPTTGMD 2058
Cdd:PRK11831 98 DMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIAL--EPDLIMFDEPFVGQD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207110406 2059 PKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKN 2115
Cdd:PRK11831 176 PITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1910-2134 |
6.66e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVHQLMGYCPQF------------- 1976
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFifqdpyasldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1977 ---DAIIdlltgrEHLEFYARLRGvpESYVEKVAqWGVQKLGL-SQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDE 2052
Cdd:PRK10261 419 tvgDSIM------EPLRVHGLLPG--KAAAARVA-WLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2053 PTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFQCLGSVQHLKNRFGDGYTIILRLSTPS 2131
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
...
gi 1207110406 2132 AEP 2134
Cdd:PRK10261 570 ADP 572
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
2011-2113 |
6.72e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.50 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2011 VQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKakrfLWNCILSVVKE---GRSVVL--TSHS 2085
Cdd:PRK10771 114 ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA----LRQEMLTLVSQvcqERQLTLlmVSHS 189
|
90 100
....*....|....*....|....*...
gi 1207110406 2086 MEECEALCTRMAIMVNGRFQCLGSVQHL 2113
Cdd:PRK10771 190 LEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1893-2103 |
8.17e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.84 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTS----------------TFRMLTGDTRITY--GEA-- 1952
Cdd:PRK11701 6 LLSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTllnalsarlapdagevHYRMRDGQLRDLYalSEAer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1953 -FLSNqsvlTEMEKVHQ--LMGYCPQFDA---IIDLL--TGREHlefYARLRGVPESYVEKVaqwgvqKLGLSQYADReA 2024
Cdd:PRK11701 84 rRLLR----TEWGFVHQhpRDGLRMQVSAggnIGERLmaVGARH---YGDIRATAGDWLERV------EIDAARIDDL-P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2025 GGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2103
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
886-1082 |
8.59e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 886 PAPREEQDARIeAEPTNLILGVSIRNLVKIYKKGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPpTAGTI 965
Cdd:PRK15134 265 PVPLPEPASPL-LDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 966 YVKGMDI----RSDMDIIRRTLGVC---------PQHNVLFDI---LTVEEhvwfygrmKGMSLEEVNKEMNSLLEDVGL 1029
Cdd:PRK15134 343 WFDGQPLhnlnRRQLLPVRHRIQVVfqdpnsslnPRLNVLQIIeegLRVHQ--------PTLSAAQREQQVIAVMEEVGL 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207110406 1030 Q-HKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL 1082
Cdd:PRK15134 415 DpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALL 468
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1895-2083 |
8.90e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1895 ILSDLSKVYKAGRKPavnrLCLGIPR-GECFGLLGVngAGKTSTFRMLTGDtrITYgeaflsNQSVLTEMEKvHQLMGYC 1973
Cdd:PLN03140 180 ILKDASGIIKPSRMT----LLLGPPSsGKTTLLLAL--AGKLDPSLKVSGE--ITY------NGYRLNEFVP-RKTSAYI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1974 PQFDAIIDLLTGREHLEFYARLRGV--------------------PESYVE----KVAQWGVQK----------LGLSQY 2019
Cdd:PLN03140 245 SQNDVHVGVMTVKETLDFSARCQGVgtrydllselarrekdagifPEAEVDlfmkATAMEGVKSslitdytlkiLGLDIC 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207110406 2020 ADREAG-----GYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTS 2083
Cdd:PLN03140 325 KDTIVGdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMS 393
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
909-1156 |
9.35e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 909 IRNLVKIYK--KGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLfppTAGTIYVKGMDIR-SDMDII------ 979
Cdd:PRK15093 6 IRNLTIEFKtsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRfDDIDLLrlspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 980 -RRTLGvcpqHNV--LF----DILTVEEHV----------WFYgrmKGMSLEEVN---KEMNSLLEDVGLQ-HKRFEQT- 1037
Cdd:PRK15093 83 rRKLVG----HNVsmIFqepqSCLDPSERVgrqlmqnipgWTY---KGRWWQRFGwrkRRAIELLHRVGIKdHKDAMRSf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1038 -KNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTHYMDEADLLGDRIAIISQG 1114
Cdd:PRK15093 156 pYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1207110406 1115 KLCCCGTPLFLKARLGTGYYLTLVK------REM-HRTPSNTSSGKIPS 1156
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQALIRaipdfgSAMpHKSRLNTLPGAIPL 284
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
919-1094 |
1.16e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTI-YVKGMdirsdmdiirrTLGVCPQHNVLFdiLT 997
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI-----------KLGYFAQHQLEF--LR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 998 VEE----HvwfygrMKGMSLEEVNKEMNSLLEDVGLQ-HKRFEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDP 1072
Cdd:PRK10636 390 ADEsplqH------LARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|..
gi 1207110406 1073 YSRRGIWDLLLKYrEGRTIILS 1094
Cdd:PRK10636 464 DMRQALTEALIDF-EGALVVVS 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
934-1071 |
1.23e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 934 GQITSFLGHNGAGKTTTMSILT----GLFPPTAGTIYVKGMDIRSDMDIIRRTLGVCPQHNVLFDILTVEEHVWFYGRMK 1009
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCK 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207110406 1010 -------GMSLEEVNKEMNSL-LEDVGLQHKRFEQTKN-----LSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVD 1071
Cdd:TIGR00956 167 tpqnrpdGVSREEYAKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1894-2169 |
1.58e-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: 46.00 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSKVYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTF----RMLTGDTRITYGEafLSNQSVltEMEKVHQL 1969
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTEGDIQIDG--VSWNSV--PLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQfDAIIDLLTGREHLEFYARLRgvpESYVEKVAQWGVQKLGLSQYADR-----EAGGY--SGGNKRKLSTAIALI 2042
Cdd:cd03289 79 FGVIPQ-KVFIFSGTFRKNLDPYGKWS---DEEIWKVAEEVGLKSVIEQFPGQldfvlVDGGCvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2043 GAAPVIFLDEPTTGMDPkakrFLWNCILSVVKE---GRSVVLTSHSMeecEAL--CTRMAIMVNGRFQCLGSVQHLKNRf 2117
Cdd:cd03289 155 SKAKILLLDEPSAHLDP----ITYQVIRKTLKQafaDCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLNE- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 2118 gdgyTIILRLSTPSAEPCPVdayiqnaFPGiqlkeRHQNVLQYQLPSQTCSL 2169
Cdd:cd03289 227 ----KSHFKQAISPSDRLKL-------FPR-----RNSSKSKRKPRPQIQAL 262
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1019-1096 |
1.68e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1019 EMNSLLEDVGLQH--KRFEQTKN----LSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDPYSRRGIWDLLLKYREGRTII 1092
Cdd:COG4178 459 ELREALEAVGLGHlaERLDEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVI 538
|
....
gi 1207110406 1093 LSTH 1096
Cdd:COG4178 539 SVGH 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1903-2059 |
2.14e-04 |
|
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: 44.79 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1903 YKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTST----FRMLTgdtrITYGEAFLSNQSVLT-EMEKVHQLMGYCPQfD 1977
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVDISKiGLHDLRSRISIIPQ-D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1978 AIidLLTG--REHLEFY-----ARLRGVpesyVEKVAQWG-VQKLGLSQYADREAGG--YSGGNKRKLSTAIALIGAAPV 2047
Cdd:cd03244 87 PV--LFSGtiRSNLDPFgeysdEELWQA----LERVGLKEfVESLPGGLDTVVEEGGenLSVGQRQLLCLARALLRKSKI 160
|
170
....*....|..
gi 1207110406 2048 IFLDEPTTGMDP 2059
Cdd:cd03244 161 LVLDEATASVDP 172
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1914-2058 |
2.47e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1914 LCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEKVH-QLMGYCPQFDAIIDLLTGRE----- 1987
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRElvaig 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 1988 HLEFYARLRGVPESYVEKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMD 2058
Cdd:PRK10575 110 RYPWHGALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1918-2058 |
2.59e-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: 46.32 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1918 IPRGECFGLLGVNGAGKTsTF-RMLTGDTRITYGEaflsnqsvLTEMEKVhqlmGYCPQFDAIIDLLTGREHLEFyARLR 1996
Cdd:COG1245 363 IREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGE--------VDEDLKI----SYKPQYISPDYDGTVEEFLRS-ANTD 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1997 GVPESYVEKVAqwgVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMD 2058
Cdd:COG1245 429 DFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
924-1096 |
2.67e-04 |
|
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: 43.68 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 924 VNHLNIKFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTAGTIYvkgmdirsdmdiirrtlgvCPQHnvlfdiltveE 1000
Cdd:cd03223 17 LKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGRIG-------------------MPEG----------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1001 HVWF-----YgrMKGMSLEEVnkemnsLL---EDVglqhkrfeqtknLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGVDP 1072
Cdd:cd03223 65 DLLFlpqrpY--LPLGTLREQ------LIypwDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....
gi 1207110406 1073 YSRRGIWDLLLKyrEGRTIILSTH 1096
Cdd:cd03223 125 ESEDRLYQLLKE--LGITVISVGH 146
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1899-2058 |
3.01e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.41 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1899 LSKVYKA-GRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVlTEMEKVHQLMGYCPQFD 1977
Cdd:PRK11000 6 LRNVTKAyGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1978 AIIDLLTGREHLEFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGM 2057
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
.
gi 1207110406 2058 D 2058
Cdd:PRK11000 165 D 165
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1910-2085 |
3.12e-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: 43.85 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1910 AVNRLCLGIPRGECFGLLGVNGAGKTStfrmLTGDTRITYGEAFLSnqSVLTEMEkvHQLMGYCPQFDAIIDLLTGrehl 1989
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKST----LVNEGLYASGKARLI--SFLPKFS--RNKLIFIDQLQFLIDVGLG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1990 efYARLrgvpesyvekvaqwgvqklglsqyaDREAGGYSGGNKRKLSTAIALIGAAP--VIFLDEPTTGMDPKAKRFLWN 2067
Cdd:cd03238 78 --YLTL-------------------------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170
....*....|....*...
gi 1207110406 2068 CILSVVKEGRSVVLTSHS 2085
Cdd:cd03238 131 VIKGLIDLGNTVILIEHN 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1886-1951 |
4.57e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 4.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1886 NGRALGDILI-LSDLSKVYkaGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG----DT-RITYGE 1951
Cdd:PRK11819 316 PGPRLGDKVIeAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGqeqpDSgTIKIGE 385
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1034-1116 |
6.34e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1034 FEQTKNLSGGMQRKLSVAIAFIGGSKVVVLDEPTagvdpysrRGIwDLLLKY----------REGRTIILSTHYMDEadL 1103
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPT--------RGI-DVGAKYeiytiinelaAEGKGVIVISSELPE--L 467
|
90
....*....|....*
gi 1207110406 1104 LG--DRIAIISQGKL 1116
Cdd:NF040905 468 LGmcDRIYVMNEGRI 482
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1903-2088 |
7.19e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.55 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1903 YKAGRKPAVNRLCLGIPRGEcFGLL-GVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLT-EMEKVHQLMGYCPQFDAII 1980
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1981 -DllTGREHLEFYARLRG-VPEsyvEKVAQWGVQKLGLSQYA-DREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGM 2057
Cdd:PRK10247 94 gD--TVYDNLIFPWQIRNqQPD---PAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|..
gi 1207110406 2058 DPKAKRFLWNCILSVVKEGRSVVL-TSHSMEE 2088
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLwVTHDKDE 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2028-2084 |
1.60e-03 |
|
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: 41.58 E-value: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207110406 2028 SGGNKRKLSTAIALIGAA----PVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:cd03227 79 SGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1928-2085 |
1.64e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1928 GVNGAGKTSTFRMLTGDTRITYGEAFLSNqsvlTEMEKVHQLmgYCPQFDAIIDL---LTGREHLEFYARLRGVPESyve 2004
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKN----CNINNIAKP--YCTYIGHNLGLkleMTVFENLKFWSEIYNSAET--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2005 kvAQWGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIGAAPVIFLDEPTTGMDPKAKRFLWNCILSVVKEGRSVVLTSH 2084
Cdd:PRK13541 104 --LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
.
gi 1207110406 2085 S 2085
Cdd:PRK13541 182 L 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1908-2086 |
1.98e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1908 KPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTGDtritygeaflsnqsvLTEMEK----VHQLMGYCPQFDAIIDLl 1983
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE---------------LSHAETssvvIRGSVAYVPQVSWIFNA- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1984 TGREHLEFYARLRgvPESYVEKVAQWGVQK-LGLSQYADREAGG-----YSGGNKRKLSTAIALIGAAPVIFLDEPTTGM 2057
Cdd:PLN03232 694 TVRENILFGSDFE--SERYWRAIDVTALQHdLDLLPGRDLTEIGergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180
....*....|....*....|....*....
gi 1207110406 2058 DPKAKRFLWNCILSVVKEGRSVVLTSHSM 2086
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQL 800
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
906-1123 |
2.51e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 906 GVSIRNLVKIYKkGAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGMDIrSDMDIIRRTLGV 985
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 986 CPQHNVLFDILTVEEHVwFYG-RMKGMSLEEVNK---EMNSLLEDVGLQHKRFEQtknLSGGmQRKlSVAI--AFIGGSK 1059
Cdd:PRK11650 81 VFQNYALYPHMSVRENM-AYGlKIRGMPKAEIEErvaEAARILELEPLLDRKPRE---LSGG-QRQ-RVAMgrAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207110406 1060 VVVLDEPTAGVDPYSR--------RgiwdllLKYREGRTIILSTHYMDEADLLGDRIAIISQGKLCCCGTPL 1123
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRvqmrleiqR------LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1893-2139 |
2.57e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAGR--KPAVNRLCLGIPRGECFGLLGVNGAGKT----STFRML-TGDTRITYGEAFLSNQSVLTEMEK 1965
Cdd:PRK15134 5 LLAIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1966 vhQLMGYCPQFDAII---------DLLTGREHL-EFYARLRGVPESYVEKVAQWGVQKLGLSQYADREAG---GYSGGNK 2032
Cdd:PRK15134 85 --TLRGVRGNKIAMIfqepmvslnPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 2033 RKLSTAIALIGAAPVIFLDEPTTGMD--PKAKrflwncILSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFQ 2105
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDvsVQAQ------ILQLLRElqqelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270
....*....|....*....|....*....|....
gi 1207110406 2106 CLGSVQHLKNRFGDGYTIILRLSTPSAEPCPVDA 2139
Cdd:PRK15134 237 EQNRAATLFSAPTHPYTQKLLNSEPSGDPVPLPE 270
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1926-2104 |
3.71e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1926 LLGVNGAGKTSTFRMLTGDTRITYGEAFLSNQSVLTEMEK---------VHQLMGYCPQFDAIIDLLTGR--------EH 1988
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengismVHQELNLVLQRSVMDNMWLGRyptkgmfvDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1989 LEFYARLRGVPESY------VEKVAqwgvqKLGLSQyadreaggysggnKRKLSTAIALIGAAPVIFLDEPTTGMDPKAK 2062
Cdd:PRK10982 109 DKMYRDTKAIFDELdididpRAKVA-----TLSVSQ-------------MQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207110406 2063 RFLWNCILSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2104
Cdd:PRK10982 171 NHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1022-1096 |
4.47e-03 |
|
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: 41.09 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1022 SLLEDVGLQHKRFEQTKN-LSGG-MQRklsVAIAFIGGSKVV----VLDEPTAGVDPYSRRGIWDLLLKYRE-GRTIILS 1094
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPtLSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVV 195
|
..
gi 1207110406 1095 TH 1096
Cdd:cd03270 196 EH 197
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
923-1096 |
4.67e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 923 AVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGL--FPP--TAGTIYVKGMDIRSDMDIIRRTL--------------G 984
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGrvMAEKLEFNGQDLQRISEKERRNLvgaevamifqdpmtS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 985 VCPQHNVLFDIL-TVEEHvwfygrmKGMSLEEVNKEMNSLLEDVGLQ--HKRFE-QTKNLSGGMQRKLSVAIAFIGGSKV 1060
Cdd:PRK11022 102 LNPCYTVGFQIMeAIKVH-------QGGNKKTRRQRAIDLLNQVGIPdpASRLDvYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1207110406 1061 VVLDEPTAGVDPYSRRGIWDLL--LKYREGRTIILSTH 1096
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLleLQQKENMALVLITH 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
928-1114 |
5.54e-03 |
|
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: 42.20 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 928 NIKFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTAGTIYVKGmdirsdmdiirrTLGVCPQ----------HNVLFDi 995
Cdd:TIGR01271 444 NISFKleKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQtswimpgtikDNIIFG- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 996 LTVEEHVwFYGRMKGMSLEE-----VNKEmNSLLEDVGLqhkrfeqtkNLSGGMQRKLSVAIAFIGGSKVVVLDEPTAGV 1070
Cdd:TIGR01271 511 LSYDEYR-YTSVIKACQLEEdialfPEKD-KTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207110406 1071 DPYSRRGIWD-LLLKYREGRTIILSTHYMDEADlLGDRIAIISQG 1114
Cdd:TIGR01271 580 DVVTEKEIFEsCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEG 623
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
919-965 |
5.69e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 5.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1207110406 919 GAKLAVNHLNIKFYEGQITSFLGHNGAGKTTTMSILTGLFPPTAGTI 965
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1894-2059 |
6.77e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.16 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1894 LILSDLSkvYKAGRKPAVNRLCLGIPRGECFGLLGVNGAGKTSTFRMLTG--DTRITY-GEAFLSNQSVLT-EMEKVHql 1969
Cdd:COG4136 2 LSLENLT--ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSAsGEVLLNGRRLTAlPAEQRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1970 MGYCPQfDaiiDLLTgrEHLEFYARLR-GVPESYV-----EKVAQwGVQKLGLSQYADREAGGYSGGNKRKLSTAIALIg 2043
Cdd:COG4136 78 IGILFQ-D---DLLF--PHLSVGENLAfALPPTIGraqrrARVEQ-ALEEAGLAGFADRDPATLSGGQRARVALLRALL- 149
|
170
....*....|....*..
gi 1207110406 2044 AAP-VIFLDEPTTGMDP 2059
Cdd:COG4136 150 AEPrALLLDEPFSKLDA 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1893-1966 |
9.58e-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: 41.21 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207110406 1893 ILILSDLSKVYKAG--RKPAVNRLCLGIPRGECFGLLGVNGAGKT----STFRMLTGDTRITYGEAFLSNQSVLT----E 1962
Cdd:COG4172 6 LLSVEDLSVAFGQGggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlserE 85
|
....
gi 1207110406 1963 MEKV 1966
Cdd:COG4172 86 LRRI 89
|
|
| |
