|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
179-1866 |
1.89e-131 |
|
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: 459.48 E-value: 1.89e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 179 ETFVKL-GVL---LCGHPFPNTDTIPLVNEIlesEDFSQANDAEIDAmpTRRRRRYEdlpTDWRPTKYCKRLYRDVTSTN 254
Cdd:TIGR01257 310 ETFTQLmGILsdlLCGYPEGGGSRVFSFNWY---EDNNYKAFLGIDS--TRKDPIYS---YDKRTTSFCNALIQSLESNP 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 255 QGKLTWNTIKPIIQGRILYTPANAMTESVVKFSNASFEELDRLKQLSRAAATILTKL---HTNATFQEAFDNLLKlakSP 331
Cdd:TIGR01257 382 LTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIwyfFDKSTQMTMIRDTLQ---NP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 332 LVKSLVgdDFDIGE----IERVFEYI----RTNQL----------IYDI----LTTVADLMDCVSADRFEAVESVEELHK 389
Cdd:TIGR01257 459 TVKDFI--NRQLGEegitAEAVLNFLyngpREKQAddmtnfdwrdIFNItdrfLRLANQYLECLVLDKFESYDDEVQLTQ 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 390 RAYELNQNKLFLAALNLEDVGLKQAS------YRLHMDTDNTQPTFENRNRFWFPGPADSMVIDLKY-HRGFVQLKQMVD 462
Cdd:TIGR01257 537 RALSLLEENRFWAGVVFPDMYPWTSSlpphvkYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYiWGGFAYLQDMVE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 463 LGIIKSKREEAgfapeedgpesgrslsglfsikqvendtpdeddddfdlsleesgdekaAPkvsasasdheattispssl 542
Cdd:TIGR01257 617 QGITRSQMQAE------------------------------------------------PP------------------- 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 543 dgvtteevrvtteqtvvsgdpdllllknedvlkrskrqglfdllggfggsgdankknkfevdnMQFYTKQFPYPAFLNDV 622
Cdd:TIGR01257 630 ---------------------------------------------------------------VGIYLQQMPYPCFVDDS 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 623 FKrgLYLAQGVQVAYLLGLVVFVALSVRERIWMRESRNSMLMRSMGLKAHSELVAWALMSFLELCVIFALISGVLYSGGI 702
Cdd:TIGR01257 647 FM--IILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRI 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 703 LGYTNWFFMMFYCLSFGLCLISFCYMCTNFFNSANIGAVASALLFFISLCPFIIVLMFDAKLSVFESFLVDLSFTTAFAK 782
Cdd:TIGR01257 725 LHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGF 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 783 GWGELIRMELQQEGLTVRHLIQVGPARSECA--MALLMFLLDLLLYAVIGLAYQRYKKNNYS-----FVKVSRSQLDGKL 855
Cdd:TIGR01257 805 GTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSflLSMKMMLLDAALYGLLAWYLDQVFPGDYGtplpwYFLLQESYWLGGE 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 856 GAS----------------------------------------------LVNVSKLYGsKCAVSNLSLDFARNQVSCLLG 889
Cdd:TIGR01257 885 GCStreeralekteplteemedpehpegindsfferelpglvpgvcvknLVKIFEPSG-RPAVDRLNITFYENQITAFLG 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 890 RNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNILIPTLTAREHLQLYAQIKippGGSGgvEEI 959
Cdd:TIGR01257 964 HNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrQSLGMCPQHNILFHHLTVAEHILFYAQLK---GRSW--EEA 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 960 RSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATH 1039
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH 1118
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1040 FMDEAKYLSDSLVIMRNGRIIA--------------------------QHSRDSLQRLCT-SNYSIRLRCA--------- 1083
Cdd:TIGR01257 1119 HMDEADLLGDRIAIISQGRLYCsgtplflkncfgtgfyltlvrkmkniQSQRGGCEGTCScTSKGFSTRCParvdeitpe 1198
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1084 -------------------DATGVTFVIQKAQQLLPQTQVTHSGAADYPHSLTIN------ASYAEHLTPGAVEFLELLQ 1138
Cdd:TIGR01257 1199 qvldgdvnelmdlvyhhvpEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETladlglSSFGISDTPLEEIFLKVTE 1278
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1139 SqVTAGSIsdveltTSSSLEQEFEQLNRNGEDAGPRR--------PASDRSGVVAGPAMITDEPPTACKQFRL------- 1203
Cdd:TIGR01257 1279 D-ADSGSL------FAGGAQQKRENANLRHPCSGPTEkagqtpqaSHTCSPGQPAAHPEGQPPPEPEDPGVPLntgarli 1351
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1204 ------LMGKRLRHLSRNYRLLLYVLLLPALFELCAM-------------------WFVSYR------------------ 1240
Cdd:TIGR01257 1352 lqhvqaLLVKRFQHTIRSHKDFLAQIVLPATFVFLALmlsiiippfgeypaltlhpWMYGQQytffsmdepnsehlevla 1431
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1241 -------------LEDDFDTVLPL-------SRSLYPQTAQFLSHERAT----------SFSEKLY-------------P 1277
Cdd:TIGR01257 1432 dvllnkpgfgnrcLKEEWLPEYPCgnstpwkTPSVSPNITHLFQKQKWTaahpspscrcSTREKLTmlpecpegagglpP 1511
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1278 QLRT--SCDHLGECRVFNTSQ---QSYDWVLNS------WgeYSERRYGGYGLNG------------------------- 1321
Cdd:TIGR01257 1512 PQRTqrSTEILQDLTDRNISDflvKTYPALIRSslkskfW--VNEQRYGGISIGGklpaipitgealvgflsdlgqmmnv 1589
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1322 SGA-----------------------TVWYNNKGYHSMMAWLNDLNSELLRTTM----NDSESSILTLNEPWKLGFAELS 1374
Cdd:TIGR01257 1590 SGGpvtreaskempdflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLpkdrDPEEYGITVISQPLNLTKEQLS 1669
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1375 TSSILRQAGDGSMVFILLIAFGLVVASGSVYLVNERVNGEKLQQRLCGVSAVTYWLVALVWDYLVMVLGLIVCLVVILMF 1454
Cdd:TIGR01257 1670 EITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGF 1749
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1455 GMPVFVDRQQLVGIIGLSLAFSFACVPSVHVAEKIFSDSSIAIVSIFCANLIVPLVTMGIILILGVVGDGPAWDDWRHAL 1534
Cdd:TIGR01257 1750 QKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAML 1829
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1535 NQAFLIFPIHALGDGFLELCKNYMVALVFRRYDIDSYKHPLASDLLGRHFTALLLVGVAALIINVLIEWHLLRRLW---Q 1611
Cdd:TIGR01257 1830 RKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWiaeP 1909
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1612 RVERLLDctyrrELDKLGQLKlvniQSIFKSCVDTgEAVRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKS 1690
Cdd:TIGR01257 1910 AKEPIFD-----EDDDVAEER----QRIISGGNKT-DILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKT 1979
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1691 TIFKLLTGQLQPDVG-----------QIYFEQPGISYCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYE 1757
Cdd:TIGR01257 1980 TTFKMLTGDTTVTSGdatvagksiltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVpaEEIEKVANWSIQSLG 2059
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1758 LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQR 1837
Cdd:TIGR01257 2060 LSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTR 2139
|
2010 2020
....*....|....*....|....*....
gi 113193620 1838 VAVLRAGQVIASDSPQRLKSEHGGYYAVT 1866
Cdd:TIGR01257 2140 LAIMVKGAFQCLGTIQHLKSKFGDGYIVT 2168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1650-1856 |
2.75e-81 |
|
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: 266.68 E-value: 2.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYC 1717
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIRFYGRLRGIRDLDQFL--DRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1795
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEevELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1796 TSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1856
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
858-1072 |
6.96e-69 |
|
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: 231.24 E-value: 6.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQ-VGVCW 925
Cdd:cd03263 2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaaRQsLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQIKippGGSggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:cd03263 82 QFDALFDELTVREHLRFYARLK---GLP--KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQhsrDSLQRLC 1072
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCI---GSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
861-1070 |
2.87e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 213.00 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNIL 930
Cdd:COG1131 5 GLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKippGGSGgvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:COG1131 85 YPDLTVRENLRFFARLY---GLPR--KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1011 NGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG1131 160 SGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1650-1859 |
7.74e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.99 E-value: 7.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYCP 1718
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvaRDPAevrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1796
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1797 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
858-1059 |
2.93e-54 |
|
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: 187.60 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 927
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLyaqikippggsggveeirsevaqtlqslnfgkhesypswqlSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:cd03230 82 PSLYENLTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1008 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
861-1075 |
5.98e-53 |
|
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: 186.60 E-value: 5.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH----------QVGVCWQDNIL 930
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkeprearrQIGVLPDERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:COG4555 86 YDRLTVRENIRYFAELYGLFD-----EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1011 NGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL-QRLCTSN 1075
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELrEEIGEEN 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1651-1860 |
5.75e-46 |
|
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: 166.57 E-value: 5.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQP-----GISYCPQ 1719
Cdd:COG4555 3 EVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrKEPrearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHG 1860
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
861-1062 |
3.52e-44 |
|
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: 160.08 E-value: 3.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDNILI 931
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTAREHLQLYAQIKIPPggsggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:cd03268 85 PNLTARENLRLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1012 GVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03268 156 GLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1650-1856 |
2.25e-41 |
|
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: 152.52 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLwlAYRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYC 1717
Cdd:cd03265 1 IEVENL--VKKYGDFeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvREPRevrrrIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVL-MDE 1794
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-RPEVLfLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1795 PTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1856
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1650-1846 |
4.97e-41 |
|
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: 149.47 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYCP 1718
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLgkdikkepeevKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECIRfygrlrgirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:cd03230 80 EEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
861-1069 |
7.59e-41 |
|
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: 150.98 E-value: 7.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQDNIL 930
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPG-----AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1011 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1069
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
861-1062 |
1.69e-39 |
|
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: 147.09 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDn 928
Cdd:COG1122 5 NLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrRKVGLVFQN- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 iliPtltarEHlQLYA------------QIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 996
Cdd:COG1122 84 ---P-----DD-QLFAptveedvafgpeNLGLPR------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
858-1066 |
3.60e-39 |
|
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: 146.08 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSK----CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVGVCWQD 927
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIKIPPGGsggveEIRSEVAQTLQSLNFGKHE-SYPsWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:cd03293 82 DALLPWLTVLDNVALGLELQGVPKA-----EARERAEELLELVGLSGFEnAYP-HQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIAQHSRD 1066
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
858-1062 |
1.35e-38 |
|
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: 143.87 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFArNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ----------VGVCWQD 927
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkqpqklrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIK-IPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKgIPSK------EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
858-1039 |
1.49e-38 |
|
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: 143.77 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 927
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG4133 84 DGLKPELTVRENLRFWAALY-------GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 113193620 1008 EPCNGVDAKARKDIWQLIER-LRQGRAVIFATH 1039
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
858-1058 |
4.26e-38 |
|
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: 140.46 E-value: 4.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniliptltar 937
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 ehlqlyaqikipPGGSGGVEEIRSEVAQTlqslnfgkhesypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:cd00267 62 ------------DIAKLPLEELRRRIGYV--------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1018 RKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:cd00267 116 RERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1661-1885 |
4.82e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.90 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1661 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-----------FEQPGISYCPQSNPLDPLLTT 1729
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpararLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1730 TECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMV 1807
Cdd:PRK13536 132 RENLLVFGRYFGMstREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1808 YATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVTCFCG-PAQQAILSRSLNQRL 1885
Cdd:PRK13536 212 WERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGdPHELSSLVKPYARRI 290
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1650-1848 |
1.16e-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: 141.26 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPG--------ISYCPQSN 1721
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnrIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 PLDPLLTTTECIRFYGRLRG--IRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1799
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1800 DPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
859-1061 |
2.90e-37 |
|
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: 140.35 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDNI 929
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvppERrnIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLyaqikipPGGSGGV--EEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:cd03259 83 LFPHLTVAENIAF-------GLKLRGVpkAEIRARVRELLELVGLEGLLNrYPH-ELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
858-1058 |
1.93e-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: 137.98 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGS--KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVC 924
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQD---NILIPTLT-----AREHLQLyaqikiPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 996
Cdd:cd03225 81 FQNpddQFFGPTVEeevafGLENLGL------PE------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1650-1855 |
2.10e-36 |
|
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: 138.23 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS--------- 1720
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD--GKDITKKNlrelrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ----NPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvtccgctpTVL- 1791
Cdd:COG1122 79 lvfqNPDDQLFAPTveEDVAFGPENLGLprEEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA--------GVLa 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1792 -------MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:COG1122 151 mepevlvLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
858-1081 |
3.25e-36 |
|
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: 138.40 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGS----KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVG 922
Cdd:COG1124 3 EVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQD--NILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKH--ESYPSwQLSGGYRRRLCVAIAFI 998
Cdd:COG1124 83 MVFQDpyASLHPRHTVDRILAEPLRIH-------GLPDREERIAELLEQVGLPPSflDRYPH-QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQRLCTSNY 1076
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*
gi 113193620 1077 SIRLR 1081
Cdd:COG1124 235 TRELL 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
858-1061 |
9.64e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.53 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVGVCWQD 927
Cdd:COG1116 9 ELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIKippggsgGV--EEIRSEVAQTLQSLNFGKHE-SYPsWQLSGGYRRRlcVAIA--FIASPS 1002
Cdd:COG1116 89 PALLPWLTVLDNVALGLELR-------GVpkAERRERARELLELVGLAGFEdAYP-HQLSGGMRQR--VAIAraLANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIA 1061
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
858-1070 |
1.19e-35 |
|
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: 136.48 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGV 923
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 924 CWQDNILIPTLTA--------REHLQLYAqikippggsggvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVA 994
Cdd:cd03261 82 LFQSGALFDSLTVfenvafplREHTRLSE------------EEIREIVLEKLEAVGLrGAEDLYPA-ELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 995 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1662-1937 |
1.36e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.32 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-------GISYCPQSNPLDPLLTTTECI 1733
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgEPldpedrrRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1734 RFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRK--LTVAVTccgCTPTVL-MDEPTSDMDPVTRDMvy 1808
Cdd:COG4152 93 VYLARLKGLskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKvqLIAALL---HDPELLiLDEPFSGLDPVNVEL-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1809 atIEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGG-YYAVTCfcgPAQQAILsrslnQ 1883
Cdd:COG4152 168 --LKDVIRELAAkgttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRnTLRLEA---DGDAGWL-----R 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1884 RLPGARDLQHYAHSLRFLVrvrsPGSLGDAPLLSELFAIlcdvcVNVARFSLSR 1937
Cdd:COG4152 238 ALPGVTVVEEDGDGAELKL----EDGADAQELLRALLAR-----GPVREFEEVR 282
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1650-1840 |
1.63e-35 |
|
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: 134.91 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAyRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI-----------SYCP 1718
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHlCQRVAV 1840
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA-ARVLDL 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1663-1860 |
1.69e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.40 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1663 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF---EQPG--------ISYCPQSNPLDPLLTTTE 1731
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgePVPSrarharqrVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFYGRLRG-----IRDLDQFLdrvLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDM 1806
Cdd:PRK13537 100 NLLVFGRYFGlsaaaARALVPPL---LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1807 VYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL-KSEHG 1860
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIG 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
858-1062 |
4.87e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 136.86 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 927
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIKippGGSGGveEIRSEVAQTLQslnFGKHES---YPSWQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:PRK13537 89 DNLDPDFTVRENLLVFGRYF---GLSAA--AARALVPPLLE---FAKLENkadAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1005 ILDEPCNGVDAKARKDIWqliERLR----QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMW---ERLRsllaRGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1649-1853 |
6.12e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPG------ISYCPQSN 1721
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPrrarrrIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 PLDPLLTTT--ECIR--FYGR---LRGIRDLD-QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1793
Cdd:COG1121 85 EVDWDFPITvrDVVLmgRYGRrglFRRPSRADrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1794 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLrAGQVIASDSPQ 1853
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
861-1068 |
7.71e-35 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 133.96 E-value: 7.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNIL 930
Cdd:TIGR03864 6 GLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHdlrrapraalARLGVVFQQPTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKippGGSGGVEEIRSEVAQTLQSLNFGKHEsyPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:TIGR03864 86 DLDLSVRQNLRYHAALH---GLSRAEARARIAELLARLGLAERADD--KVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1011 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALarDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1652-1849 |
1.58e-33 |
|
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: 129.62 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLWLAYRRGHyAVRNVNFSVQRGeCFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYCPQS 1720
Cdd:cd03264 3 LENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQklrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIpsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1799 MDPVTRdMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:cd03264 161 LDPEER-IRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
859-1058 |
2.07e-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: 128.07 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCW 925
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLyaqikippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:cd03229 83 QDFALFPHLTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1648-1852 |
2.60e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1648 EAVRAENLWLAYRRGH---------------------YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQ 1706
Cdd:COG1134 3 SMIEVENVSKSYRLYHepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1707 IyfeqpgISYCPQSNPL------DPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLT 1778
Cdd:COG1134 83 V------EVNGRVSALLelgagfHPELTGRENIYLNGRLLGLsrKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1779 VAV-TCcgCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1852
Cdd:COG1134 157 FAVaTA--VDPDILlVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
858-1060 |
3.04e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.91 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDN 928
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppEKrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQ--LYAQiKIPPggsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA--FIASPSV 1003
Cdd:COG3842 87 ALFPHLTVAENVAfgLRMR-GVPK------AEIRARVAELLELVGLEGLADrYPH-QLSGGQQQR--VALAraLAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
858-1062 |
3.51e-33 |
|
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: 126.77 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniLIPTLTAR 937
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-----------EVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 EHLQLyaqikippggsgGVEEIrsevaqtlqslnfgkhesypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:cd03216 71 DARRA------------GIAMV---------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1018 RKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03216 118 VERLFKVIRRLRaQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
861-1060 |
3.66e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH--------------QVGVCW 925
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipylrrRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLN-FGKHESYPSwQLSGGYRRRLCVAIAFIASPSV 1003
Cdd:COG2884 86 QDFRLLPDRTVYENVALPLRVtGKSR------KEIRRRVREVLDLVGlSDKAKALPH-ELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATH---FMDEAKYlsdSLVIMRNGRII 1060
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHdleLVDRMPK---RVLELEDGRLV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1651-1853 |
4.82e-33 |
|
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: 128.71 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------QP------GISYC 1717
Cdd:cd03219 2 EVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPheiarlGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIR------------FYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCG 1785
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1786 CTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
858-1062 |
5.59e-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: 129.39 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 926
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelaRRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTARE--------HLQLYAQIKippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 998
Cdd:COG1120 83 EPPAPFGLTVRElvalgrypHLGLFGRPS---------AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
861-1062 |
5.62e-33 |
|
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: 128.71 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVC--WQDN 928
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppHEIarlGIGrtFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQIK-----IPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 1003
Cdd:cd03219 85 RLFPELTVLENVMVAAQARtgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
858-1070 |
7.42e-33 |
|
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: 128.56 E-value: 7.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGV 923
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 924 CWQDNILIPTLTAREHLQ--LYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA--FI 998
Cdd:COG1127 87 LFQGGALFDSLTVFENVAfpLREHTDLSE------AEIRELVLEKLELVGLPGAADkMPS-ELSGGMRKR--VALAraLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
858-1062 |
1.06e-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: 126.01 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTAR 937
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-----------LASLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 EHLQlyaqikippggsggveeIRSEVAQTLQSLNFG--KHESYpsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 1015
Cdd:cd03214 70 ELAR-----------------KIAYVPQALELLGLAhlADRPF--NELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1016 KARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03214 131 AHQIELLELLRRLarERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
859-1062 |
1.07e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 131.11 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDN 928
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlarARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYaqikippGGSGGVEEIRSE-VAQTLqsLNFGKHES---YPSWQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:PRK13536 124 NLDLEFTVRENLLVF-------GRYFGMSTREIEaVIPSL--LEFARLESkadARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1005 ILDEPCNGVDAKARKDIWqliERLR----QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIW---ERLRsllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
861-1070 |
1.41e-32 |
|
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: 127.80 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDN 928
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelrRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKHE---SYPsWQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:cd03295 85 GLFPHMTVEENIALVPKLlKWPK------EKIRERADELLALVGLDPAEfadRYP-HELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
861-1062 |
1.90e-32 |
|
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: 127.85 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVC--WQDN 928
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglppHRIarlGIArtFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQIKIPPGGSGGV----------EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 998
Cdd:COG0411 89 RLFPELTVLENVLVAAHARLGRGLLAALlrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
858-1068 |
1.95e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 134.26 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------- 918
Cdd:COG1123 262 EVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 HQVGVCWQD--NILIPTLTAREH----LQLYaqikippgGSGGVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRR 990
Cdd:COG1123 342 RRVQMVFQDpySSLNPRMTVGDIiaepLRLH--------GLLSRAERRERVAELLERVGLPPDlaDRYP-HELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 991 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
861-1062 |
2.09e-32 |
|
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: 126.24 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQVGVCWQDNILIPT 933
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarNRIGYLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLQLYAQIK-IPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:cd03269 85 MKVIDQLVYLAQLKgLKK------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1013 VDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1650-1849 |
2.71e-32 |
|
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: 126.33 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYR---RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-----GIS 1715
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkEPaearrRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1716 YCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1793
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLkgDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1794 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
858-1064 |
2.98e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 126.31 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSK----CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 918
Cdd:COG1136 6 ELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 HQVGVCWQDNILIPTLTAREhlqlyaQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF 997
Cdd:COG1136 86 RHIGFVFQFFNLLPELTALE------NVALPLLLAGvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHS 1064
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
858-1059 |
3.19e-32 |
|
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: 126.07 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 918
Cdd:cd03255 2 ELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 HQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAF 997
Cdd:cd03255 82 RHIGFVFQSFNLLPDLTALENVELPLLLAGVPK-----KERRERAEELLERVGLGDRLNhYPS-ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYlSDSLVIMRNGRI 1059
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
861-1062 |
9.07e-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: 124.93 E-value: 9.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVG 922
Cdd:cd03257 6 NLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQD--NILIPTLTAREHLQ--LYAQikippGGSGGVEEIRSEVAQTLQSLNFGKH--ESYPSwQLSGGYRRRLCVAIA 996
Cdd:cd03257 86 MVFQDpmSSLNPRMTIGEQIAepLRIH-----GKLSKKEARKEAVLLLLVGVGLPEEvlNRYPH-ELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1229-1600 |
1.20e-31 |
|
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: 128.28 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1229 FELCAMWFVSYRLEDDFDT---VLPLSRS-LYPQTAQFLSHERATSFSEKlypqlrtscdhlgecrvFNTSQQSYDWVLN 1304
Cdd:pfam12698 14 LILLLGLIFSNAVNDPEELpvaVVDEDNSsLSRQLVRALEASPTVNLVQY-----------------VDSEEEAKEALKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1305 SWGEYSERRYGGYGLN-----GSGATVWYNNKGYHSMMAWLNDLNSELLRTTMNDSESSILTLNEPWKLGFAELSTSSIL 1379
Cdd:pfam12698 77 GKIDGLLVIPKGFSKDllkgeSATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1380 RQAGDGSMVFILLIAFGLVVASGSVYLVNERVNGEKLQQRLCGVSAVTYWLVALVWDYLVMVLGLIVCLvvILMFGMPVF 1459
Cdd:pfam12698 157 SGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL--LLLFGIGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1460 VDrqQLVGIIGLSLAFSFACVPSVHVAEKIFSDSSIAIVSIFCANLIVplvtMGIILILGVVGDGPAWddwrhaLNQAFL 1539
Cdd:pfam12698 235 FG--NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLL----SGFFGGLFPLEDPPSF------LQWIFS 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1540 IFPIHALGDGFLELCKNYmvalvfrrydidsykhPLASdlLGRHFTALLLVGVAALIINVL 1600
Cdd:pfam12698 303 IIPFFSPIDGLLRLIYGD----------------SLWE--IAPSLIILLLFAVVLLLLALL 345
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1651-1845 |
1.21e-31 |
|
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: 124.12 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1720
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 --NPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDE 1794
Cdd:cd03225 81 fqNPDDQFFGPTveEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1795 PTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
858-1059 |
4.02e-31 |
|
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: 123.12 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDN 928
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPK-----AEIKERVAEALDLVQLEGYANrKPS-QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1008 EPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
858-1066 |
4.03e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqVGVCWQD---------- 927
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-PRRARRRigyvpqraev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPtLTAREHLQLYAQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG1121 87 DWDFP-ITVRDVVLMGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1008 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMrNGRIIAQHSRD 1066
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1651-1850 |
4.15e-31 |
|
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: 122.64 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-------EQPGISYCPQSNPL 1723
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DPL--LTTTECI--RFYGRLRGIRDLD----QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1795
Cdd:cd03235 80 DRDfpISVRDVVlmGLYGHKGLFRRLSkadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1796 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLrAGQVIASD 1850
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
858-1061 |
8.02e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQD 927
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprERRVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLN---FGKHesYPSwQLSGGYRRRlcVAIA--FIASPS 1002
Cdd:COG1118 84 YALFPHMTVAENIAFGLRVRPPSK-----AEIRARVEELLELVQlegLADR--YPS-QLSGGQRQR--VALAraLAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1665-1853 |
2.35e-30 |
|
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: 121.68 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTE 1731
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglpphriaRLGIARTFQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CI-----------------RFYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVLM-D 1793
Cdd:COG0411 99 NVlvaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT-EPKLLLlD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1794 EPTSDMDPV-TRDMVyATIEQLllaRR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:COG0411 178 EPAAGLNPEeTEELA-ELIRRL---RDergiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1651-1845 |
2.65e-30 |
|
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: 118.12 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpldpllttt 1730
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 ecirfygRLRGIRDLDQfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1810
Cdd:cd00267 71 -------LRRRIGYVPQ---------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 113193620 1811 IEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:cd00267 123 LRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
858-1068 |
3.09e-30 |
|
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: 120.23 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVCW-- 925
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppHERaraGIGYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQIKIPPGGSGGVEEI----------RSEVAQTlqslnfgkhesypswqLSGGYRRRLCVAI 995
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfprlkerRKQLAGT----------------LSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1662-1849 |
3.60e-30 |
|
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: 119.63 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLD------------PLLTT 1729
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD--GKSYQKNIEALRrigalieapgfyPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1730 TECIRFYGRLRGIRDLDQflDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPV-TRDMvy 1808
Cdd:cd03268 90 RENLRLLARLLGIRKKRI--DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDgIKEL-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1809 atiEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:cd03268 166 ---RELILSLRDqgitVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
861-1062 |
6.14e-30 |
|
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: 119.18 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVG-VCWQDNIL--I 931
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGyVPQRRSIDrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PtLTAREHLQLYAQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:cd03235 84 P-ISVRDVVLMGLYGHKGLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1012 GVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSlVIMRNGRIIAQ 1062
Cdd:cd03235 162 GVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDR-VLLLNRTVVAS 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
860-1060 |
8.02e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 119.75 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNIL 930
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKiPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEP 1009
Cdd:cd03296 86 FRHMTVFDNVAFGLRVK-PRSERPPEAEIRAKVHELLKLVQLdWLADRYPA-QLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1010 CNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1650-1850 |
1.31e-29 |
|
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: 118.40 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGH---------------------YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY 1708
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1709 --------FEqPGISycpqsnpLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLT 1778
Cdd:cd03220 81 vrgrvsslLG-LGGG-------FNPELTGRENIYLNGRLLGLsrKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1779 VAV-TCCGCtPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1850
Cdd:cd03220 153 FAIaTALEP-DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
858-1070 |
1.53e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.60 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQVGVCWQDNI-------- 929
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPEDRRRIgylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLYAQIKippggsgGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG4152 82 LYPKMKVGEQLVYLARLK-------GLskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1008 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
858-1060 |
2.25e-29 |
|
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: 118.05 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI-----RQSSGKVLLAGE-------------H 919
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 920 QVGVCWQdnilIPTLTareHLQLYAQIKIPP--GGSGGVEEIRSEVAQTLQSLNFGKHESYPSW--QLSGGYRRRLCVAI 995
Cdd:cd03260 82 RVGMVFQ----KPNPF---PGSIYDNVAYGLrlHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
858-1068 |
2.84e-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: 118.03 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH----------QVGVCW-- 925
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkraRLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSK-----KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
858-1071 |
3.01e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.36 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCW 925
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQikipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRrlCVAI--AFIASP 1001
Cdd:COG1129 86 QELNLVPNLSVAENIFLGRE----PRRGGLIdwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ--LVEIarALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1002 SVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH-----SRDSLQRL 1071
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1649-1853 |
3.01e-29 |
|
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: 118.61 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG--------------I 1714
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--GrdlaslsrrelarrI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1715 SYCPQSNPLDPLLTTTECIRfYGRLRGIRDLDQF-------LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1787
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVA-LGRYPHLGLFGRPsaedreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1788 PTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHsvsEIEH---LCQRVAVLRAGQVIASDSPQ 1853
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLH---DLNLaarYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
859-1059 |
3.83e-29 |
|
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: 116.97 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNI 929
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkDRDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPK-----DEIDERVREVAELLQIEHLlDRKPK-QLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1009 PCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
871-1061 |
7.72e-29 |
|
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: 116.31 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQDNILIPTLTAREHL 940
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaeaRRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYaqikippGGSGGVE--EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:cd03266 100 EYF-------AGLYGLKgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1019 KDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:cd03266 173 RALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1650-1855 |
1.44e-28 |
|
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: 115.72 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ------P-------GISY 1716
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPmhkrarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1717 CPQSNPLDPLLTTTECIR----FYGRLRGIRdlDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM 1792
Cdd:cd03218 80 LPQEASIFRKLTVEENILavleIRGLSKKER--EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIA-RALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1793 -DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:cd03218 157 lDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1662-1849 |
1.63e-28 |
|
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: 113.29 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPqSNPLDplltttecirfyGRLRG 1741
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--GKEVSF-ASPRD------------ARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1742 IRDLDQfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAV 1821
Cdd:cd03216 77 IAMVYQ---------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180
....*....|....*....|....*...
gi 113193620 1822 VLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:cd03216 136 IFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1651-1858 |
2.47e-28 |
|
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: 114.84 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-------GISYC 1717
Cdd:cd03224 2 EVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditgLPpheraraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTY-ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVLM- 1792
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIAralMS----RPKLLLl 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1793 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1650-1847 |
5.83e-28 |
|
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: 114.14 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------Q 1711
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1712 PGISYCPQsNP---LDPLLTT----TECIRFYGR--------------LRGIRDLDQFLDRvldtyelRPYKdvqvrnLS 1770
Cdd:cd03257 82 KEIQMVFQ-DPmssLNPRMTIgeqiAEPLRIHGKlskkearkeavlllLVGVGLPEEVLNR-------YPHE------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1771 GGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDPVTRdmvyATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAG 1844
Cdd:cd03257 148 GGQRQRVAIARALA-LNPKLLIaDEPTSALDVSVQ----AQILDLLkkLQEElglTLLFITHDLGVVAKIADRVAVMYAG 222
|
...
gi 113193620 1845 QVI 1847
Cdd:cd03257 223 KIV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
861-1070 |
8.78e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.57 E-value: 8.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQV-------GVCWQDNI 929
Cdd:COG4525 8 HVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVtgpgadrGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLYAQIKippggsgGVE--EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG4525 87 LLPWLNVLDNVAFGLRLR-------GVPkaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1008 EPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIAQHSRDSLQR 1070
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLELDFSRR 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1645-1855 |
1.10e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 120.01 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAVRAENLWLAY----RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------- 1710
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklsrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1711 -----QPGISYCPQsNP---LDPLLTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRP-YKDVQVRNLSGGNRRKLT 1778
Cdd:COG1123 336 slrelRRRVQMVFQ-DPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVaelLERVGLPPdLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1779 VA---VTccgcTPTVLM-DEPTSDMDPVtrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:COG1123 415 IAralAL----EPKLLIlDEPTSALDVS----VQAQILNLLrdLQRElglTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
....*.
gi 113193620 1850 DSPQRL 1855
Cdd:COG1123 487 GPTEEV 492
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
874-1060 |
1.49e-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: 111.97 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----HQVGVCW---QD-NILIPTLTAREhlQLYA 944
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakERRKSIGyvmQDvDYQLFTDSVRE--ELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 945 QIKIPPGGSGGVEEIrsevaqtLQSLN-FGKHESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1023
Cdd:cd03226 96 GLKELDAGNEQAETV-------LKDLDlYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 113193620 1024 LIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03226 168 LIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
858-1070 |
2.07e-27 |
|
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: 119.48 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---HQVGVCWQDNI---- 929
Cdd:COG4988 338 ELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsDLDPASWRRQIawvp 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 ---LIPTLTAREHLQLYAqikipPGGSGgvEEIRSEVAQT-----LQSLNFGKH----ESypSWQLSGGYRRRLCVAIAF 997
Cdd:COG4988 418 qnpYLFAGTIRENLRLGR-----PDASD--EELEAALEAAgldefVAALPDGLDtplgEG--GRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLA 560
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
860-1068 |
2.41e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.85 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS---SGKVLLAGE-----------HQVGVCW 925
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsealrgRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QD--NILIPtLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 1003
Cdd:COG1123 90 QDpmTQLNP-VTVGDQIAEALENLGLSR-----AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
858-1059 |
1.23e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH---------QVGVCWQDN 928
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRlcVAI--AFIASPSVV 1004
Cdd:COG3839 85 ALYPHMTVYENIAFPLKLrKVPK------AEIDRRVREAAELLGLEDLlDRKPK-QLSGGQRQR--VALgrALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1005 ILDEPCNGVDAKARkdiWQLIERLRQ-----GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:COG3839 156 LLDEPLSNLDAKLR---VEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
874-1062 |
1.30e-26 |
|
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: 109.69 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARN-QVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------------EHQVGVCWQDNILIPTLTAR 937
Cdd:cd03297 14 TLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 EHLqLYAQIKIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:cd03297 94 ENL-AFGLKRKRNR------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1018 RKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
872-1011 |
4.46e-26 |
|
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: 105.81 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTLTAREHL 940
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 941 QLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFG----KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:pfam00005 81 RLGLLLKGLSK-----REKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1666-1797 |
7.52e-26 |
|
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: 105.04 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQSNPLDPLLTTTECI 1733
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1734 RFYGRLRGI--RDLDQFLDRVLDTYELRPYKD----VQVRNLSGGNRRKLTVAVTCCgCTPTVL-MDEPTS 1797
Cdd:pfam00005 81 RLGLLLKGLskREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALL-TKPKLLlLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
866-1068 |
7.95e-26 |
|
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: 108.15 E-value: 7.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVCW--QDNILIPT 933
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglppHRIarlGIGYvpEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLQLYAQikiPPGGSGGVEEIRSEVAQTLQSLnfGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGV 1013
Cdd:COG0410 93 LTVEENLLLGAY---ARRDRAEVRADLERVYELFPRL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1014 DAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG0410 168 APLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
871-1070 |
8.01e-26 |
|
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: 114.86 E-value: 8.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREH 939
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrRRIAVVPQRPHLFDT-TLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 940 LQLYAqikipPGGSggvEEirsEVAQTLQSLNFGKH-ESYP----SW------QLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:COG4987 429 LRLAR-----PDAT---DE---ELWAALERVGLGDWlAALPdgldTWlgeggrRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1009 PCNGVDAKARKDIWQLIERLRQGRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGRTVLLITHrlaGLERM----DRILVLEDGRIVEQGTHEELLA 558
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1651-1847 |
1.75e-25 |
|
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: 106.19 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS---------YCPQsN 1721
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksigYVMQ-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 PLDPLLTTT---ECirfygrLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVT-CCGCtPTVLMDE 1794
Cdd:cd03226 80 VDYQLFTDSvreEL------LLGLKELDAGNEQaetVLKDLDLYALKERHPLSLSGGQKQRLAIAAAlLSGK-DLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1795 PTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1651-1853 |
1.83e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ------P-------GISYC 1717
Cdd:COG1137 5 EAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQsnplDPL----LTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPT-V 1790
Cdd:COG1137 84 PQ----EASifrkLTVEDNILAVLELRKLskKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA-RALATNPKfI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1791 LMDEPTSDMDPVT----RDMVYAtieqllLARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKIIRH------LKERgiGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
861-1062 |
2.41e-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: 106.59 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------H---QVGVCW--QDN 928
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmHeraRLGIGYlpQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQ--LYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:TIGR04406 86 SIFRKLTVEENIMavLEIRKDLDR------AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAE 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
858-1062 |
3.51e-25 |
|
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: 106.13 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG--------------EH 919
Cdd:cd03258 3 ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 920 QVGVCWQDNILIPTLTAREHLQLYAQIkippggsGGVE--EIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIA 996
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEI-------AGVPkaEIEERVLELLELVGLeDKADAYPA-QLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1650-1845 |
4.79e-25 |
|
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: 103.62 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPG-----------ISY 1716
Cdd:cd03228 1 IEFKNVSFSYPgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1717 CPQsnplDP-LLTTTecirfygrlrgIRDldqfldrvldtyelrpykdvqvrN-LSGGNRRKLTVAVTCCGCTPTVLMDE 1794
Cdd:cd03228 81 VPQ----DPfLFSGT-----------IRE-----------------------NiLSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1795 PTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQ 1845
Cdd:cd03228 123 ATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
858-1059 |
4.89e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.90 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 926
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTlTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGkhESYPSWQ---LSGGYRRRLCVAIAFIASPSV 1003
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLR-------ERKFDRERALELLERLGLP--PDILDKPverLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
845-1060 |
4.94e-25 |
|
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: 106.57 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 845 KVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------ 918
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaams 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 ---------HQVGVCWQDNILIPTLTAREHLQLYAQIKippggsgGV-EEIRSEVA-QTLQSLNFGKHE-SYPSwQLSGG 986
Cdd:cd03294 93 rkelrelrrKKISMVFQSFALLPHRTVLENVAFGLEVQ-------GVpRAEREERAaEALELVGLEGWEhKYPD-ELSGG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 987 YRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1596-1863 |
6.42e-25 |
|
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: 113.01 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1596 IINVLIEWHLLRRLWQRVERLLDctyrRELDKLGQLKLVNIQSIfkscvdTGEaVRAENLWLAYR-RGHYAVRNVNFSVQ 1674
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILD----LPPEREEGRSKLSLPRL------KGD-IELENVSFRYPgDSPPVLDNISLTIK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1675 RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpgISYCPQSNPL------------DPLLT 1728
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpaslrRQ--IGVVLQDVFLfsgtirenitlgDPDAT 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 T---TECIRFYGrlrgirdLDQFLDRVLDTYELrpykdvQV----RNLSGGNRRKLTVA---VTccgcTPTVL-MDEPTS 1797
Cdd:COG2274 578 DeeiIEAARLAG-------LHDFIEALPMGYDT------VVgeggSNLSGGQRQRLAIAralLR----NPRILiLDEATS 640
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1798 DMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1863
Cdd:COG2274 641 ALDAETEAIILENLRR-LLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1651-1849 |
6.93e-25 |
|
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: 103.67 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPqsnpldpllttt 1730
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 ecIRFYGRLRGIrdLDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1810
Cdd:cd03214 68 --PKELARKIAY--VPQALELL----GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 113193620 1811 IEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:cd03214 140 LRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
872-1060 |
7.95e-25 |
|
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: 105.05 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS---SGKVLLAGE----HQVGVCW----QDNILIPTLTAREHL 940
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpDQFQKCVayvrQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYAQIKIPPGGSGGVEEIRSEVAqTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKD 1020
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKRVEDV-LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1021 IWQLIERL-RQGRAVIFATHF-MDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03234 182 LVSTLSQLaRRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
861-1059 |
8.29e-25 |
|
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: 104.41 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCW 925
Cdd:cd03292 5 NVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylrRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPP-----REIRKRVPAALELVGLsHKHRALPA-ELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1665-1850 |
8.29e-25 |
|
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: 105.11 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-------------YFEQPGISYcPQSNPLDPLLTTTE 1731
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVF-GQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFygrLRGIRDLDQF-----LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVL-MDEPTSDMDPVTRD 1805
Cdd:cd03267 115 SFYL---LAAIYDLPPArfkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH-EPEILfLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1806 MVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1850
Cdd:cd03267 191 NIRNFLKEYNRERGTtVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
861-1058 |
1.07e-24 |
|
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: 102.46 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTARE 938
Cdd:cd03228 5 NVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----------DGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 hlqLYAQIKIPP------GGSggveeIRSEVaqtlqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:cd03228 74 ---LRKNIAYVPqdpflfSGT-----IRENI-------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1013 VDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIMRNGR 1058
Cdd:cd03228 127 LDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
861-1061 |
1.19e-24 |
|
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: 104.73 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGsKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDNILI 931
Cdd:cd03299 5 NLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekRDISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEP 1009
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDK-----KEIERKVLEIAEMLGID-HllNRKPE-TLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1010 CNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1614-1966 |
1.32e-24 |
|
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: 113.18 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1614 ERLLDCTYRRELDKLGQLKLV-NIQSIFKSCvdtgeavraenlwlayrrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTI 1692
Cdd:TIGR01257 911 EGINDSFFERELPGLVPGVCVkNLVKIFEPS------------------GRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1693 FKLLTGQLQPDVGQIYFE-----------QPGISYCPQSNPLDPLLTTTECIRFYGRLRGiRDLDQF---LDRVLDTYEL 1758
Cdd:TIGR01257 973 LSILTGLLPPTSGTVLVGgkdietnldavRQSLGMCPQHNILFHHLTVAEHILFYAQLKG-RSWEEAqleMEAMLEDTGL 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1759 RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRdmvyATIEQLLL---ARRAVVLTSHSVSEIEHLC 1835
Cdd:TIGR01257 1052 HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RSIWDLLLkyrSGRTIIMSTHHMDEADLLG 1127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1836 QRVAVLRAGQVIASDSPQRLKSEHG-GYYAV-----------------TCFCG--------PA------QQAILSRSLNQ 1883
Cdd:TIGR01257 1128 DRIAIISQGRLYCSGTPLFLKNCFGtGFYLTlvrkmkniqsqrggcegTCSCTskgfstrcPArvdeitPEQVLDGDVNE 1207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1884 -------RLPGARDLQHYAHSLRFLVRVRSPGSLGDAPLLSELFAILCDvcVNVARFSLSRCRFETVFERILDSSESnGS 1956
Cdd:TIGR01257 1208 lmdlvyhHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLAD--LGLSSFGISDTPLEEIFLKVTEDADS-GS 1284
|
410
....*....|
gi 113193620 1957 NGVHKDQQQQ 1966
Cdd:TIGR01257 1285 LFAGGAQQKR 1294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1650-1848 |
1.52e-24 |
|
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: 103.71 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------QPGISYCPQ 1719
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgpGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPLLTTTECIRFYGRLRGIRD------LDQFLDRV-LDTYE-LRPykdvqvRNLSGGNRRKL----TVAVtccgcT 1787
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKaearerAEELLELVgLSGFEnAYP------HQLSGGMRQRValarALAV-----D 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1788 PTV-LMDEPTSDMDPVTRdmvyATIEQLLLA-----RRAVVLTSHSVSEIEHLCQRVAVL--RAGQVIA 1848
Cdd:cd03293 150 PDVlLLDEPFSALDALTR----EQLQEELLDiwretGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
866-1044 |
2.10e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTL--TAREHLQLY 943
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 944 AQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1023
Cdd:NF040873 82 RWARRGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|..
gi 113193620 1024 LI-ERLRQGRAVIFATHFMDEA 1044
Cdd:NF040873 161 LLaEEHARGATVVVVTHDLELV 182
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1665-1862 |
2.51e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.94 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpgiSYCP----------------QSNPLDPLLT 1728
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL----GYVPfkrrkefarrigvvfgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKltvavtccgC--------TPTVL-MDEPTS 1797
Cdd:COG4586 113 AIDSFRLLKAIYRIpdAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMR---------CelaaallhRPKILfLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGY 1862
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
840-1062 |
2.59e-24 |
|
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: 103.57 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 840 NYSFVKVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE- 918
Cdd:cd03267 5 NLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 ---------HQVGVCW-QDNILIPTLTAREHLQLYAQI-KIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGY 987
Cdd:cd03267 85 pwkrrkkflRRIGVVFgQKTQLWWDLPVIDSFYLLAAIyDLPPA------RFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 988 RRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1662-1845 |
3.10e-24 |
|
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: 101.49 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpgisycpqsnplDPLLTTTECIRfygrlrg 1741
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------------GEDLTDLEDEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1742 iRDLDQFLDRVLDTYELRPYKDVQ---VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL-LA 1817
Cdd:cd03229 72 -PPLRRRIGMVFQDFALFPHLTVLeniALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQaQL 150
|
170 180
....*....|....*....|....*...
gi 113193620 1818 RRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:cd03229 151 GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
867-1060 |
3.15e-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: 102.24 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR--QSSGKVLLAGE--------HQVGVCWQDNILIPTLTA 936
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRpldkrsfrKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 937 REHLQLYAQIKippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1016
Cdd:cd03213 100 RETLMFAAKLR----------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1017 ARKDIWQLIERLRQ-GRAVIFATH-FMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03213 146 SALQVMSLLRRLADtGRTIICSIHqPSSEIFELFDKLLLLSQGRVI 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
858-1062 |
6.88e-24 |
|
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: 102.86 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL------LAGE------HQVGVC- 924
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEdvwelrKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 --WQDNILiPTLTAREHLQ--LYAQIKIPPGGSggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIAS 1000
Cdd:COG1119 85 paLQLRFP-RDETVLDVVLsgFFDSIGLYREPT---DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
861-1062 |
7.47e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.53 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 926
Cdd:PRK13632 12 NVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkeirKKIGIIFQn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 -DNILIpTLTAREHLQL-YAQIKIPPggsGGVEEIRSEVAQTLQSLNFGKHESYpswQLSGGYRRRlcVAIAFIAS--PS 1002
Cdd:PRK13632 92 pDNQFI-GATVEDDIAFgLENKKVPP---KKMKDIIDDLAKKVGMEDYLDKEPQ---NLSGGQKQR--VAIASVLAlnPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAkYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1652-1855 |
8.15e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 8.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-------------GISYCP 1718
Cdd:PRK10895 6 AKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1795
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRaneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1796 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
858-1062 |
9.11e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.03 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ-----VGVCW 925
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmHKrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDniliPT----LTAREHLQLYAQIKIPPggsggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 1001
Cdd:COG1137 85 QE----ASifrkLTVEDNILAVLELRKLS-----KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1002 SVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1650-1848 |
1.23e-23 |
|
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: 101.06 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQ 1719
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPLLTTTECIRFYGRLRGIR--DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:cd03259 160 ALDAKLREELREELKELQRELGItTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1651-1857 |
1.25e-23 |
|
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: 101.60 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-------GISYC 1717
Cdd:COG0410 5 EVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeditgLPphriarlGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIR--FYGRlRGIRDLDQFLDRVLDTY-ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVL 1791
Cdd:COG0410 84 PEGRRIFPSLTVEENLLlgAYAR-RDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGralMS----RPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1792 M-DEPTSDMDPVTRDMVYATIEQllLARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:COG0410 159 LlDEPSLGLAPLIVEEIFEIIRR--LNREgvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
858-1059 |
1.43e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.03 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDN 928
Cdd:PRK09452 16 ELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQ--LYAQiKIPPggsggvEEIRSEVAQTL---QSLNFGKHEsyPSwQLSGGYRRRLCVAIAFIASPSV 1003
Cdd:PRK09452 96 ALFPHMTVFENVAfgLRMQ-KTPA------AEITPRVMEALrmvQLEEFAQRK--PH-QLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERL-RQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALqRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1649-1894 |
2.58e-23 |
|
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: 106.53 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFEQ------------P 1712
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 GISYCPQS--NPLDPlLTTTECIRFYGRLRGIrDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1787
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGL-SRAEARARVLELLEavgLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1788 PTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVT 1866
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVP 241
|
250 260
....*....|....*....|....*...
gi 113193620 1867 CFCGPAQQAILSRSLNQRLPGARDLQHY 1894
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLLEVRNLSKR 269
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1657-1856 |
2.83e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 100.65 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS---------------YCPQS 1720
Cdd:cd03261 6 LTKSFGGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaelyrlrrrmgMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:cd03261 86 GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1798 DMDPVTRDMVYATIeqLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1856
Cdd:cd03261 166 GLDPIASGVIDDLI--RSLKKElglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
853-1060 |
2.90e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 853 GKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEH-QVGVCWQDN-IL 930
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvKIGYFDQHQeEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAqikipPGGSggveeiRSEVAQTLQSLNFGKHESY-PSWQLSGGYRRRLCVAIAFIASPSVVILDEP 1009
Cdd:COG0488 391 DPDKTVLDELRDGA-----PGGT------EQEVRGYLGRFLFSGDDAFkPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1010 CNGVDAKARKdiwQLIERLR--QGrAVIFATH---FMDEakyLSDSLVIMRNGRII 1060
Cdd:COG0488 460 TNHLDIETLE---ALEEALDdfPG-TVLLVSHdryFLDR---VATRILEFEDGGVR 508
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
884-1062 |
3.16e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 103.64 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 884 VSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQ--VGVCWQDNILIPTLTAREHLqLYAQIKI 948
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflppHRrrIGYVFQEARLFPHLSVRGNL-LYGRKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 949 PPGGSggveeiRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRlcVAI--AFIASPSVVILDEPCNGVDAKARKDIWQLI 1025
Cdd:COG4148 106 PRAER------RISFDEVVELLGIGHLlDRRPA-TLSGGERQR--VAIgrALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 113193620 1026 ERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG4148 177 ERLRDELDipILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1645-1860 |
3.79e-23 |
|
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: 106.38 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QP 1712
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlsdldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 GISYCPQsNPLdpLLTTT--ECIRFYGR-------LRGIR--DLDQFLDRV---LDTyelrpykdvQV----RNLSGGNR 1774
Cdd:COG4988 412 QIAWVPQ-NPY--LFAGTirENLRLGRPdasdeelEAALEaaGLDEFVAALpdgLDT---------PLgeggRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1775 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQR 1854
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
....*.
gi 113193620 1855 LKSEHG 1860
Cdd:COG4988 558 LLAKNG 563
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1649-1859 |
4.08e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 100.44 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNP-LDPL 1726
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD--GQDITGLSEKeLYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1727 ----------------LTTTECIRF----YGRL--RGIRDL-DQFLDRV--LDTYELRPykdvqvRNLSGGNRRKltVA- 1780
Cdd:COG1127 81 rrrigmlfqggalfdsLTVFENVAFplreHTDLseAEIRELvLEKLELVglPGAADKMP------SELSGGMRKR--VAl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1781 ----VTccgcTPTVLM-DEPTSDMDPVTRDMVYATIEQLllaRRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1851
Cdd:COG1127 153 aralAL----DPEILLyDEPTAGLDPITSAVIDELIREL---RDElgltSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*....
gi 113193620 1852 PQRL-KSEH 1859
Cdd:COG1127 226 PEELlASDD 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1665-1848 |
4.90e-23 |
|
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: 99.59 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQsnplDPLLtttec 1732
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldpadlRRNIGYVPQ----DVTL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 irFYGRLRG-------------------IRDLDQFLDRVLDTYELrpykdvQV----RNLSGGNRRKLTVAVTCCGCTPT 1789
Cdd:cd03245 90 --FYGTLRDnitlgapladderilraaeLAGVTDFVNKHPNGLDL------QIgergRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1790 VLMDEPTSDMDPVTRDMVyatIEQL--LLARRAVVLTSHSVSEIEhLCQRVAVLRAGQVIA 1848
Cdd:cd03245 162 LLLDEPTSAMDMNSEERL---KERLrqLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVA 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
860-1070 |
5.30e-23 |
|
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: 102.88 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAvsNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQ--VGVC 924
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppEKrrIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQDNILIPTLTAREHLqLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:TIGR02142 81 FQEARLFPHLSVRGNL-RYGMKRARP------SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1645-1860 |
6.45e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 107.13 E-value: 6.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAVRAENLWLayRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-FEQP---------- 1712
Cdd:NF033858 262 DDEPAIEARGLTM--RFGDFtAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGQPvdagdiatrr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 GISYCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTV 1790
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNLELHARLFHLpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIH-KPEL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1791 L-MDEPTSDMDPVTRDMVYatieQLL--LARRAVV---LTSHSVSEIEhLCQRVAVLRAGQVIASDSPQRLKSEHG 1860
Cdd:NF033858 419 LiLDEPTSGVDPVARDMFW----RLLieLSREDGVtifISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
858-1071 |
8.64e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCW 925
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaiaLGIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYAqiKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAI--AFIASPSV 1003
Cdd:COG3845 87 QHFMLVPNLTVAENIVLGL--EPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEIlkALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRII-----AQHSRDSLQRL 1071
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdtAETSEEELAEL 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
858-1062 |
9.33e-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: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVcwQDNI--LIPT 933
Cdd:cd03247 2 SINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALssLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLqlyaqikippggsggveeirseVAQTLQSlNFGKhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGV 1013
Cdd:cd03247 80 LNQRPYL----------------------FDTTLRN-NLGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1014 DAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLsDSLVIMRNGRIIAQ 1062
Cdd:cd03247 130 DPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1650-1860 |
1.04e-22 |
|
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: 98.84 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPG-----------ISYC 1717
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIrdisrkslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQsnplDPLL---TTTECIRfYGRLRGIRD----------LDQFLDRVLDTYelrpykDVQVR----NLSGGNRRKLTVA 1780
Cdd:cd03254 83 LQ----DTFLfsgTIMENIR-LGRPNATDEevieaakeagAHDFIMKLPNGY------DTVLGenggNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1781 VTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHG 1860
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIII-AHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
861-1059 |
1.18e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQ----- 926
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlharDRKVGFVFQhyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 ------DNIL--IPTLTAREHLQLYAqikippggsggveeIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIA 996
Cdd:PRK10851 87 rhmtvfDNIAfgLTVLPRRERPNAAA--------------IKAKVTQLLEMVQLA-HlaDRYPA-QLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDI--W--QLIERLRqgRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELrrWlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
874-1057 |
1.24e-22 |
|
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: 98.69 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhQVG-------VCWQDNILIPTLTAREHLQLYAQI 946
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-QITepgpdrmVVFQNYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 947 KIPPGGSGGVEEIrseVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDiwqLIE 1026
Cdd:TIGR01184 82 VLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN---LQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 113193620 1027 RLRQ-----GRAVIFATHFMDEAKYLSDSLVIMRNG 1057
Cdd:TIGR01184 156 ELMQiweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
857-1062 |
1.79e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.59 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 857 ASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKV-LLAGE-----HQVGVCWQdnI- 929
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDmadarHRRAVCPR--Ia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 ---------LIPTLTAREHLQ----LYAQikippggsgGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 996
Cdd:NF033858 80 ympqglgknLYPTLSVFENLDffgrLFGQ---------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRA---VIFATHFMDEAKYLsDSLVIMRNGRIIAQ 1062
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAERF-DWLVAMDAGRVLAT 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
871-1060 |
1.81e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.55 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCW-QDNILIPTLTAREH 939
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkefaRRIGVVFgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 940 LQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:COG4586 117 FRLLKAIyRIPD------AEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1019 KDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG4586 191 EAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
861-1068 |
1.96e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.45 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ------------VGVCWQDN 928
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaagVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLyAQIkipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK11288 89 HLVPEMTVAENLYL-GQL---PHKGGIVnrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH------SRDSL 1068
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFddmaqvDRDQL 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1662-1849 |
2.60e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP------------GISYCPQSNPLDPLLT 1728
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPvrfrsprdaqaaGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIrFYGRL---RGI-------RDLDQFLDRV-LDtyeLRPykDVQVRNLSGGNR------RKLTVavtccgcTPTVL 1791
Cdd:COG1129 96 VAENI-FLGREprrGGLidwramrRRARELLARLgLD---IDP--DTPVGDLSVAQQqlveiaRALSR-------DARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1792 -MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:COG1129 163 iLDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
868-1060 |
2.66e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.01 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 868 SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCWQ--DNILIPT 933
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiRNKAGMVFQnpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVILDEPCN 1011
Cdd:PRK13633 102 IVEEDVAFGPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAmrPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1012 GVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRII 1060
Cdd:PRK13633 174 MLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
861-1060 |
2.87e-22 |
|
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: 98.02 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGS-KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCW 925
Cdd:cd03256 5 NLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHL--QLYAQIKIPPGGSGGVEEIRSEVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPS 1002
Cdd:cd03256 85 QQFNLIERLSVLENVlsGRLGRRSTWRSLFGLFPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
845-1068 |
2.88e-22 |
|
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: 104.53 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 845 KVSRSQLDGKLgaSLVNVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---- 918
Cdd:COG2274 464 KLSLPRLKGDI--ELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrq 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 -------HQVGVCWQDNILIPTlTAREHLQLyaqikippgGSGGV--EEIRsEVAQTLQSLNF---------------GK 974
Cdd:COG2274 542 idpaslrRQIGVVLQDVFLFSG-TIRENITL---------GDPDAtdEEII-EAARLAGLHDFiealpmgydtvvgegGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 975 hesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIM 1054
Cdd:COG2274 611 -------NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR-LADRIIVL 682
|
250
....*....|....
gi 113193620 1055 RNGRIIAQHSRDSL 1068
Cdd:COG2274 683 DKGRIVEDGTHEEL 696
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
871-1044 |
5.57e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.05 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNILIPTLTAREHL 940
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiatrRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:NF033858 361 ELHARLfHLPA------AEIAARVAEMLERFDLADVaDALPD-SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180
....*....|....*....|....*...
gi 113193620 1019 KDIWQLIERL-RQGRAVIF-ATHFMDEA 1044
Cdd:NF033858 434 DMFWRLLIELsREDGVTIFiSTHFMNEA 461
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1650-1852 |
6.03e-22 |
|
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: 96.99 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG------ISYC 1717
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedirEQDPvelrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIRF------YGRLRGIRDLDQFLDRV-LDTYElrpYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1790
Cdd:cd03295 81 IQQIGLFPHMTVEENIALvpkllkWPKEKIRERADELLALVgLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1791 LMDEPTSDMDPVTRDMV---YATIEQLLlaRRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1852
Cdd:cd03295 158 LMDEPFGALDPITRDQLqeeFKRLQQEL--GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
859-1070 |
7.57e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH------QVGVCWQDNILIP 932
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 933 TLTAREHLQLYAQIkippggsGGVE-EIRSEVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:PRK11248 84 WRNVQDNVAFGLQL-------AGVEkMQRLEIAhQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1011 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMR--NGRIIAQHSRDSLQR 1070
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLNFARR 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
845-1061 |
7.66e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 96.06 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 845 KVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvGVC 924
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WqdniLI-------PTLTAREHLQLYAQIKippGGSGgvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF 997
Cdd:cd03220 87 S----LLglgggfnPELTGRENIYLNGRLL---GLSR--KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
867-1062 |
8.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ---DNILIP 932
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrKFVGLVFQnpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 933 TLTarehlqlyAQIKIPPGGSGGVEE-IRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:PRK13652 95 TVE--------QDIAFGPINLGLDEEtVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1012 GVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
861-1068 |
1.01e-21 |
|
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: 96.14 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDN 928
Cdd:cd03254 7 NVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTlTAREHLQLyaqikippGGSGGVEEIRSEVAQTLQSLNFGKH-----ESYPSWQ---LSGGYRRRLCVAIAFIAS 1000
Cdd:cd03254 87 FLFSG-TIMENIRL--------GRPNATDEEVIEAAKEAGAHDFIMKlpngyDTVLGENggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
858-1062 |
1.74e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.84 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------H 919
Cdd:COG1135 3 ELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalserelraarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 920 QVGVCWQ-----------DNILIPtltarehLQLyaqIKIPPggsggvEEIRSEVAQTLQslnF----GKHESYPSwQLS 984
Cdd:COG1135 83 KIGMIFQhfnllssrtvaENVALP-------LEI---AGVPK------AEIRKRVAELLE---LvglsDKADAYPS-QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 985 GGYRRRlcVAIA--FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG1135 143 GGQKQR--VGIAraLANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
..
gi 113193620 1061 AQ 1062
Cdd:COG1135 221 EQ 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1650-1846 |
1.76e-21 |
|
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: 94.86 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG------------- 1713
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD--Gtdisklsekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1714 -----ISYCPQSNPLDPLLTTTECIRFYGRLRGIRDLD------QFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVT 1782
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKErreraeELLERV----GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1783 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL-LARRAVVLTSHSVsEIEHLCQRVAVLRAGQV 1846
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1650-1847 |
2.31e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfeQPG----ISYCPQSN-PLD 1724
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---KLGetvkIGYFDQHQeELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1725 PLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYElrpykDVQ--VRNLSGGNRR-----KLTVAvtccgcTPTVL-MDEPT 1796
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGD-----DAFkpVGVLSGGEKArlalaKLLLS------PPNVLlLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1797 SDMDPVTRDMvyatIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:COG0488 461 NHLDIETLEA----LEEALDDfPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
861-1043 |
3.18e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTLTAREHL 940
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 ---------------QLYAQIKIPPGGSGGVEE------------IRSEVAQTLQSLNFGKHEsypsWQ-----LSGGYR 988
Cdd:COG0488 83 ldgdaelraleaeleELEAKLAEPDEDLERLAElqeefealggweAEARAEEILSGLGFPEED----LDrpvseLSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 989 RRLCVAIAFIASPSVVILDEPCNGVDAKARkdIWqLIERLRQGR-AVIFATH---FMDE 1043
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESI--EW-LEEFLKNYPgTVLVVSHdryFLDR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
875-1062 |
5.78e-21 |
|
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: 93.33 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 875 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNILIPTLTAREHLQLyaq 945
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappaDRPVSMLFQENNLFAHLTVEQNVGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 946 ikippGGSGGV---EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIW 1022
Cdd:cd03298 94 -----GLSPGLkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1023 QLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:cd03298 169 DLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
858-1062 |
5.86e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 926
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpsrelaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTARE--------HlqlyaqikippggSGGV--EEIRSEVAQTLQSLNFG--KHEsYPSwQLSGGYRRRLCVA 994
Cdd:COG4604 83 ENHINSRLTVRElvafgrfpY-------------SKGRltAEDREIIDEAIAYLDLEdlADR-YLD-ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 995 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVI-------FATHFmdeakylSDSLVIMRNGRIIAQ 1062
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLadELGKTVVivlhdinFASCY-------ADHIVAMKDGRVVAQ 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
859-1064 |
7.47e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEHQVGVCWQDNILIPT 933
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHL-------QLYAQ-----IKIPPGGSGG-VEEIRSEVAQTLQSLNFGKHESYPS-WQLSGGYRRRLCVAIAFIA 999
Cdd:PRK13645 88 LRKEIGLvfqfpeyQLFQEtiekdIAFGPVNLGEnKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1000 SPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1064
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
858-1043 |
1.05e-20 |
|
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: 90.20 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLlagehqvgvcWQDNILIPTLTar 937
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT----------WGSTVKIGYFE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 ehlqlyaqikippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:cd03221 70 --------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190
....*....|....*....|....*....|
gi 113193620 1018 RKdiwQLIERLRQ-GRAVIFATH---FMDE 1043
Cdd:cd03221 106 IE---ALEEALKEyPGTVILVSHdryFLDQ 132
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1650-1855 |
2.11e-20 |
|
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: 92.24 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG-----QLQPDVGQIYFEQPGIsYCPQSNPL- 1723
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDI-YDLDVDVLe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 ------------DPL-LTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRPY-KD-VQVRNLSGGNRRKL----TVAV 1781
Cdd:cd03260 79 lrrrvgmvfqkpNPFpGSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDEvKDrLHALGLSGGQQQRLclarALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1782 tccgcTPTV-LMDEPTSDMDPVTRdmvyATIEQLL--LARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:cd03260 159 -----EPEVlLLDEPTSALDPIST----AKIEELIaeLKKEyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
861-1062 |
2.54e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTARE-- 938
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-----------ISMLSSRQla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 -HLQLYAQIKIPPGGSgGVEEI-------------------RSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 998
Cdd:PRK11231 76 rRLALLPQHHLTPEGI-TVRELvaygrspwlslwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
859-1070 |
2.59e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQVGVC--WQDNI 929
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiQQRDICmvFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPtltareHLQLYAQIkippgGSG----GV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 1003
Cdd:PRK11432 89 LFP------HMSLGENV-----GYGlkmlGVpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1676-1850 |
3.24e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 91.20 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1676 GECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------------EQPGISYCPQSNPLDPLLTTTECIRF-YGR 1738
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkinlppQQRKIGLVFQQYALFPHLNVRENLAFgLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1739 LRGIRDLDQFlDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR 1818
Cdd:cd03297 103 KRNREDRISV-DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 113193620 1819 RAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASD 1850
Cdd:cd03297 182 NIPVIfVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1662-1853 |
3.26e-20 |
|
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: 91.63 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTE 1731
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditnlppEKRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFYGRLRgIRDLDQFLDRVLDTYEL---RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVy 1808
Cdd:cd03299 91 NIAYGLKKR-KVDKKEIERKVLEIAEMlgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1809 atIEQLLLARRAVVLT----SHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:cd03299 169 --REELKKIRKEFGVTvlhvTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
862-1063 |
3.30e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 862 VSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG--------------EHQVGVCWQ 926
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTarehlqLYAQIKIP---PGGSGgvEEIRSEVAQTLQSLN-FGKHESYPSwQLSGGYRRRLCVAIAFIASPS 1002
Cdd:PRK10908 87 DHHLLMDRT------VYDNVAIPliiAGASG--DDIRRRVSAALDKVGlLDKAKNFPI-QLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH 1063
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
869-1062 |
4.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 869 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-------------QVGVCWQdnilIPtlt 935
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsdirkKVGLVFQ----YP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 arEHlQL-----YAQIKIPPGGSG-GVEEIRSEVAQTLQ--SLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVI 1005
Cdd:PRK13637 93 --EY-QLfeetiEKDIAFGPINLGlSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRR--VAIAGVVAmePKILI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1648-1853 |
5.05e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1648 EAVRAENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISY--------- 1716
Cdd:PRK13548 1 AMLEARNL--SVRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLADWspaelarrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1717 --CPQSNPLDPLLTTTECIRFyGRL---RGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVA-----VTCCGC 1786
Cdd:PRK13548 79 avLPQHSSLSFPFTVEEVVAM-GRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqLWEPDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1787 TPTVLM-DEPTSDMDPvtrdmvYATIEQLLLARR-------AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:PRK13548 158 PPRWLLlDEPTSALDL------AHQHHVLRLARQlaherglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1665-1849 |
6.35e-20 |
|
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: 89.29 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQpgisycpqsnplDPLLTTTECIRFYgrlrgIRD 1744
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG------------VPVSDLEKALSSL-----ISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1745 LDQfldrvldtyelRPYK-DVQVRN-----LSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRdmvYATIEQLL--L 1816
Cdd:cd03247 80 LNQ-----------RPYLfDTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE---RQLLSLIFevL 145
|
170 180 190
....*....|....*....|....*....|...
gi 113193620 1817 ARRAVVLTSHSVSEIEHLcQRVAVLRAGQVIAS 1849
Cdd:cd03247 146 KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
871-1062 |
8.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQ---DNILIPTL 934
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrKTVGIVFQnpdDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 ---TAREHLQLyaqiKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVILDEP 1009
Cdd:PRK13639 97 eedVAFGPLNL----GLSK------EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR--VAIAGILAmkPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1010 CNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1649-1855 |
1.15e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.85 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCP 1718
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglppEKRNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNR-RkltVA-----VtccgCTPTV 1790
Cdd:COG3842 84 QDYALFPHLTVAENVAFGLRMRGVpkAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VAlaralA----PEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1791 -LMDEPTSDMDPVTRDMVYATIEQLLlaRRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:COG3842 157 lLLDEPLSALDAKLREEMREELRRLQ--RELgitFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
871-1060 |
1.50e-19 |
|
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: 92.04 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE---------------HQVGVCWQD--NIL 930
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEdllklsekelrkirgREIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNFGKHE----SYPSwQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:COG0444 100 NPVMTVGD--QIAEPLRIHGGLSK--AEARERAIELLERVGLPDPErrldRYPH-ELSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1068 |
1.72e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 853 GKLGASLVNVSKLY---GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR------QSSGKVLLAGE----- 918
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 ------HQVGVCWQDNILIPtltareHLQLYAQIKIPPGGSGGVE--EIRSEVAQTLQSLNFGKhESY-----PSWQLSG 985
Cdd:PRK14246 84 daiklrKEVGMVFQQPNPFP------HLSIYDNIAYPLKSHGIKEkrEIKKIVEECLRKVGLWK-EVYdrlnsPASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 986 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSR 1065
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
...
gi 113193620 1066 DSL 1068
Cdd:PRK14246 237 NEI 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
874-1080 |
2.03e-19 |
|
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: 90.25 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCWQDNI--LIPTLTAR 937
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrkqrrafrRDVQLVFQDSPsaVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 ----EHLQLYAQIKIPPGGSGGVE-----EIRSEVAQtlqslnfgkheSYPSwQLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:TIGR02769 109 qiigEPLRHLTSLDESEQKARIAElldmvGLRSEDAD-----------KLPR-QLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1009 PCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQhsRDSLQRLCTSNYSIRL 1080
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE--CDVAQLLSFKHPAGRN 248
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
871-1062 |
2.41e-19 |
|
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: 88.80 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDNILIPTlTAREH 939
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 940 LQLyaqikippgGSGGVEEIRSEVAQTLQSLN--FGKHESYPSWQ-------LSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:cd03245 98 ITL---------GAPLADDERILRAAELAGVTdfVNKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1011 NGVDAKARKdiwQLIERLRQ---GRAVIFATH---FMDeakyLSDSLVIMRNGRIIAQ 1062
Cdd:cd03245 169 SAMDMNSEE---RLKERLRQllgDKTLIIITHrpsLLD----LVDRIIVMDSGRIVAD 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
859-1070 |
2.45e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAvsNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDNI 929
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppAErpVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLyaqiKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESY-PSwQLSGGYRRRlcVAIA--FIASPSVVIL 1006
Cdd:COG3840 82 LFPHLTVAQNIGL----GLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRlPG-QLSGGQRQR--VALArcLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
858-1059 |
4.26e-19 |
|
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: 87.97 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVC 924
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkninelrQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQDNILIPTLTAREHLQLyAQIKIPpggsgGVEEIRSEvAQTLQSLN----FGKHESYPSwQLSGGYRRRLCVAIAFIAS 1000
Cdd:cd03262 82 FQQFNLFPHLTVLENITL-APIKVK-----GMSKAEAE-ERALELLEkvglADKADAYPA-QLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
874-1062 |
4.82e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.33 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLTARE 938
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaelrnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 HLQLYAQI-KIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:PRK11629 107 NVAMPLLIgKKKPA------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1018 RKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLViMRNGRIIAQ 1062
Cdd:PRK11629 181 ADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
867-1039 |
4.93e-19 |
|
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: 87.41 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH--QVGVCWQDNILI--------PTLTA 936
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaEQRDEPHENILYlghlpglkPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 937 REHLQLYAQIkippggsGGVEeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1016
Cdd:TIGR01189 91 LENLHFWAAI-------HGGA--QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 113193620 1017 ARKDIWQLIE-RLRQGRAVIFATH 1039
Cdd:TIGR01189 162 GVALLAGLLRaHLARGGIVLLTTH 185
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1649-1864 |
6.71e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.92 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpgI 1714
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleslrRQ--I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1715 SYCPQsnplDP-LLTTT--ECIRfYGRLrGIRD-----------LDQFLDRV---LDTYelrpykdVQVR--NLSGGNRR 1775
Cdd:COG1132 417 GVVPQ----DTfLFSGTirENIR-YGRP-DATDeeveeaakaaqAHEFIEALpdgYDTV-------VGERgvNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1776 KLTVAvtccgcTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRL 1855
Cdd:COG1132 484 RIAIArallkdPPILILDEATSALDTETEALIQEALER-LMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
....*....
gi 113193620 1856 kSEHGGYYA 1864
Cdd:COG1132 562 -LARGGLYA 569
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1665-1855 |
7.00e-19 |
|
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: 88.85 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------------QSNPLDPLLT 1728
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrkkismvfQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR-D 1805
Cdd:cd03294 119 VLENVAFGLEVQGVprAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRrE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1806 MvyatiEQLLLA-----RRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:cd03294 199 M-----QDELLRlqaelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
871-1059 |
7.24e-19 |
|
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: 86.33 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniLIPTLTAREHLQLyaqikipp 950
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK-----------PVTRRSPRDAIRA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 951 gGSGGVEEIRSEVAqTLQSLNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR- 1029
Cdd:cd03215 76 -GIAYVPEDRKREG-LVLDLSVAENIALSS-LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAd 152
|
170 180 190
....*....|....*....|....*....|
gi 113193620 1030 QGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:cd03215 153 AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
856-1058 |
7.95e-19 |
|
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: 86.75 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 856 GASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehQVGVC----W------ 925
Cdd:cd03250 5 DASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVsqepWiqngti 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILiptLTAREHLQLYAQ----------IKIPPGGsggveeIRSEVAQtlQSLNfgkhesypswqLSGGYRRRLCVAI 995
Cdd:cd03250 83 RENIL---FGKPFDEERYEKvikacalepdLEILPDG------DLTEIGE--KGIN-----------LSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQ--LIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGR 1058
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
861-1059 |
8.52e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGEhqvgvcwqdnilIPTLTAREHL 940
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT------------APLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYAQIK--------IPPGGSGGVEEIRSEVAQTLQSLnfGKHESYPSW--QLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:PRK11247 84 RLMFQDArllpwkkvIDNVGLGLKGQWRDAALQALAAV--GLADRANEWpaALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1011 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK11247 162 GALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
871-1068 |
9.44e-19 |
|
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: 87.54 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDNILIpTLTAREH 939
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 940 LQLyaqikIPPGGSggVEEIrSEVAQTLQSLNFGKH--ESYPSW------QLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:cd03252 96 IAL-----ADPGMS--MERV-IEAAKLAGAHDFISElpEGYDTIvgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1012 GVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
871-1064 |
1.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTAREHL---------- 940
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-----------DDITITHKTKDKYIrpvrkrigmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 ------QLYA-----QIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK13646 91 fqfpesQLFEdtverEIIFGPKNFKmNLDEVKNYAHRLLMDLGFSRDvmSQSP-FQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDE-AKYlSDSLVIMRNGRIIAQHS 1064
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEvARY-ADEVIVMKEGSIVSQTS 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
829-1062 |
1.01e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 829 IGLAYQRYKKNNYSFVKvsrsqldgklgaSLVNVSKL-YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR 907
Cdd:COG1134 10 VSKSYRLYHEPSRSLKE------------LLLRRRRTrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 908 QSSGKVLLAG------EHQVGvcwqdniLIPTLTAREHLQLYAQIKippGGSggveeiRSEVAQTLQS-LNF---GKHES 977
Cdd:COG1134 78 PTSGRVEVNGrvsallELGAG-------FHPELTGRENIYLNGRLL---GLS------RKEIDEKFDEiVEFaelGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 978 YPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA----KARKdiwQLIERLRQGRAVIFATHFMDEAKYLSDSLVI 1053
Cdd:COG1134 142 QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLA---RIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 113193620 1054 MRNGRIIAQ 1062
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
866-1062 |
1.07e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQDNilip 932
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllalrQQVATVFQDP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 933 tltarEHLQLYAQIKIPPGGS---GGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:PRK13638 87 -----EQQIFYTDIDSDIAFSlrnLGVpeAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1008 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
857-1062 |
1.31e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 857 ASLVNVSKL---YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GV 923
Cdd:PRK11300 3 QPLLSVSGLmmrFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpgHQIarmGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 924 C--WQDNILIPTLTAREHLqLYAQ------------IKIPpGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRR 989
Cdd:PRK11300 83 VrtFQHVRLFREMTVIENL-LVAQhqqlktglfsglLKTP-AFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 990 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
871-1062 |
1.39e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQD-NILIPTLTARE 938
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekwvrSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 hlqlyaQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1017
Cdd:PRK13647 100 ------DVAFGPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1018 RKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13647 174 QETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
858-1063 |
1.53e-18 |
|
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: 86.72 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAV----SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 918
Cdd:COG4181 10 ELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedararlra 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 HQVGVCWQDNILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA- 996
Cdd:COG4181 90 RHVGFVFQSFQLLPTLTALENVMLPLELA-------GRRDARARARALLERVGLGHRLDhYPA-QLSGGEQQR--VALAr 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 997 -FIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHfmDEAkyL---SDSLVIMRNGRIIAQH 1063
Cdd:COG4181 160 aFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH--DPA--LaarCDRVLRLRAGRLVEDT 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
873-1039 |
1.78e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.63 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 873 SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------------HQVGVcwqdnilIPTLT 935
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdllylgHQPGI-------KTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLYAQIkippGGSGGVEEIrsevAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIA--FIASPSVVILDEPCNGV 1013
Cdd:PRK13538 91 ALENLRFYQRL----HGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 113193620 1014 DAKARKDIWQLIER-LRQGRAVIFATH 1039
Cdd:PRK13538 161 DKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
861-1060 |
2.36e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNILI 931
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTAREHLQL-YAQIKIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:PRK11607 104 PHMTVEQNIAFgLKQDKLPKA------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1011 NGVDAKARkDIWQL-----IERLrqGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK11607 178 GALDKKLR-DRMQLevvdiLERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
858-1039 |
2.59e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT--LT 935
Cdd:PRK09544 6 SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTlpLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLYAQIKippggsggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 1015
Cdd:PRK09544 86 VNRFLRLRPGTK------------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180
....*....|....*....|....*.
gi 113193620 1016 KARKDIWQLIERLRQ--GRAVIFATH 1039
Cdd:PRK09544 154 NGQVALYDLIDQLRRelDCAVLMVSH 179
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1651-1854 |
2.74e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYC----------- 1717
Cdd:COG4559 3 EAENL--SVRLGGRTLlDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrLNGRPLAAWSpwelarrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPLDPLLTTTECIRFyGRLRGIR---DLDQFLDRVLDTYELRPYKDVQVRNLSGGNR------RKLT-VAVTCCGCT 1787
Cdd:COG4559 81 PQHSSLAFPFTVEEVVAL-GRAPHGSsaaQDRQIVREALALVGLAHLAGRSYQTLSGGEQqrvqlaRVLAqLWEPVDGGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1788 PTVLMDEPTSDMDP--------VTRDmvyatieqllLARR--AVV-------LTShsvseieHLCQRVAVLRAGQVIASD 1850
Cdd:COG4559 160 RWLFLDEPTSALDLahqhavlrLARQ----------LARRggGVVavlhdlnLAA-------QYADRILLLHQGRLVAQG 222
|
....
gi 113193620 1851 SPQR 1854
Cdd:COG4559 223 TPEE 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1672-1840 |
3.02e-18 |
|
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: 86.31 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1672 SVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSnpLDPLLTTTECIRFYGRLRGIRDLDQFLDR 1751
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY--IKADYEGTVRDLLSSITKDFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1752 VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLL-ARRAVVLTSHSVSE 1830
Cdd:cd03237 99 IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEnNEKTAFVVEHDIIM 178
|
170
....*....|
gi 113193620 1831 IEHLCQRVAV 1840
Cdd:cd03237 179 IDYLADRLIV 188
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1650-1846 |
4.02e-18 |
|
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: 85.00 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------Q 1719
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdiamvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVpkDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1798 DMDPVTRDMVYATIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
871-1062 |
4.49e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQ--DNILIPTlt 935
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESVGMVFQdpDNQLFSA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 arehlQLYAQIKIPPGGSGGVE-EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 1014
Cdd:PRK13636 99 -----SVYQDVSFGAVNLKLPEdEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1015 AKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1650-1847 |
5.47e-18 |
|
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: 87.03 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGH---YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFE------------- 1710
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDgedllklsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1711 ---QPGISYCPQsNP---LDPLLTT----TECIRFYGRLRGiRDLDQFLDRVLDTYELRPYKDV------QvrnLSGGNR 1774
Cdd:COG0444 82 kirGREIQMIFQ-DPmtsLNPVMTVgdqiAEPLRIHGGLSK-AEARERAIELLERVGLPDPERRldryphE---LSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1775 RKLTVAVTCCgCTPTVL-MDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:COG0444 157 QRVMIARALA-LEPKLLiADEPTTALD-VT---IQAQILNLLkdLQRElglAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1650-1850 |
6.72e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGE-CFgLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-----------EQP----- 1712
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkrrEIPylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 -GISYcpQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTccgc 1786
Cdd:COG2884 81 iGVVF--QDFRLLPDRTVYENVALPLRVTGKsrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAralVN---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1787 TPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1850
Cdd:COG2884 155 RPELLLaDEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
858-1054 |
7.83e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE---------HQVGVCW 925
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLqLYAqikIPPGGSGgvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:COG4136 83 QDDLLFPHLSVGENL-AFA---LPPTIGR--AQRRARVEQALEEAGLaGFADRDPA-TLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLI-ERLRQ-GRAVIFATHfmDEAKYLSDSLVIM 1054
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVfEQIRQrGIPALLVTH--DEEDAPAAGRVLD 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1665-1849 |
8.82e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYcpqsNPLDPLLTTTECIR---------- 1734
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NINY----NKLDHKLAAQLGIGiiyqelsvid 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 --------FYGRLR-----GIRDLD-----QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1796
Cdd:PRK09700 94 eltvlenlYIGRHLtkkvcGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1797 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
873-1039 |
1.01e-17 |
|
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: 83.70 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 873 SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--HQVGVCWQDNILI--------PTLTAREHLQL 942
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLYlghapgikTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 YAQIkippGGSGGVEEirsevaqTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKArkdIW 1022
Cdd:cd03231 97 WHAD----HSDEQVEE-------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG---VA 162
|
170 180
....*....|....*....|.
gi 113193620 1023 QLIERLR----QGRAVIFATH 1039
Cdd:cd03231 163 RFAEAMAghcaRGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
861-1039 |
1.07e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGvcwQDNI 929
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaeacHYLG---HRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREHLQLYAQIKippGGSggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEP 1009
Cdd:PRK13539 84 MKPALTVAENLEFWAAFL---GGE------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1010 CNGVDAKARKDIWQLI-ERLRQGRAVIFATH 1039
Cdd:PRK13539 155 TAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1652-1847 |
1.09e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPG--ISYCPQSNPLDPLLT 1728
Cdd:COG0488 1 LENLSKSF--GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGlrIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIrfYGRLRGIRDLDQFLDRV-----------------------LDTYELRP--------------YKDVQVRNLSG 1771
Cdd:COG0488 78 VLDTV--LDGDAELRALEAELEELeaklaepdedlerlaelqeefeaLGGWEAEAraeeilsglgfpeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1772 GNRRKLTVA---VtccgCTPTVLM-DEPTSDMDpvtrdmVYATI--EQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAG 1844
Cdd:COG0488 156 GWRRRVALAralL----SEPDLLLlDEPTNHLD------LESIEwlEEFLKNYPgTVLVVSHDRYFLDRVATRILELDRG 225
|
...
gi 113193620 1845 QVI 1847
Cdd:COG0488 226 KLT 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1649-1841 |
1.10e-17 |
|
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: 88.88 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY------------FEQPGISY 1716
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadadSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1717 CPQSnpldPLL---TTTECIRFY----------------GRLRGIRDLDQFLDRVLDTyelrpykdvQVRNLSGGNRRKL 1777
Cdd:TIGR02857 401 VPQH----PFLfagTIAENIRLArpdasdaeirealeraGLDEFVAALPQGLDTPIGE---------GGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1778 TVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVsEIEHLCQRVAVL 1841
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
858-1067 |
1.15e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------------Q 920
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkairelrrN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQDNILIPTLTAREHLqLYAQIKIPpggsgGV--EEIRSEVAQTLQSLNFGKH-ESYPsWQLSGGYRRRLCVAIAF 997
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNL-IEAPCRVL-----GLskDQALARAEKLLERLRLKPYaDRFP-LHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDS 1067
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
868-1062 |
1.20e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 868 SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQ--DNILIPTl 934
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvRRQVGMVFQnpDNQFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 TAREHLQL-YAQIKIPPggsggvEEIRSEVAQTLQSLN---FGKHEsyPSwQLSGGYRRRlcVAIAFI--ASPSVVILDE 1008
Cdd:PRK13635 98 TVQDDVAFgLENIGVPR------EEMVERVDQALRQVGmedFLNRE--PH-RLSGGQKQR--VAIAGVlaLQPDIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1009 PCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQ 1062
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
858-1068 |
1.45e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLY--GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVC 924
Cdd:PRK11160 340 TLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrQAISVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQdNILIPTLTAREHLQLYAqikipPGGSggvEEIRSEVaqtLQSLNFGKH----ESYPSW------QLSGGYRRRLCVA 994
Cdd:PRK11160 420 SQ-RVHLFSATLRDNLLLAA-----PNAS---DEALIEV---LQQVGLEKLleddKGLNAWlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 995 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltGLEQF----DRICVMDNGQIIEQGTHQEL 560
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
858-1054 |
1.53e-17 |
|
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: 88.50 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGV---CWQDNIL--- 930
Cdd:TIGR02857 323 EFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadSWRDQIAwvp 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 -IPTLTA---REHLQLYAqikipPGGSGgvEEIRS--------EVAQTL-QSLNF--GKHESypswQLSGGYRRRLCVAI 995
Cdd:TIGR02857 403 qHPFLFAgtiAENIRLAR-----PDASD--AEIREaleragldEFVAALpQGLDTpiGEGGA----GLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHfMDEAKYLSDSLVIM 1054
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH-RLALAALADRIVVL 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
871-1061 |
1.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------------EHQVGVCWQdnilIPTLT 935
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLyAQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:PRK13643 97 LFEETVL-KDVAFGPQNFGiPKEKAEKIAAEKLEMVGLADEfwEKSP-FELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1013 VDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
866-1060 |
1.69e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKL------LTGQIRqSSGKVLLAGE-------------HQVGVCWQ 926
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGAR-VEGEILLDGEdiydpdvdvvelrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 ----------DNILIPtltAREHlqlyaQIKippgGSGGVEEI--RS--------EVAQTLQSLNFGkhesypswqLSGG 986
Cdd:COG1117 100 kpnpfpksiyDNVAYG---LRLH-----GIK----SKSELDEIveESlrkaalwdEVKDRLKKSALG---------LSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 987 YRRRLCVAIAfIA-SPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG1117 159 QQQRLCIARA-LAvEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
874-1071 |
2.45e-17 |
|
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: 82.19 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTG--QIRQSSGKVLLAGEhqvgvcwqdNI--LIPTLTAREHLQLYAQ--IK 947
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE---------DItdLPPEERARLGIFLAFQypPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 IPpggsgGVEeirseVAQTLQSLNFGkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIER 1027
Cdd:cd03217 89 IP-----GVK-----NADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1028 LR-QGRAVIFATHFMDEAKYLSDSLV-IMRNGRIIAQHSRDSLQRL 1071
Cdd:cd03217 150 LReEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGDKELALEI 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1665-1849 |
3.36e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP------------GISYCPQSNPLDPLLTTTE 1731
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPvrirsprdaialGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CI------RFYGRLRgIRDLDQFLDRVLDTYELR--PykDVQVRNLSGGNR----------RKltvavtccgctPTVL-M 1792
Cdd:COG3845 100 NIvlglepTKGGRLD-RKAARARIRELSERYGLDvdP--DAKVEDLSVGEQqrveilkalyRG-----------ARILiL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1793 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1649-1849 |
3.43e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY---------FEQPGISYCPQ 1719
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqaLQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLD---PLLttTECIRFYGR------LRGIRDLD-QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPT 1789
Cdd:PRK15056 86 SEEVDwsfPVL--VEDVVMMGRyghmgwLRRAKKRDrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1790 VLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQrVAVLRAGQVIAS 1849
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLAS 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1650-1858 |
4.26e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYC-----PQSNPLD 1724
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS--GIDTGdfsklQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1725 PLLTTTECIRFYGR--------------LRGIrDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1790
Cdd:PRK13644 80 GIVFQNPETQFVGRtveedlafgpenlcLPPI-EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1791 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIeHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
861-1064 |
4.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYG-----SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH---------------Q 920
Cdd:PRK13641 7 NVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlkklrkK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQdnilIPTLTAREHLQLyAQIKIPPGGSGGVE-EIRSEVAQTLQSLNFGKHESYPS-WQLSGGYRRRLCVAIAFI 998
Cdd:PRK13641 87 VSLVFQ----FPEAQLFENTVL-KDVEFGPKNFGFSEdEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQL-IERLRQGRAVIFATHFMDE-AKYLSDSLViMRNGRIIAQHS 1064
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDvAEYADDVLV-LEHGKLIKHAS 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
856-1081 |
5.04e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 856 GASLVNVSKLY---GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH------------- 919
Cdd:PRK11831 4 VANLVDMRGVSftrGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 920 -------QVGVCWQD-----NILIPTltaREHLQLYAQIkippggsggveeIRSEVAQTLQSLNF-GKHESYPSwQLSGG 986
Cdd:PRK11831 84 krmsmlfQSGALFTDmnvfdNVAYPL---REHTQLPAPL------------LHSTVMMKLEAVGLrGAAKLMPS-ELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 987 YRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1064
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|....*..
gi 113193620 1065 RDSLQrlctSNYSIRLR 1081
Cdd:PRK11831 228 AQALQ----ANPDPRVR 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1656-1847 |
5.73e-17 |
|
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: 81.93 E-value: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1656 WLAYRRghyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD---VGQIYFE---------QPGISYCPQSNPL 1723
Cdd:cd03234 16 WNKYAR---ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpdqfQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYE------LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVllrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRAVVLTSHS-VSEIEHLCQRVAVLRAGQVI 1847
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1657-1859 |
7.37e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.72 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAVRnVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-----------EQPgISYCPQSNPLDP 1725
Cdd:COG3840 7 LTYRYGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalppaERP-VSMLFQENNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIRFygrlrGIRD-----------LDQFLDRV-LDTYELR-PykdvqvRNLSGGNRRKltVAVTCCGC--TPTV 1790
Cdd:COG3840 85 HLTVAQNIGL-----GLRPglkltaeqraqVEQALERVgLAGLLDRlP------GQLSGGQRQR--VALARCLVrkRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1791 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
887-1062 |
7.77e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEHQ----------------VGVCWQdnilIPtltarEHlQLYAQ----- 945
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkknkklkplrkkVGIVFQ----FP-----EH-QLFEEtvekd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 946 IKIPPGGSGGVEEIRSEVAQTLQSLnFGKHESYPS---WQLSGGYRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKD 1020
Cdd:PRK13634 107 ICFGPMNFGVSEEDAKQKAREMIEL-VGLPEELLArspFELSGGQMRR--VAIAGVLAmePEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1021 IWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13634 184 MMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
858-1062 |
7.84e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------------Q 920
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairllrqK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQDNILIPTLTAREHLqLYAQIKIPpGGSGgvEEIRSEVAQTLQSLNFG-KHESYPSwQLSGGYRRRLCVAIAFIA 999
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENL-IEAPCKVL-GLSK--EQAREKAMKLLARLRLTdKADRFPL-HLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1000 SPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
881-1039 |
8.21e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLTAREHLQLYAQ 945
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklraKHVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 946 IKippGGSGGveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI 1025
Cdd:PRK10584 115 LR---GESSR--QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170
....*....|....*.
gi 113193620 1026 ERL--RQGRAVIFATH 1039
Cdd:PRK10584 190 FSLnrEHGTTLILVTH 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1652-1827 |
1.03e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLwLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-----------YFEQpgISYCPQS 1720
Cdd:PRK13539 5 GEDL-ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiddpdVAEA--CHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NPLDPLLTTTECIRFYGRLRGIRDLDqfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1800
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1801 PVTRDMvyatIEQLLLARRA----VVLTSHS 1827
Cdd:PRK13539 160 AAAVAL----FAELIRAHLAqggiVIAATHI 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1650-1852 |
1.20e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRG----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLDP 1725
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID--GVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LL-----------------TTTECIRFYGRLRGIRDlDQFLDRVLDTYEL-----RPYKDVQVRNLSGGNRRKLTVAvTC 1783
Cdd:PRK13637 81 IRkkvglvfqypeyqlfeeTIEKDIAFGPINLGLSE-EEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIA-GV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1784 CGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1852
Cdd:PRK13637 159 VAMEPKILiLDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
859-1060 |
1.21e-16 |
|
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: 85.62 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLY-----GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKV-LLAGEHQV----------- 921
Cdd:TIGR03269 282 VRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVdmtkpgpdgrg 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 922 ------GVCWQDNILIPTLTAREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHES------YPSwQLSGGYRR 989
Cdd:TIGR03269 362 rakryiGILHQEYDLYPHRTVLDNLTEAIGLELPD------ELARMKAVITLKMVGFDEEKAeeildkYPD-ELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 990 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
875-1070 |
1.30e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 875 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTLTAREhlqLY 943
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAYLPQQLPAAEGMTVRE---LV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 944 AQIKIPPGGS----GGVEEIRSEVAQTLQSLNFGKHESYPSwqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARK 1019
Cdd:PRK10575 107 AIGRYPWHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDS--LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1020 DIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:PRK10575 185 DVLALVHRLSQERGltVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
858-1068 |
1.42e-16 |
|
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: 81.12 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVC 924
Cdd:cd03251 2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQDNILIPTlTAREHLqLYAQikipPGGSggVEEIRsEVAQTLQSLNF--GKHESYPSW------QLSGGYRRRLCVAIA 996
Cdd:cd03251 82 SQDVFLFND-TVAENI-AYGR----PGAT--REEVE-EAARAANAHEFimELPEGYDTVigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1650-1863 |
1.42e-16 |
|
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: 81.12 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN------- 1721
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 -PLDPLL---TTTECIRfYGRLRGIRD----------LDQFLDRVLDTYElrpyKDVQVR--NLSGGNRRKLTVAVTCCG 1785
Cdd:cd03251 81 vSQDVFLfndTVAENIA-YGRPGATREeveeaaraanAHEFIMELPEGYD----TVIGERgvKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1786 CTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1863
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
859-1062 |
1.53e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.31 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQ 920
Cdd:PRK11153 4 LKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQ-----------DNILIPtltarehLQLYAQIKippggsggvEEIRSEVAQTLQSLNFG-KHESYPSwQLSGGYR 988
Cdd:PRK11153 84 IGMIFQhfnllssrtvfDNVALP-------LELAGTPK---------AEIKARVTELLELVGLSdKADRYPA-QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 989 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1650-1858 |
1.70e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1720
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ----NPLDPLL--TTTECIRFyGRLRGIRDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVL 1791
Cdd:PRK13639 82 ivfqNPDDQLFapTVEEDVAF-GPLNLGLSKEEVEKRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1792 MDEPTSDMDPvtrdMVYATIEQLL--LARRA--VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK13639 161 LDEPTSGLDP----MGASQIMKLLydLNKEGitIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1650-1864 |
1.93e-16 |
|
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: 80.74 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-----------GISYC 1717
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSNPL--DpllTTTECIRfYGRL----------RGIRDLDQFLDRVLDTYELRpykdVQVRN--LSGGNRRKLTVAVTC 1783
Cdd:cd03253 81 PQDTVLfnD---TIGYNIR-YGRPdatdeevieaAKAAQIHDKIMRFPDGYDTI----VGERGlkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1784 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1863
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
.
gi 113193620 1864 A 1864
Cdd:cd03253 231 E 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
887-1059 |
2.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.70 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ--DNILIPTlTAREHLQLYAQIK-IPpgg 952
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdirHKIGMVFQnpDNQFVGA-TVEDDVAFGLENKgIP--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 953 sggVEEIRSEVAQTLQ---SLNFGKHEsyPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR 1029
Cdd:PRK13650 114 ---HEEMKERVNEALElvgMQDFKERE--PA-RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR 187
|
170 180 190
....*....|....*....|....*....|..
gi 113193620 1030 Q--GRAVIFATHFMDEAKyLSDSLVIMRNGRI 1059
Cdd:PRK13650 188 DdyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
858-1071 |
2.74e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL------------LAGEHQVGVCW 925
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNILIPTLTAREHLQLYaqiKIPPGGSGGV-----EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIAS 1000
Cdd:PRK09700 87 QELSVIDELTVLENLYIG---RHLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNG-----RIIAQHSRDSLQRL 1071
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVRL 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1648-1846 |
3.03e-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: 78.63 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1648 EAVRAENLWlayrrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGI 1714
Cdd:cd03215 3 PVLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaiRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1715 SYCPQSnpldplltttecirfygRLR-GIrdldqFLDR-VLDTYELRPYkdvqvrnLSGGNRRKLTVAVTCCGCTPTVLM 1792
Cdd:cd03215 78 AYVPED-----------------RKReGL-----VLDLsVAENIALSSL-------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1793 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1665-1849 |
3.41e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQP------------GISYCPQSNPLDPLLTTTE 1731
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEmrfasttaalaaGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIrFYGRL---RGIRDLDQFLDRVLDTYE-----LRPykDVQVRNLSGGNRRKLTVAvtccgctpTVLM--------DEP 1795
Cdd:PRK11288 99 NL-YLGQLphkGGIVNRRLLNYEAREQLEhlgvdIDP--DTPLKYLSIGQRQMVEIA--------KALArnarviafDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1796 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1665-1853 |
3.47e-16 |
|
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: 79.97 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTECIR 1734
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphkrpvntvfQNYALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 FYGRLRGIR--DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR-DMvyaTI 1811
Cdd:cd03300 95 FGLRLKKLPkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRkDM---QL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1812 EQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:cd03300 172 ELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1665-1858 |
3.52e-16 |
|
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: 84.08 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------QPGI-----------------SYCP 1718
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtKPGPdgrgrakryigilhqeyDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLlttTECIRF-----YGRLRGIRDL------DQFLDRVLDTYElrpykdvqvRNLSGGNRRKLTVAVTCCGCT 1787
Cdd:TIGR03269 379 HRTVLDNL---TEAIGLelpdeLARMKAVITLkmvgfdEEKAEEILDKYP---------DELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1788 PTVLMDEPTSDMDPVTRDMVYATIeqlLLARRAV----VLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSI---LKAREEMeqtfIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1666-1847 |
3.52e-16 |
|
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: 78.75 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP--DVGQIYFE---------QPGISYCPQSNPLDPLLTTTECIR 1734
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgrpldkrsfRKIIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 FYGRLRGIrdldqfldrvldtyelrpykdvqvrnlSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQL 1814
Cdd:cd03213 105 FAAKLRGL---------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|....
gi 113193620 1815 LLARRAVVLTSHSVS-EIEHLCQRVAVLRAGQVI 1847
Cdd:cd03213 158 ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
851-1066 |
3.58e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 851 LDGKLGASLVNVSKLYGSkcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI- 929
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 --------------LIPTLTAREHLQLYAQIKIP-PGGSGGVEEIRSEVAQTLQSLNFgkheSYPSWQ-----LSGGYRR 989
Cdd:PRK10762 327 ngivyisedrkrdgLVLGMSVKENMSLTALRYFSrAGGSLKHADEQQAVSDFIRLFNI----KTPSMEqaiglLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 990 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1066
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1654-1852 |
4.04e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1654 NLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ-------------S 1720
Cdd:PRK13638 6 DLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllalrqqvatvfQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NPLDPLLTT--TECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1796
Cdd:PRK13638 85 DPEQQIFYTdiDSDIAFSLRNLGVpeAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1797 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1852
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
858-1062 |
6.20e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDN 928
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREH----LQLYAQIKippggsggvEEIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIAFIASPS 1002
Cdd:PRK11000 85 ALYPHLSVAENmsfgLKLAGAKK---------EEINQRVNQVAEVLQLA-HllDRKPK-ALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRiIAQ 1062
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGR-VAQ 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1659-1849 |
8.11e-16 |
|
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: 79.36 E-value: 8.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1659 YRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQ---IYFEQPG----------ISYCpqSNPLDP 1725
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFGERRGgedvwelrkrIGLV--SPALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIR------FY---GRLRGIRDLDQFL-DRVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVL- 1791
Cdd:COG1119 90 RFPRDETVLdvvlsgFFdsiGLYREPTDEQRERaRELLELLGLAHLADRPFGTLSQGEQRRVLIAralVK----DPELLi 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1792 MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
861-1068 |
9.12e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ-----VGVCWQDN 928
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplHArarrgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHLQLYAQIKippggSGGVEEIRSEVAQTL-QSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIR-----DDLSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1008 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1653-1846 |
1.46e-15 |
|
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: 77.83 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI----------------YFEQP-GIS 1715
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgraipYLRRKiGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1716 YcpQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1793
Cdd:cd03292 84 F--QDFRLLPDRNVYENVAFALEVTGVppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1794 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1650-1845 |
1.60e-15 |
|
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: 75.56 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYCPQsnpldpllt 1728
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 ttecirfygrlrgirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGcTPTVLM-DEPTSDMDPVTRDMV 1807
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLE-NPNLLLlDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 113193620 1808 yatIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:cd03221 110 ---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1651-1846 |
1.63e-15 |
|
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: 76.49 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP----------DVGQIYFEQPG--ISYC 1717
Cdd:cd03246 2 EVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtsgrvrldgaDISQWDPNELGdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQSnplDPLLTTTecirfygrlrgIRDldqfldrvldtyelrpykdvqvrN-LSGGNRRKLTVAVTCCGCTPTVLMDEPT 1796
Cdd:cd03246 82 PQD---DELFSGS-----------IAE-----------------------NiLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1797 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEhLCQRVAVLRAGQV 1846
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1666-1931 |
1.75e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS------------YCPQSNPLDPLLTTTECI 1733
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrrvaSVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1734 RF-----YGRLRGIRDLDQ-FLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtrdmV 1807
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD------I 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1808 YATIEQLLLAR------RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ------RLKSEHGGYYAVTcfCGPAQQA 1875
Cdd:PRK09536 173 NHQVRTLELVRrlvddgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAdvltadTLRAAFDARTAVG--TDPATGA 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1876 ILSRSLNQRLPGARDLQHYAHSLrflvrvrspGSlGD--APLLSELFAILCDVCVNVA 1931
Cdd:PRK09536 251 PTVTPLPDPDRTEAAADTRVHVV---------GG-GQpaARAVSRLVAAGASVSVGPV 298
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
867-1068 |
1.76e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.13 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIpTLT 935
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLqLYAQIKIPPggsggvEEIRsEVAQTLQSLNF---------------GKhesypswQLSGGYRRRLCVAIAFIAS 1000
Cdd:COG1132 430 IRENI-RYGRPDATD------EEVE-EAAKAAQAHEFiealpdgydtvvgerGV-------NLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHfmdeakYLS-----DSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVEQGTHEEL 561
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
859-1068 |
1.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCW 925
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgiRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QD-NILIPTLTAREHLQLYAQ-IKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRrlCVAIAFI--ASP 1001
Cdd:PRK13644 84 QNpETQFVGRTVEEDLAFGPEnLCLPP------IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ--CVALAGIltMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1002 SVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAkYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1664-1855 |
1.99e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1664 YAVRNVNFSVQ-------------RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQP-----------GISYCP 1718
Cdd:PRK10575 12 FALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPLLTTTECI---RF-----YGRLrGIRDLDQfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1790
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigRYpwhgaLGRF-GAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1791 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTS-HSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
867-1039 |
2.36e-15 |
|
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: 81.64 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTlT 935
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPvssldqdevrrRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLYAqikipPGGSGgvEEI-----RSEVAQTLQSLNFGKHESYPSW--QLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:TIGR02868 425 VRENLRLAR-----PDATD--EELwaaleRVGLADWLRALPDGLDTVLGEGgaRLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1009 PCNGVDAKARKDIWQLIERLRQGRAVIFATH 1039
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
826-1068 |
2.40e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 826 YAVIGLAYQRYKKnnYSFVKVSRSQLDGKLGASLvnvsklygskcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQ 905
Cdd:PRK10070 11 YKIFGEHPQRAFK--YIEQGLSKEQILEKTGLSL-----------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 906 IRQSSGKVLLAG---------------EHQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSL 970
Cdd:PRK10070 78 IEPTRGQVLIDGvdiakisdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINA-----EERREKALDALRQV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 971 NFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYL 1047
Cdd:PRK10070 153 GLENYaHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRI 231
|
250 260
....*....|....*....|.
gi 113193620 1048 SDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK10070 232 GDRIAIMQNGEVVQVGTPDEI 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1662-1859 |
2.67e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1731
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyqrpinmmfQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFyGRLRGIRDLDQFLDRVLDTYELRPYKDVQVR---NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD-MV 1807
Cdd:PRK11607 111 NIAF-GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrMQ 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1808 YATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLkSEH 1859
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI-YEH 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
871-1060 |
2.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL---------AGEHQVGVCWQDNI--------LIPT 933
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKKIknfkelrrRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLQLYA-----QIKIPPGGSG-GVEEIRSEVAQTLQSLnfGKHESY---PSWQLSGGYRRRlcVAIAFIAS--PS 1002
Cdd:PRK13631 121 VFQFPEYQLFKdtiekDIMFGPVALGvKKSEAKKLAKFYLNKM--GLDDSYlerSPFGLSGGQKRR--VAIAGILAiqPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
861-1062 |
2.92e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.85 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNI 929
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelaRRRAVLPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTARE--HLQLYAQikipPGGSGGVEEIRSEVAQTLQSLNFGkHESYPswQLSGGYRRR------LC-VAIAFIAS 1000
Cdd:COG4559 86 LAFPFTVEEvvALGRAPH----GSSAAQDRQIVREALALVGLAHLA-GRSYQ--TLSGGEQQRvqlarvLAqLWEPVDGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHfmD---EAKYlSDSLVIMRNGRIIAQ 1062
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLH--DlnlAAQY-ADRILLLHQGRLVAQ 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
861-1059 |
2.93e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.25 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCA--VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 926
Cdd:PRK13648 12 NVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklrKHIGIVFQn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 -DNILIPTLTA-------REHLQLYaqikippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 998
Cdd:PRK13648 92 pDNQFVGSIVKydvafglENHAVPY-------------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 999 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAV--IFATHFMDEAKYlSDSLVIMRNGRI 1059
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1665-1848 |
2.95e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-------------EQPGISYCPQSNPLDPLLTTTE 1731
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpkssQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIrFYGR-----LRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:PRK10762 99 NI-FLGRefvnrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1651-1859 |
2.96e-15 |
|
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: 77.22 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------ 1718
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrqlrrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 ---QSNPLDPLLTTTECIRFyGRL------RGIRDLDQFLDRV-----LDTYELRPYKDVQVRNLSGGNRRKLTVAVTCC 1784
Cdd:cd03256 82 mifQQFNLIERLSVLENVLS-GRLgrrstwRSLFGLFPKEEKQralaaLERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1785 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1664-1848 |
3.19e-15 |
|
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: 76.76 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1664 YAVRNVNFSVQ--RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1731
Cdd:cd03298 10 YGEQPMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrpvsmlfQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFyGRLRGIR-------DLDQFLDRV-LDTYELRpykdvQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1803
Cdd:cd03298 90 NVGL-GLSPGLKltaedrqAIEVALARVgLAGLEKR-----LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1804 RDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLmVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
861-1049 |
3.49e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIK-------LLTGQirQSSGKVLLAGEH-------------Q 920
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNlyapdvdpvevrrR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQDNILIPTltarehlQLYAQIKIPP---GGSGGVEEI--RS--------EVAQTLQslnfgkhESYPSwqLSGGY 987
Cdd:PRK14243 93 IGMVFQKPNPFPK-------SIYDNIAYGArinGYKGDMDELveRSlrqaalwdEVKDKLK-------QSGLS--LSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 988 RRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSD 1049
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1645-1853 |
3.71e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAVRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPGISYCPQS--- 1720
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--TVGGMVLSEETvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ----------NPLDPLLTTT--ECIRFYGRLRGI-RD-----LDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVT 1782
Cdd:PRK13635 79 vrrqvgmvfqNPDNQFVGATvqDDVAFGLENIGVpREemverVDQALRQV----GMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1783 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQ 1853
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1662-1845 |
3.86e-15 |
|
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: 75.97 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGISYCPQSnpldP-LLTTT--ECIRFyGr 1738
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PGSIAYVSQE----PwIQNGTirENILF-G- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1739 lrgiRDLD-QFLDRVLDTYELRPykDVQV-------------RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:cd03250 90 ----KPFDeERYEKVIKACALEP--DLEIlpdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1805 DMVYAT-IEQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQ 1845
Cdd:cd03250 164 RHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1660-1847 |
4.18e-15 |
|
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: 76.15 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1660 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFE-----------QPGISYCPQSNPLDP 1725
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNgipykefaekyPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIRFYGRLRGirdlDQFldrvldtyelrpykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1805
Cdd:cd03233 97 TLTVRETLDFALRCKG----NEF-----------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1806 MVYATIEQLLLARRAVVLTSHSVS--EIEHLCQRVAVLRAGQVI 1847
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
855-1060 |
4.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 855 LGASLVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------ 917
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 918 ---EHQVGVCWQdnilIPtltareHLQLYAQIKIPPGGSG----GVEEIRSEvAQTLQSLNF-GKHESYPS---WQLSGG 986
Cdd:PRK13649 81 kqiRKKVGLVFQ----FP------ESQLFEETVLKDVAFGpqnfGVSQEEAE-ALAREKLALvGISESLFEknpFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 987 YRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK13649 150 QMRR--VAIAGILAmePKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
872-1059 |
5.20e-15 |
|
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: 74.95 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPtltarehl 940
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 qlyaqikippgGSggveeirseVAQTLqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKD 1020
Cdd:cd03246 90 -----------GS---------IAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 113193620 1021 IWQLIERLR-QGRAVIFATHFMdEAKYLSDSLVIMRNGRI 1059
Cdd:cd03246 135 LNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
871-1068 |
5.51e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCWQD---NILIPTLT 935
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLYAQIKIppgGSGGV---EEIRSEVAQTLQSLNFgkheSYPSW-----QLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG1129 347 IRENITLASLDRL---SRGGLldrRRERALAEEYIKRLRI----KTPSPeqpvgNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1008 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
887-1039 |
5.99e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE-------HQV-GVCWQDNILIPTLTAREHLQLYAQIKIPPGGSGg 955
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMpidakemRAIsAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTK- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 956 vEEIRSEVAQTLQSLNF-----------GKHESypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1024
Cdd:TIGR00955 135 -KEKRERVDEVLQALGLrkcantrigvpGRVKG-----LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....*.
gi 113193620 1025 IERLRQ-GRAVIFATH 1039
Cdd:TIGR00955 209 LKGLAQkGKTIICTIH 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1657-1826 |
6.36e-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: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-----------GISYCPQSNPLD 1724
Cdd:cd03231 6 LTCERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiarGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1725 PLLTTTECIRFYGRLRGIRDLDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:cd03231 86 TTLSVLENLRFWHADHSDEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|..
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSH 1826
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1660-1847 |
7.75e-15 |
|
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: 76.08 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1660 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY------FEQPGISYCPQS----------NPL 1723
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdlTLLSGKELRKARrrigmifqhfNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DPlLTTTECIRFYGRLRGIRDLDQfLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDM 1799
Cdd:cd03258 95 SS-RTVFENVALPLEIAGVPKAEI-EERVLELLElvgLEDKADAYPAQLSGGQKQRVGIA-RALANNPKVLLcDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1800 DPVTRDmvyaTIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:cd03258 172 DPETTQ----SILALLrdINRElglTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
861-1049 |
8.01e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLT------GQIRqSSGKVLLAGEH-------------QV 921
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVR-VEGRVEFFNQNiyerrvnlnrlrrQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 922 GVCWQDNILIPtltarehLQLYAQI----KI----PPGGSGGVEEIRSEVAQTLQSLNFGKHESypSWQLSGGYRRRLCV 993
Cdd:PRK14258 91 SMVHPKPNLFP-------MSVYDNVaygvKIvgwrPKLEIDDIVESALKDADLWDEIKHKIHKS--ALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 994 AIAFIASPSVVILDEPCNGVDAKARKDIWQLIE--RLRQGRAVIFATHFMDEAKYLSD 1049
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1652-1826 |
8.20e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-----------YCPQ 1719
Cdd:PRK13538 4 ARNL--ACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyhqdllYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPLLTTTECIRFYGRLRGIRDLDQFLDrVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTCCgctPTVLMDEP- 1795
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArlwLTRA---PLWILDEPf 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 113193620 1796 TS-DMDPVtrdmvyATIEQLLLARRA----VVLTSH 1826
Cdd:PRK13538 158 TAiDKQGV------ARLEALLAQHAEqggmVILTTH 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1665-1852 |
8.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD--------VGQIYF---------EQPGISYcpqSNPLDPLL 1727
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitVDGITLtaktvwdirEKVGIVF---QNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 --TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1803
Cdd:PRK13640 99 gaTVGDDVAFGLENRAVprPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1804 RDMVYATIEQLLLARRAVVLT-SHSVSEIEHLCQrVAVLRAGQVIASDSP 1852
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISiTHDIDEANMADQ-VLVLDDGKLLAQGSP 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1644-1848 |
8.76e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAV-RAENLWlayRRGHyaVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP--------- 1712
Cdd:COG1129 250 AAPGEVVlEVEGLS---VGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgKPvrirsprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 ---GISYCP---QSNPLDPLLTTTE-----CIRFYGRLRGIRD--LDQFLDRVLDTYELR-PYKDVQVRNLSGGNRRKLT 1778
Cdd:COG1129 325 iraGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRrrERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1779 VA---VTCcgctPTVL-MDEPTSDMDPVTRDMVYATIEQLllARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:COG1129 405 LAkwlATD----PKVLiLDEPTRGIDVGAKAEIYRLIREL--AAEgkAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
861-1062 |
1.16e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQV------------GVCWQDN 928
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLadwspaelarrrAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTARE--HLQLYaqikipPGGSGGVEEiRSEVAQTLQSLNFG--KHESYPswQLSGGYRRRlcVAIAFI------ 998
Cdd:PRK13548 86 SLSFPFTVEEvvAMGRA------PHGLSRAED-DALVAAALAQVDLAhlAGRDYP--QLSGGEQQR--VQLARVlaqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 999 --ASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
866-1060 |
1.40e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.72 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-----QSSGKVLLAGehqvgvcwQDNILIPTLTAREHL 940
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDG--------QDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYAQIKIP-PGGS---------------GGVEEIRSEVAQTLQSLNFGKHE----SYPSWQLSGGYRRRLCVAIAFIAS 1000
Cdd:PRK14247 85 QMVFQIPNPiPNLSifenvalglklnrlvKSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
869-1087 |
1.51e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 869 KCAVSNLSLDFARNQVSCLLGRNGAGKS----TLIKLL--------TGQIRQSSGKVLLAGE--------HQVGVCWQDN 928
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEqtlrgvrgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 I--LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNF----GKHESYPSwQLSGGYRRRLCVAIAFIASPS 1002
Cdd:PRK15134 102 MvsLNPLHTLEK--QLYEVLSLHRGMRR--EAARGEILNCLDRVGIrqaaKRLTDYPH-QLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQRLCTSNYSIRL 1080
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKL 256
|
....*..
gi 113193620 1081 RCADATG 1087
Cdd:PRK15134 257 LNSEPSG 263
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1657-1859 |
1.55e-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: 76.00 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------QPGISYCPQS 1720
Cdd:TIGR02769 17 LFGAKQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlyqldrkqrrafRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NP--LDPLLTTTECI----RFYGRLRGIRDLDQFLDrVLDTYELRP-YKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1793
Cdd:TIGR02769 97 SPsaVNPRMTVRQIIgeplRHLTSLDESEQKARIAE-LLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1794 EPTSDMDPVTRdmvyATIEQLLLARR-----AVVLTSHSVSEIEHLCQRVAVLRAGQVIAS-DSPQRLKSEH 1859
Cdd:TIGR02769 176 EAVSNLDMVLQ----AVILELLRKLQqafgtAYLFITHDLRLVQSFCQRVAVMDKGQIVEEcDVAQLLSFKH 243
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
957-1069 |
1.56e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.47 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 957 EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVI 1035
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVL 198
|
90 100 110
....*....|....*....|....*....|....
gi 113193620 1036 FATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1069
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1648-1858 |
1.78e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1648 EAVRAENLWLAYRRG-----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS-- 1720
Cdd:PRK13633 3 EMIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTSDEEnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ------------NPLDPLLTTT--ECIRFYGRLRGI------RDLDQFLDRVlDTYElrpYKDVQVRNLSGGNRRKLTVA 1780
Cdd:PRK13633 81 wdirnkagmvfqNPDNQIVATIveEDVAFGPENLGIppeeirERVDESLKKV-GMYE---YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1781 VTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQllLARR---AVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKKygiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 113193620 1858 E 1858
Cdd:PRK13633 234 E 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1650-1859 |
1.83e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAY--RRghyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-----------GIS 1715
Cdd:PRK11231 3 LRTENLTVGYgtKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPismlssrqlarRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1716 YCPQSNPLDPLLTTTECI--------RFYGRLRGirDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1787
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVaygrspwlSLWGRLSA--EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1788 PTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
861-1062 |
2.07e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQV------------------- 921
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseaerrrllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 922 -GVCWQDniliptltAREHLQLyaqiKIPPGGSGG----------VEEIRSEVAQTLQ--SLNFGKHESYPSwQLSGGYR 988
Cdd:PRK11701 91 wGFVHQH--------PRDGLRM----QVSAGGNIGerlmavgarhYGDIRATAGDWLErvEIDAARIDDLPT-TFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 989 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1650-1858 |
2.35e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ---------- 1719
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmklresvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 ---SNPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLM 1792
Cdd:PRK13636 86 mvfQDPDNQLFSASvyQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1793 DEPTSDMDPV-TRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK13636 166 DEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
866-1062 |
2.41e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 866 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTL 934
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 TAREhlqLYAQIKIP--PGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:PRK10253 97 TVQE---LVARGRYPhqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1013 VDAKARKDIWQLIERLRQGRAVIFAT--HFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAvlHDLNQACRYASHLIALREGKIVAQ 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1651-1853 |
2.95e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1651 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------ 1718
Cdd:PRK11701 8 SVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 --------QSNPLD--------------PLLTTTEciRFYGRLRgiRDLDQFLDRVldtyELRPYK-DVQVRNLSGGNRR 1775
Cdd:PRK11701 87 lrtewgfvHQHPRDglrmqvsaggnigeRLMAVGA--RHYGDIR--ATAGDWLERV----EIDAARiDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1776 KLTVA---VTccgcTPT-VLMDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK11701 159 RLQIArnlVT----HPRlVFMDEPTGGLD-VS---VQARLLDLLrgLVRElglAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....
gi 113193620 1847 IAS-------DSPQ 1853
Cdd:PRK11701 231 VESgltdqvlDDPQ 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
858-1060 |
2.99e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGS-----KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-------EHQ----V 921
Cdd:COG1101 3 ELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpEYKrakyI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 922 GVCWQDNIL--IPTLTAREHLQL-YAQIKIPPGGSGGVEEIRSEVAQTLQSLNFG--KHESYPSWQLSGGYRRRLCVAIA 996
Cdd:COG1101 83 GRVFQDPMMgtAPSMTIEENLALaYRRGKRRGLRRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1662-1857 |
3.62e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP-QSNPLDPLLTTTECIRFYGRLR 1740
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1741 GIRDL--------------------------DQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVAVtcCGCT-PTV 1790
Cdd:PRK11300 97 VIENLlvaqhqqlktglfsgllktpafrraeSEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIAR--CMVTqPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1791 LM-DEPTSDMDPVTRDMVYATIEQLllaRR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:PRK11300 175 LMlDEPAAGLNPKETKELDELIAEL---RNehnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
871-1064 |
7.19e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDniliPT--LTAR 937
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysyrsqRIRMIFQD----PStsLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 EHLQLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1016
Cdd:PRK15112 104 QRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1017 ARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1064
Cdd:PRK15112 184 MRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
861-1062 |
8.04e-14 |
|
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: 76.68 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgVCWQDnILIPTLtaRE 938
Cdd:TIGR02203 335 NVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-----HDLAD-YTLASL--RR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 HLQLYAQ------------IKIPPGGSGGVEEIRSEVAQT-LQSL----------NFGKHESypswQLSGGYRRRLCVAI 995
Cdd:TIGR02203 407 QVALVSQdvvlfndtiannIAYGRTEQADRAEIERALAAAyAQDFvdklplgldtPIGENGV----LLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQ 1062
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1646-1852 |
9.36e-14 |
|
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: 72.06 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1646 TGEaVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN--- 1721
Cdd:cd03369 4 HGE-IEVENLSVRYAPDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 -----PLDPLLtttecirFYGRLRGirDLDQFlDRvldtyelrpYKDVQVR----------NLSGGNRRKLTVAVTCCGC 1786
Cdd:cd03369 83 sltiiPQDPTL-------FSGTIRS--NLDPF-DE---------YSDEEIYgalrvsegglNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1787 TPTVLMDEPTSDMDPVTRDMVYATIEQLLlaRRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSP 1852
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTiAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1660-1930 |
1.09e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.73 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1660 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycpqsnPLDPlltttecirfyGRL 1739
Cdd:COG1135 15 GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT------ALSE-----------REL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1740 RGIR-------------------------------DLDQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVA---VT 1782
Cdd:COG1135 78 RAARrkigmifqhfnllssrtvaenvalpleiagvPKAEIRKRVaelLELVGLSDKADAYPSQLSGGQKQRVGIAralAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1783 ccgcTPTVLM-DEPTSDMDPVTRDmvyaTIEQLLL-ARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIasdspqrlk 1856
Cdd:COG1135 158 ----NPKVLLcDEATSALDPETTR----SILDLLKdINRelglTIVLITHEMDVVRRICDRVAVLENGRIV--------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1857 sEHGGYYAVtcFCGPAQ---QAILSRSLNQRLPG--ARDLQHYAHSLRfLVRVRSPGSLGDAPLLSELFAILcDVCVNV 1930
Cdd:COG1135 221 -EQGPVLDV--FANPQSeltRRFLPTVLNDELPEelLARLREAAGGGR-LVRLTFVGESADEPLLSELARRF-GVDVNI 294
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
858-1068 |
1.25e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGvcWQDNILIPTLTA- 936
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD--WQTAKIMREAVAi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 937 -REHLQLYAQIKIPPG-GSGGVEEIRSEVAQTLQSLnfgkHESYPSWQ---------LSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:PRK11614 85 vPEGRRVFSRMTVEENlAMGGFFAERDQFQERIKWV----YELFPRLHerriqragtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1663-1855 |
1.27e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1663 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE--------------QPGISYcpqSNPLDPLL- 1727
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteenvwdirhKIGMVF---QNPDNQFVg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 -TTTECIRFYGRLRGIrDLDQFLDRVLDTYEL---RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1803
Cdd:PRK13650 97 aTVEDDVAFGLENKGI-PHEEMKERVNEALELvgmQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1804 RDMVYATIEQLLLARRAVVLT-SHSVSEIEhLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISiTHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
861-1061 |
1.36e-13 |
|
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: 75.63 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEHQVG------------VCWQ 926
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKAsnirdteragivIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTAREHLQLYAQIKIpPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITL-PGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1666-1853 |
1.51e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------QSNPLDPLLTTTECI 1733
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelakrlailrQENHINSRLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1734 RF----Y--GRLRGiRDlDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMdpvtrDMV 1807
Cdd:COG4604 97 AFgrfpYskGRLTA-ED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNL-----DMK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1808 YAT-IEQLL--LAR---RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:COG4604 170 HSVqMMKLLrrLADelgKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1667-1849 |
1.84e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1667 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTECI 1733
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltpakahQLGIYLVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1734 RF-----YGRLRGIRDLDQFLDRVLD------TYELrpyKDVQVRNLSGGNRRKLTVavtccgctptVLMDEPTSDMDPV 1802
Cdd:PRK15439 108 LFglpkrQASMQKMKQLLAALGCQLDldssagSLEV---ADRQIVEILRGLMRDSRI----------LILDEPTASLTPA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1803 TRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
861-1071 |
2.18e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-------------QVGVCWQD 927
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpkvderlirqEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLqLYAQIKIPPGGSGGVEEIRSEVaqtLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK09493 86 FYLFPHLTALENV-MFGPLRVRGASKEEAEKQAREL---LAKVGLAERAHhYPS-ELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL------QRL 1071
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLiknppsQRL 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1657-1826 |
2.52e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAVRN-VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QPG--------ISYCPQSNPLDPL 1726
Cdd:PRK13543 17 LAFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTAtrgdrsrfMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1727 LTTTECIRFYGRLRGiRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDM 1806
Cdd:PRK13543 97 LSTLENLHFLCGLHG-RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 113193620 1807 VYATIEQLLLARRAVVLTSH 1826
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1667-1846 |
2.60e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1667 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ-------------PGISYCPQSNP-----LDPLLT 1728
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalstaqrlaRGLVYLPEDRQssglyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIRFYGR----LRGIRDldqflDRVLDTYELR-----PYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSD 1798
Cdd:PRK15439 360 WNVCALTHNRrgfwIKPARE-----NAVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIA-KCLEASPQLLIvDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1665-1887 |
3.63e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.53 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------------QPGISYCPQSNPLDPLLT 1728
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIRFYGRLRGIRDLDQfLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1805
Cdd:PRK10070 123 VLDNTAFGMELAGINAEER-REKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1806 MVYATIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVTCFCGP------AQQAILS 1878
Cdd:PRK10070 202 EMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVdisqvfSAKDIAR 281
|
250
....*....|..
gi 113193620 1879 RSLN---QRLPG 1887
Cdd:PRK10070 282 RTPNgliRKTPG 293
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
867-1062 |
3.96e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKST----LIKLLTGQ---------IRQSSGKVLLAGEHQVGVCWQD--NILI 931
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgqpLHNLNRRQLLPVRHRIQVVFQDpnSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTArehLQLYA---QIKIPPGGSGGVEEirsEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK15134 377 PRLNV---LQIIEeglRVHQPTLSAAQREQ---QVIAVMEEvgLDPETRHRYPA-EFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1653-1852 |
4.57e-13 |
|
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: 70.60 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG--------------ISYC 1717
Cdd:cd03244 6 KNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID--GvdiskiglhdlrsrISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1718 PQsnplDPLLtttecirFYGRLRgiRDLDQF-------LDRVLDTYELRPY-------KDVQV----RNLSGGNRRKLTV 1779
Cdd:cd03244 84 PQ----DPVL-------FSGTIR--SNLDPFgeysdeeLWQALERVGLKEFveslpggLDTVVeeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1780 AVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSP 1852
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
847-1068 |
4.60e-13 |
|
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: 74.78 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 847 SRSQLDGKLGASLVNVSKLYGSKcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQvgvcwq 926
Cdd:TIGR01193 466 ELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL------ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLtaREHLQLYAQIKIPPGGS----------GGVE-----------EIRSEVAQTlqSLNFGKHESYPSWQLSG 985
Cdd:TIGR01193 539 KDIDRHTL--RQFINYLPQEPYIFSGSilenlllgakENVSqdeiwaaceiaEIKDDIENM--PLGYQTELSEEGSSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 986 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIwqlIERLR--QGRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQH 1063
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLLnlQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
....*
gi 113193620 1064 SRDSL 1068
Cdd:TIGR01193 691 SHDEL 695
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1650-1855 |
4.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-------------GIS 1715
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgEPitkenirevrkfvGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1716 YcpqSNPLDPLLTTT--ECIRFYGRLRGIRD--LDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVL 1791
Cdd:PRK13652 84 F---QNPDDQIFSPTveQDIAFGPINLGLDEetVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIA-GVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1792 -MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13652 160 vLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
882-1039 |
6.56e-13 |
|
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: 69.19 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 882 NQVSCLLGRNGAGKSTLIKLLTGQIRQS--SGKVLLAG-------EHQVGVCWQDNILIPTLTAREHLQLYAQIKippgg 952
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGrpldknfQRSTGYVEQQDVHSPNLTVREALRFSALLR----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 953 sggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQG 1031
Cdd:cd03232 108 -----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSG 158
|
....*...
gi 113193620 1032 RAVIFATH 1039
Cdd:cd03232 159 QAILCTIH 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
975-1059 |
7.05e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 975 HESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVI 1053
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLV 475
|
....*.
gi 113193620 1054 MRNGRI 1059
Cdd:PRK15439 476 MHQGEI 481
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1676-1841 |
7.87e-13 |
|
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: 70.47 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1676 GECFGLLGKNGAGKSTIFKLLTGQLQPDVG--------------------QIYFEQ-------PGISycPQSNPLDPLlt 1728
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselQNYFTKllegdvkVIVK--PQYVDLIPK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 tteciRFYGRLRGI---RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1805
Cdd:cd03236 102 -----AVKGKVGELlkkKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 113193620 1806 MVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVL 1841
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
872-1068 |
9.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQ--DNILIPTlTARE 938
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrrKIGMVFQnpDNQFVGA-TVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 HLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:PRK13642 102 DVAFGMENQGIPR-----EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1019 KDIWQLIERLRQGR--AVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK13642 177 QEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
860-1060 |
9.15e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIK-----LLTGQIRQSSGKVLLAGEH-------------QV 921
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNiyspdvdpievrrEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 922 GVCWQDNILIPTLTAREHLQLYAQIKippGGSGGVEEIRSEVAQTLQSLNF-----GKHESYPSwQLSGGYRRRLCVAIA 996
Cdd:PRK14267 88 GMVFQYPNPFPHLTIYDNVAIGVKLN---GLVKSKKELDERVEWALKKAALwdevkDRLNDYPS-NLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1649-1847 |
1.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGIsYCPQSNPL 1723
Cdd:PRK14267 4 AIETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNI-YSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 D---------------PLLTTTECI----RFYGRLRGIRDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLT 1778
Cdd:PRK14267 82 EvrrevgmvfqypnpfPHLTIYDNVaigvKLNGLVKSKKELDERVEWALKKAAL--WDEVKDRlndypsNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1779 VAVTCCGCTPTVLMDEPTSDMDPVTRdmvyATIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGT----AKIEELLFELKkeyTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
861-1060 |
1.05e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLY---------GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehqvgvCWQDNILI 931
Cdd:PRK10419 8 GLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----------SWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTA-----REHLQLYAQIkiPPGGSG---GVEEIRSEVAQTLQSLNFGKHES------------------YPSwQLSG 985
Cdd:PRK10419 78 KLNRAqrkafRRDIQMVFQD--SISAVNprkTVREIIREPLRHLLSLDKAERLArasemlravdlddsvldkRPP-QLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 986 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1665-1845 |
1.10e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.39 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGisycpqsNPLDpLLTTTECIRFYGRLRGIRD 1744
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-------GWVD-LAQASPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1745 LDQFLD---RV--LDT-----YEL---RPYKDVQVRNL------------------SGGNRRKLTVAVTCCGCTPTVLMD 1793
Cdd:COG4778 98 VSQFLRvipRVsaLDVvaeplLERgvdREEARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1794 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1663-1851 |
1.18e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1663 HY----AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPL-DPLLTTTECIRFYG 1737
Cdd:PRK11614 14 HYgkiqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1738 RLRGIRDL---------DQFLDRVLDTYELRP----YKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:PRK11614 94 RMTVEENLamggffaerDQFQERIKWVYELFPrlheRRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1851
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
871-1062 |
1.25e-12 |
|
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: 72.79 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRqSSGKVLLAGEHqvgvcwqdnilIPTLTAREHLQLYAQIKI-- 948
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQD-----------LDGLSRRALRPLRRRMQVvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 949 ------------------------PPGGSGgvEEIRSEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPS 1002
Cdd:COG4172 369 qdpfgslsprmtvgqiiaeglrvhGPGLSA--AERRARVAEALEEvgLDPAARHRYPH-EFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1003 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLqrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
872-1062 |
1.26e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKS----TLIKLLTGQIRQSSGKVLLAGEHQVGvCWQDNILIPTLtarehlqlyaqIK 947
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP-CALRGRKIATI-----------MQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 IPPGGSGGVEEIRSEVAQTLQSLnfGKH----------------------ESYPsWQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:PRK10418 87 NPRSAFNPLHTMHTHARETCLAL--GKPaddatltaaleavglenaarvlKLYP-FEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
874-1068 |
1.29e-12 |
|
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: 69.49 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTlTAREHLQL 942
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsQIGLVSQEPVLFDG-TIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 yaqikippGGSGGVEEIRSEVAQTLQSLNF------------GKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:cd03249 100 --------GKPDATDEEVEEAAKKANIHDFimslpdgydtlvGERGS----QLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1011 NGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
858-1061 |
1.33e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 926
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTARE--------HLQLYAQIKipPGGSGGVEEI--RSEVAQtlqslnFGKHesyPSWQLSGGYRRRLCVAIA 996
Cdd:PRK09536 85 DTSLSFEFDVRQvvemgrtpHRSRFDTWT--ETDRAAVERAmeRTGVAQ------FADR---PVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 997 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1646-1848 |
1.62e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1646 TGEAV-RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------Q 1711
Cdd:COG3845 253 PGEVVlEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeditglsprerrR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1712 PGISYCPQsnplDPL-------LTTTECI--RFYGRL----RGIRD---LDQFLDRVLDTYELR-PYKDVQVRNLSGGNR 1774
Cdd:COG3845 333 LGVAYIPE----DRLgrglvpdMSVAENLilGRYRRPpfsrGGFLDrkaIRAFAEELIEEFDVRtPGPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1775 RKLTVA--VTccgCTPTVL-MDEPTSDMDPVTRDMVYatieQLLLARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:COG3845 409 QKVILAreLS---RDPKLLiAAQPTRGLDVGAIEFIH----QRLLELRdagaAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
.
gi 113193620 1848 A 1848
Cdd:COG3845 482 G 482
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1650-1852 |
1.73e-12 |
|
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: 72.14 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDVGQIYFEqpgISYCPQSNPLD-PL 1726
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH---VALCEKCGYVErPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1727 LTTTEC-----------IRFYG------------------RLRGIRDLDQFLDRVLDTYELRPYK-------------DV 1764
Cdd:TIGR03269 77 KVGEPCpvcggtlepeeVDFWNlsdklrrrirkriaimlqRTFALYGDDTVLDNVLEALEEIGYEgkeavgravdlieMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1765 QV--------RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLC 1835
Cdd:TIGR03269 157 QLshrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLS 236
|
250
....*....|....*..
gi 113193620 1836 QRVAVLRAGQVIASDSP 1852
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTP 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1668-1800 |
1.83e-12 |
|
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: 72.28 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPGISYCPQS-NPLDPLLTTTECIRfygrlrgiRDL 1745
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQSrDALDPNKTVWEEIS--------GGL 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1746 DQFldrVLDTYEL--RPY--------KDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1800
Cdd:TIGR03719 412 DII---KLGKREIpsRAYvgrfnfkgSDQQkkVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1649-1858 |
2.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ--------- 1719
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrskvgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 --SNPLDPLLTTT--ECIRFYGRLRGIRDlDQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLM 1792
Cdd:PRK13647 84 vfQDPDDQVFSSTvwDDVAFGPVNMGLDK-DEVERRVeeaLKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1793 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
861-1061 |
2.20e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEHQ------------VGVCWQ 926
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqasnirdteragIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTAREHLQLYAQIKipPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEIT--PGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1007 DEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1665-1850 |
2.30e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPD---VGQIYF-------------EQPGISYCPQSNPLDPLLT 1728
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFegeelqasnirdtERAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIrFYGR---LRGIRDLDQFL---DRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSdmdPV 1802
Cdd:PRK13549 99 VLENI-FLGNeitPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA---SL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1803 TRdmvyATIEQLL-----LARRAV--VLTSHSVSEIEHLCQRVAVLRAGQVIASD 1850
Cdd:PRK13549 175 TE----SETAVLLdiirdLKAHGIacIYISHKLNEVKAISDTICVIRDGRHIGTR 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1669-1846 |
2.57e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1669 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-------FEQP------GISYCPQSNPLD---PLLTTTE- 1731
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidIRSPrdairaGIMLCPEDRKAEgiiPVHSVADn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 ----CIRFYGRLRGIRD-------LDQFLDRvldtyeLR---PYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:PRK11288 352 inisARRHHLRAGCLINnrweaenADRFIRS------LNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
869-1064 |
3.47e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 869 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTG-------------------------QIRQSSGKVLLAGEHQ-VG 922
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnskitvdgitltaktvwDIREKVGIVFQNPDNQfVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQDNI---LIPTLTAREHLqlyaqIKIppggsggVEEIRSEVAQtlqsLNFGKHEsyPSWqLSGGYRRRlcVAIAFIA 999
Cdd:PRK13640 100 ATVGDDVafgLENRAVPRPEM-----IKI-------VRDVLADVGM----LDYIDSE--PAN-LSGGQKQR--VAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1000 S--PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQHS 1064
Cdd:PRK13640 159 AvePKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
887-1058 |
3.56e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGE-------HQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGGSggvE 957
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqilKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLT---K 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 958 EIRSEVAQTLQS-LNFGKHESYPSWQ-----LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ- 1030
Cdd:PLN03211 176 QEKILVAESVISeLGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQk 255
|
170 180
....*....|....*....|....*....
gi 113193620 1031 GRAVIFATHFMDEAKY-LSDSLVIMRNGR 1058
Cdd:PLN03211 256 GKTIVTSMHQPSSRVYqMFDSVLVLSEGR 284
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1658-1919 |
3.99e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1658 AYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycpqsnPLDP------------ 1725
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT------ALSEkelrkarrqigm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 ------LL---TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCcGCTPTVLM-D 1793
Cdd:PRK11153 87 ifqhfnLLssrTVFDNVALPLELAGTpkAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL-ASNPKVLLcD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1794 EPTSDMDPVTRDmvyaTIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIasdspqrlksEHGGYYAVtcF 1868
Cdd:PRK11153 166 EATSALDPATTR----SILELLkdINRElglTIVLITHEMDVVKRICDRVAVIDAGRLV----------EQGTVSEV--F 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1869 CGPAQ---QAILSRSLNQRLPG---ARDLQHYAHSLRFLVRVRSPGSLGDAPLLSEL 1919
Cdd:PRK11153 230 SHPKHpltREFIQSTLHLDLPEdylARLQAEPTTGSGPLLRLEFTGESVDAPLLSET 286
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1665-1871 |
4.50e-12 |
|
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: 68.13 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------QPGISYCPQSNPLDPLLTTTECIR 1734
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvqERNVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 FYGRLRGIR------DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDMDPVTRdmv 1807
Cdd:cd03296 97 FGLRVKPRSerppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA-RALAVEPKVLLlDEPFGALDAKVR--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1808 yatiEQLllaRR-----------AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLkSEHGGYYAVTCFCGP 1871
Cdd:cd03296 173 ----KEL---RRwlrrlhdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV-YDHPASPFVYSFLGE 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1649-1853 |
5.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.48 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGH-YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS------- 1720
Cdd:PRK13632 7 MIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID--GITISKENlkeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ------NPLDPLL--TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1790
Cdd:PRK13632 85 igiifqNPDNQFIgaTVEDDIAFGLENKKVppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1791 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEhLCQRVAVLRAGQVIASDSPQ 1853
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
871-1069 |
6.75e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCWQDNILIPTLTARE 938
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfngpkssqEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 HLQLYAQIKIPPGGSGGvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:PRK10762 99 NIFLGREFVNRFGRIDW-KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1019 KDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1069
Cdd:PRK10762 178 ESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1650-1858 |
8.47e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD--------------------VGQIYF 1709
Cdd:PRK09984 5 IRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1710 EQPGISYCPQSNPLDPLLTTTE---------------CIRFYGRLRGIRDLdQFLDRVldtyELRPYKDVQVRNLSGGNR 1774
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLEnvligalgstpfwrtCFSWFTREQKQRAL-QALTRV----GMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1775 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*
gi 113193620 1854 RLKSE 1858
Cdd:PRK09984 239 QFDNE 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1653-1847 |
9.65e-12 |
|
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: 69.71 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRGHY---AVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQLQPDVGQIYFE--------------- 1710
Cdd:COG4172 10 EDLSVAFGQGGGtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgqdllglserelrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1711 ----------QPGISycpqsnpLDPLLTT----TECIRFYGRLRG------IRDLdqfLDRV--------LDTYelrPYK 1762
Cdd:COG4172 90 rgnriamifqEPMTS-------LNPLHTIgkqiAEVLRLHRGLSGaaararALEL---LERVgipdperrLDAY---PHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1763 dvqvrnLSGGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQ 1836
Cdd:COG4172 157 ------LSGGQRQRVMIAMALA-NEPDLLIaDEPTTALD-VT---VQAQILDLLkdLQRElgmALLLITHDLGVVRRFAD 225
|
250
....*....|.
gi 113193620 1837 RVAVLRAGQVI 1847
Cdd:COG4172 226 RVAVMRQGEIV 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1668-1826 |
1.18e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-GISYCPQSNPLDPLLTTTecIRFYGRLR-GIRDL 1745
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLDTTLPLT--VNRFLRLRpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1746 DQF--LDRVLDTYELrpykDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLllaRR---- 1819
Cdd:PRK09544 100 DILpaLKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL---RReldc 172
|
....*..
gi 113193620 1820 AVVLTSH 1826
Cdd:PRK09544 173 AVLMVSH 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1659-1855 |
1.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1659 YRRG----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLLT------ 1728
Cdd:PRK13646 12 YQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKrigmvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 ----------TTECIRFYGRLRGIRDLDQFLDRVL----------DTYELRPYKdvqvrnLSGGNRRKLTVaVTCCGCTP 1788
Cdd:PRK13646 92 qfpesqlfedTVEREIIFGPKNFKMNLDEVKNYAHrllmdlgfsrDVMSQSPFQ------MSGGQMRKIAI-VSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1789 TVL-MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13646 165 DIIvLDEPTAGLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1665-1879 |
1.25e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAG--KSTIFKLLTGqlqPDVGQiyfeQPG--ISYCPQSNPLDPLLTTTECIR------ 1734
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR----RPWrf*TWCANRRALRRTIG*HRPVR*grres 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 FYGRLR----------GIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:NF000106 101 FSGRENlymigr*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYyavTCFCGPAQQAILSR 1879
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR---TLQIRPAHAAELDR 252
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
876-1069 |
1.43e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 876 SLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-HQ--------VGVCWQDNILIPTLTAREH--LQLYA 944
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTttppsrrpVSMLFQENNLFSHLTVAQNigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 945 QIKIPPGGSGGVEEIRSEVAqtLQSLnfgkHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1024
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMG--IEDL----LARLPG-QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1025 IERLRQGRAV--IFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1069
Cdd:PRK10771 172 VSQVCQERQLtlLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1657-1847 |
1.58e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------QPGISYCPQS 1720
Cdd:PRK10419 18 LSGKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklnraqrkafRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NP--LDPLLTTTECIRfyGRLRGIRDLDQF-----LDRVLDTYELRPyKDVQVR--NLSGGNRRKLTVAvTCCGCTPT-V 1790
Cdd:PRK10419 98 SIsaVNPRKTVREIIR--EPLRHLLSLDKAerlarASEMLRAVDLDD-SVLDKRppQLSGGQLQRVCLA-RALAVEPKlL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1791 LMDEPTSDMDPVTRdmvyATIEQLLLARR-----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK10419 174 ILDEAVSNLDLVLQ----AGVIRLLKKLQqqfgtACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1649-1800 |
1.73e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYaVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYCPQ--SNPLDP 1725
Cdd:PRK15064 319 ALEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQdhAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIRFYgrlRGIRDLDQ----FLDRVLDTYElrpykDV--QVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1799
Cdd:PRK15064 398 DLTLFDWMSQW---RQEGDDEQavrgTLGRLLFSQD-----DIkkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
.
gi 113193620 1800 D 1800
Cdd:PRK15064 470 D 470
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
860-1062 |
1.74e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAVSNLSLdfARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----EHQVGVC----------- 924
Cdd:PRK11144 4 LNFKQQLGDLCLTVNLTL--PAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGIClppekrrigyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 925 WQDNILIPTLTAREHLQlYaqikippggsGGVEEIRSEVAQTLQSLNFGKH-ESYPsWQLSGGYRRRlcVAI--AFIASP 1001
Cdd:PRK11144 82 FQDARLFPHYKVRGNLR-Y----------GMAKSMVAQFDKIVALLGIEPLlDRYP-GSLSGGEKQR--VAIgrALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1002 SVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAReiNIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
860-1068 |
1.75e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 860 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSG-----KVLLAGE------------HQVG 922
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRsifnyrdvlefrRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQ----------DNILIPT----LTAREHLQLYAQIKIPPGGsggveeIRSEVAQTLQSLNFgkhesypswQLSGGYR 988
Cdd:PRK14271 105 MLFQrpnpfpmsimDNVLAGVrahkLVPRKEFRGVAQARLTEVG------LWDAVKDRLSDSPF---------RLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 989 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
871-1062 |
1.78e-11 |
|
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: 68.94 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKS----TLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNI-- 929
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllglserelrrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTL---------QSLNfgkheSYPSwQLSGGYRRRLCVAIAFIAS 1000
Cdd:COG4172 105 LNPLHTIGK--QIAEVLRLHRGLSG--AAARARALELLervgipdpeRRLD-----AYPH-QLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1001 PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1657-1859 |
1.97e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAVRnVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------QPGISYCPQSNPLDPL 1726
Cdd:PRK10771 7 ITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttppsRRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1727 LTTTECIRFyGRLRGIR-------DLDQFLDRV-LDTYELR-PYKdvqvrnLSGGNRRKltVAVTCCGC--TPTVLMDEP 1795
Cdd:PRK10771 86 LTVAQNIGL-GLNPGLKlnaaqreKLHAIARQMgIEDLLARlPGQ------LSGGQRQR--VALARCLVreQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1796 TSDMDPVTRDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
855-1066 |
2.46e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 855 LGASLVNVSKLYGSKCAvSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVG 922
Cdd:PRK11288 253 LGEVRLRLDGLKGPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQDNI---LIPTLTAREHLQLYAQIKIPPGG---SGGVEEirsEVAQT-LQSLNFgkheSYPSWQ-----LSGGYRRR 990
Cdd:PRK11288 332 LCPEDRKaegIIPVHSVADNINISARRHHLRAGcliNNRWEA---ENADRfIRSLNI----KTPSREqlimnLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 991 lcvAI--AFIASP-SVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1066
Cdd:PRK11288 405 ---AIlgRWLSEDmKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELARE 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
859-1061 |
2.47e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLY----GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------------E 918
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadalaqlrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 919 HqVGVCWQDNILIPTLTAREHlqlyaqIKIPPGGSGGVEEIRSEVAQTL-QSLNFGKHESYPSWQLSGGYRRRLCVAIAF 997
Cdd:PRK10535 87 H-FGFIFQRYHLLSHLTAAQN------VEVPAVYAGLERKQRLLRAQELlQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYlSDSLVIMRNGRIIA 1061
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVR 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
871-1061 |
2.49e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.51 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------------------HQVGvcwqdn 928
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgvayipedrLGRG------ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 iLIPTLTAREHLQLYAQIKiPPGGSGGV---EEIRsEVAQTL--------QSLNfgkhesYPSWQLSGGYRRRLCVAIAF 997
Cdd:COG3845 347 -LVPDMSVAENLILGRYRR-PPFSRGGFldrKAIR-AFAEELieefdvrtPGPD------TPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQ-LIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
871-1060 |
2.57e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKV-----LLAGEHQ--------------------VGVCW 925
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRqvielseqsaaqmrhvrgadMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 926 QDNI--LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNFGKHES----YPSwQLSGGYRRRLCVAIAFIA 999
Cdd:PRK10261 111 QEPMtsLNPVFTVGE--QIAESIRLHQGASR--EEAMVEAKRMLDQVRIPEAQTilsrYPH-QLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1000 SPSVVILDEPCNGVDAKARKDIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1650-1864 |
2.62e-11 |
|
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: 65.64 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAY--RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpg 1713
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdlnlrwlrSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1714 ISYCPQsnplDPLL---TTTECIRfYGRLRGIRDLDQ----------FLDRVLDTYelrpykDVQVRN----LSGGNRRK 1776
Cdd:cd03249 79 IGLVSQ----EPVLfdgTIAENIR-YGKPDATDEEVEeaakkanihdFIMSLPDGY------DTLVGErgsqLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1777 LTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLK 1856
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVI-AHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
....*...
gi 113193620 1857 SEHGGYYA 1864
Cdd:cd03249 226 AQKGVYAK 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
861-1060 |
2.64e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL------------TGQIR--------QSSGKVLLAGEhq 920
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVynghniysPRTDTVDLRKE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQDNILIPtLTAREH----LQLyAQIKIPPGGSGGVEE------IRSEVAQTLqslnfgkHESypSWQLSGGYRRR 990
Cdd:PRK14239 88 IGMVFQQPNPFP-MSIYENvvygLRL-KGIKDKQVLDEAVEKslkgasIWDEVKDRL-------HDS--ALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 991 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1649-1864 |
2.70e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpldplL 1727
Cdd:PRK11160 338 SLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA-----L 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 TTTECI---R---FYGRLRGIRDL------DQFLDRVLDTYELRpyKDVQV------------RNLSGGNRRKLTVAVTC 1783
Cdd:PRK11160 413 RQAISVvsqRvhlFSATLRDNLLLaapnasDEALIEVLQQVGLE--KLLEDdkglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1784 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLcQRVAVLRAGQVIASDSPQRLKSEHGGYY 1863
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
.
gi 113193620 1864 A 1864
Cdd:PRK11160 569 Q 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
874-1062 |
2.96e-11 |
|
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: 65.33 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREHLQl 942
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrRAIGVVPQDTVLFND-TIGYNIR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 YAQIkippggSGGVEEIR--SEVAQ---TLQSLNFGkhesYPS------WQLSGGYRRRLCVAIAFIASPSVVILDEPCN 1011
Cdd:cd03253 97 YGRP------DATDEEVIeaAKAAQihdKIMRFPDG----YDTivgergLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1012 GVDAKARKDIWQLIERLRQGRAVIFATH----FMDeakylSDSLVIMRNGRIIAQ 1062
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHrlstIVN-----ADKIIVLKDGRIVER 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1657-1857 |
3.53e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1657 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI---------------SYCPQS 1720
Cdd:PRK11831 13 VSFTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlytvrkrmSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 NPLDPLLTTTECIRFygRLRGIRDLDQFLDRV-----LDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DE 1794
Cdd:PRK11831 93 GALFTDMNVFDNVAY--PLREHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALA-RAIALEPDLIMfDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1795 PTSDMDPVTRDMVYATIEQL--LLARRAVVLtSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELnsALGVTCVVV-SHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
872-1066 |
3.88e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.25 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTLTAREHL 940
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdwsaaelaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYAQikippgGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI-------ASPSVVILDEPCNGV 1013
Cdd:COG4138 91 ALHQP------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1014 DAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1066
Cdd:COG4138 165 DVAQQAALDRLLRELcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1665-1886 |
4.02e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLLTTTEcirfygrlrgiRD 1744
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVH-----------QE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1745 LDQFLDR-VLDTYEL-------------RPYKD---------------VQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1795
Cdd:PRK10982 82 LNLVLQRsVMDNMWLgryptkgmfvdqdKMYRDtkaifdeldididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1796 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHggyyAVTCFCGpaqqa 1875
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDK----IIAMMVG----- 232
|
250
....*....|.
gi 113193620 1876 ilsRSLNQRLP 1886
Cdd:PRK10982 233 ---RSLTQRFP 240
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
874-1059 |
4.29e-11 |
|
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: 64.80 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------EH-----QVGVCWQDniliPTLTAREhlql 942
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyEHkylhsKVSLVGQE----PVLFARS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 yAQIKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSW--------QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 1014
Cdd:cd03248 104 -LQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1015 AKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRI 1059
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
861-1068 |
4.31e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.06 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL-------TGQIR---QSSGKVLLAG-EHQVGVCWQDN 928
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILidgTDIRTVTRASlRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIpTLTAREHLQLYAqikipPGGSGgvEEIR--SEVAQTL-----QSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 1001
Cdd:PRK13657 419 GLF-NRSIEDNIRVGR-----PDATD--EEMRaaAERAQAHdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1002 SVVILDEPCNGVDAKARKDIWQLIERLRQGRavifaTHFMDeAKYLS-----DSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLStvrnaDRILVFDNGRVVESGSFDEL 556
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
871-1061 |
5.51e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLT 935
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvayvpQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 1015
Cdd:PRK15056 102 MMGRYGHMGWLRRAK------KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1016 KARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLViMRNGRIIA 1061
Cdd:PRK15056 176 KTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLA 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
862-1019 |
5.64e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 862 VSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI--LIPTLTAREH 939
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLefLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 940 LqlyaqIKIPPggsggvEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:PRK10636 398 L-----ARLAP------QELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
.
gi 113193620 1019 K 1019
Cdd:PRK10636 467 Q 467
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1668-1855 |
5.77e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYF--------EQPGIS-YCPQSNPLDPLLTTTECIRF 1735
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLngmpidakEMRAISaYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1736 YGRLRGIRDLD-----QFLDRVLDTYELRPYKDV------QVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:TIGR00955 123 QAHLRMPRRVTkkekrERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSHS-VSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1653-1863 |
6.60e-11 |
|
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: 64.43 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQ 1719
Cdd:cd03252 4 EHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladpawlRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPL------------DPLLTTTECI---RFYGRLRGIRDLDQFLDRVLDTyelrpykdvQVRNLSGGNRRKLTVAVTCC 1784
Cdd:cd03252 84 ENVLfnrsirdnialaDPGMSMERVIeaaKLAGAHDFISELPEGYDTIVGE---------QGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1785 GCTPTVLMDEPTSDMD-----PVTRDMvyatieQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:cd03252 155 HNPRILIFDEATSALDyesehAIMRNM------HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
....
gi 113193620 1860 GGYY 1863
Cdd:cd03252 228 GLYA 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
861-1014 |
6.61e-11 |
|
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: 67.27 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEhQVGVCWQDNiliptltAREHL 940
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE-TVKLAYVDQ-------SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 Q----LYAQIkippggSGGVEEIR---SEVA--QTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:TIGR03719 398 DpnktVWEEI------SGGLDIIKlgkREIPsrAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....
gi 113193620 1011 NGVD 1014
Cdd:TIGR03719 472 NDLD 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1649-1860 |
7.88e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQpdVGQIyfE---------------Q 1711
Cdd:NF033858 1 VARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQ--QGRV--EvlggdmadarhrravC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1712 PGISYCPQ---SNpLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVavtCCGC 1786
Cdd:NF033858 76 PRIAYMPQglgKN-LYPTLSVFENLDFFGRLFGQdaAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL---CCAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1787 --TPTVL-MDEPTSDMDPVTRDMVYATIEQLLlARRA----VVLTSHsVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEH 1859
Cdd:NF033858 152 ihDPDLLiLDEPTTGVDPLSRRQFWELIDRIR-AERPgmsvLVATAY-MEEAER-FDWLVAMDAGRVLATGTPAELLART 228
|
.
gi 113193620 1860 G 1860
Cdd:NF033858 229 G 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
857-1068 |
8.15e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 857 ASLVNVSKLYGskcAVSNL-SLDFA--RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGV 923
Cdd:PRK15439 12 LCARSISKQYS---GVEVLkGIDFTlhAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakaHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 924 CW--QDNILIPTLTAREHLQLyaqikippgGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 1001
Cdd:PRK15439 89 YLvpQEPLLFPNLSVKENILF---------GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1002 SVVILDEPCNGVD-AKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRI-----IAQHSRDSL 1068
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIalsgkTADLSTDDI 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1650-1851 |
8.41e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRghYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV----GQIYFEqpGISYCPQS----- 1720
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLD--GKPVAPCAlrgrk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 ------NP---LDPLLTTTECIRFYGRLRGIRDLDQFL------------DRVLDTYelrPYKdvqvrnLSGGNRRKLTV 1779
Cdd:PRK10418 81 iatimqNPrsaFNPLHTMHTHARETCLALGKPADDATLtaaleavglenaARVLKLY---PFE------MSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1780 AVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRA--VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1851
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLES-IVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
871-1058 |
9.31e-11 |
|
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: 63.99 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL-----------AGEHQV--------GVCWQDNILI 931
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdggwvdlaqASPREIlalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 932 PTLTAREhlqLYAQikipPGGSGGV--EEIRSEVAQTLQSLNFGKHesypSWQL-----SGGYRRRLCVAIAFIASPSVV 1004
Cdd:COG4778 106 PRVSALD---VVAE----PLLERGVdrEEARARARELLARLNLPER----LWDLppatfSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1665-1847 |
9.51e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLT--GQLQPDV---GQIYFEQPGIsYCP----------------QSNPL 1723
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYNGHNI-YSPrtdtvdlrkeigmvfqQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DplLTTTECIRFYGRLRGIRD---LDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDE 1794
Cdd:PRK14239 99 P--MSIYENVVYGLRLKGIKDkqvLDEAVEKSLKGASI--WDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1795 PTSDMDPVTRDMvyatIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK14239 175 PTSALDPISAGK----IEETLLGLKddyTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1666-1826 |
1.01e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI---------YFEQPGISYCPQSNPLDPLLTTTECIRFY 1736
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQHRAELDPEKTVMDNLAEGKQEVMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1737 GRLRGIRD-LDQFLdrvldtyeLRPYKDVQ-VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMvyatIEQL 1814
Cdd:PRK11147 415 GRPRHVLGyLQDFL--------FHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL----LEEL 482
|
170
....*....|...
gi 113193620 1815 LLARRA-VVLTSH 1826
Cdd:PRK11147 483 LDSYQGtVLLVSH 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
874-1054 |
1.05e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI--RQSSGKVllagEHQVGVCWQDNILIptltarEHlqlyaqikIPPG 951
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----DVPDNQFGREASLI------DA--------IGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 952 GSggveeirseVAQTLQSLNFGKHESYPSW-----QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD---AKARKDIWQ 1023
Cdd:COG2401 110 GD---------FKDAVELLNAVGLSDAVLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQ 180
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1024 LIERlRQGRAVIFATHFMDEAKYLSDSLVIM 1054
Cdd:COG2401 181 KLAR-RAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1666-1826 |
1.15e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYCPQSNPLDPLLTTTE-C- 1732
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsikkdlctyQKQLCFVGHRSGINPYLTLREnCl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 --IRFYGRLRGIrdldqflDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1810
Cdd:PRK13540 97 ydIHFSPGAVGI-------TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*.
gi 113193620 1811 IEQLLLARRAVVLTSH 1826
Cdd:PRK13540 170 IQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1650-1855 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGH--YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE--------------QPG 1713
Cdd:PRK13642 5 LEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgelltaenvwnlrrKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1714 ISYcpqSNPLDPLL--TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPT 1789
Cdd:PRK13642 85 MVF---QNPDNQFVgaTVEDDVAFGMENQGIprEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1790 VLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1666-1849 |
1.24e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQ-----LQPDV-------GQIYFEQpgIS-YCPQSNPLDPLLTTTEC 1732
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggyIEGDIrisgfpkKQETFAR--ISgYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 IRFYGRLRGIRDLDQ-----FLDRVLDTYELRPYKDVQV-----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPV 1802
Cdd:PLN03140 974 LIYSAFLRLPKEVSKeekmmFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1803 TRDMVYATIEQLLLARRAVVLTSH--SVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYS 1102
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
859-1061 |
1.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTARE 938
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-----------IDFKSSKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 939 HLQlyaqikippggsGGVEEIRSEVAQTLQ-----SLNFGKhesYPS-------------------------------WQ 982
Cdd:PRK10982 70 ALE------------NGISMVHQELNLVLQrsvmdNMWLGR---YPTkgmfvdqdkmyrdtkaifdeldididprakvAT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 983 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
858-1059 |
1.41e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQD 927
Cdd:PRK11650 5 KLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepaDRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAREHLQlYAqIKIppggsGGV--EEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:PRK11650 85 YALYPHMSVRENMA-YG-LKI-----RGMpkAEIEERVAEAARILELEPLlDRKPR-ELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1005 ILDEPCNGVDAKARK----DIWQLIERLRQgrAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK11650 157 LFDEPLSNLDAKLRVqmrlEIQRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1665-1849 |
1.54e-10 |
|
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: 66.00 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPD---VGQIYF-------------EQPGISYCPQSNPLDPLLT 1728
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWsgsplkasnirdtERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIrFYGR---LRGIR-DLDQFLDR---VLDTYELRPYKDVQ-VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1800
Cdd:TIGR02633 95 VAENI-FLGNeitLPGGRmAYNAMYLRaknLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 113193620 1801 PVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1662-1858 |
1.75e-10 |
|
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: 64.11 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDvGQIYFEqpGISYcpQSNPLDPL-----LTTTECIRFY 1736
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQID--GVSW--NSVPLQKWrkafgVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1737 GRLRGIRD-----LDQFLDRVLDTYELR------PYK-DVQVRN----LSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1800
Cdd:cd03289 91 GTFRKNLDpygkwSDEEIWKVAEEVGLKsvieqfPGQlDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1801 PVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:cd03289 171 PITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1668-1847 |
1.87e-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: 62.26 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLL---------TGQLQPDvGQ---IYFeQPGISYCPQSNPLDPLLTTTECIRF 1735
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLagrktagviTGEILIN-GRpldKNF-QRSTGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1736 YGRLRGirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL 1815
Cdd:cd03232 103 SALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170 180 190
....*....|....*....|....*....|....
gi 113193620 1816 LARRAVVLTSHSVSE-IEHLCQRVAVL-RAGQVI 1847
Cdd:cd03232 156 DSGQAILCTIHQPSAsIFEKFDRLLLLkRGGKTV 189
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1668-1833 |
1.89e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGEcFGLL-GKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI------------SYCPQSnpldPLL---TTTE 1731
Cdd:PRK10247 25 NISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeiyrqqvSYCAQT----PTLfgdTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFYGRLRGIR-DLDQFLDRvLDTYELrPYKDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVY 1808
Cdd:PRK10247 100 NLIFPWQIRNQQpDPAIFLDD-LERFAL-PDTILTknIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180
....*....|....*....|....*.
gi 113193620 1809 ATIEQLLLARR-AVVLTSHSVSEIEH 1833
Cdd:PRK10247 178 EIIHRYVREQNiAVLWVTHDKDEINH 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1663-1846 |
1.92e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1663 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGiSYCPQSNPLDPLLTTTECIRFYGRLRGI 1742
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-ALIAISSGLNGQLTGIENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1743 --RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTcCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARR 1819
Cdd:PRK13545 116 tkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAIS-VHINPDILvIDEALSVGDQTFTKKCLDKMNEFKEQGK 194
|
170 180
....*....|....*....|....*..
gi 113193620 1820 AVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK13545 195 TIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1664-1846 |
1.93e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1664 YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPLLTTTECIRFYGRLRGI 1742
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--DRNGeVSVIAISAGLSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1743 --RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRA 1820
Cdd:PRK13546 116 krKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKT 195
|
170 180
....*....|....*....|....*.
gi 113193620 1821 VVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK13546 196 IFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1673-1840 |
2.03e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1673 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqPGISYCPQSNPLDPLLTTTECirfygrLRGIRdlDQFLDRV 1752
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIKPDYDGTVEDL------LRSIT--DDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1753 LDTYELRPYK-----DVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SH 1826
Cdd:PRK13409 433 YKSEIIKPLQlerllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVvDH 512
|
170
....*....|....
gi 113193620 1827 SVSEIEHLCQRVAV 1840
Cdd:PRK13409 513 DIYMIDYISDRLMV 526
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1650-1846 |
2.10e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1720
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrrqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 -----------------NPLDPLL---TTTECIRfygrlrgiRDLDQFLDRV--LDTYELRPYKdvqvrnLSGGNRRKLT 1778
Cdd:PRK10908 82 gmifqdhhllmdrtvydNVAIPLIiagASGDDIR--------RRVSAALDKVglLDKAKNFPIQ------LSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1779 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
883-1057 |
2.40e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 883 QVSCLLGRNGAGKSTLIKLL---------TGQIRQSSGKVLLAG-EHQVGVCWQDNILIPTLTAREHLQLYAQIKIPpgG 952
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervttgviTGGDRLVNGRPLDSSfQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQP--K 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 953 SGGVEEIRSEVAQTLQSLNFgkhESY-------PSWQLSGGYRRRLCVAIAFIASP-SVVILDEPCNGVDAKARKDIWQL 1024
Cdd:TIGR00956 868 SVSKSEKMEYVEEVIKLLEM---ESYadavvgvPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKL 944
|
170 180 190
....*....|....*....|....*....|....*....
gi 113193620 1025 IERL-RQGRAVIFATH-----FMDEAkylsDSLVIMRNG 1057
Cdd:TIGR00956 945 MRKLaDHGQAILCTIHqpsaiLFEEF----DRLLLLQKG 979
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1666-1855 |
2.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLT-------GQLQPDVGQIYF-------------EQPGISYcPQSNPLdP 1725
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFgkdifqidaiklrKEVGMVF-QQPNPF-P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIRFYGRLRGI---RDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1796
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIkekREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1797 SDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK14246 182 SMIDIVNSQAIEKLITE-LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
887-1060 |
2.93e-10 |
|
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: 61.89 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAG----------EHQVGVCWQDNILIPTLTAREHLQLYAQIKippggs 953
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGipykefaekyPGEIIYVSEEDVHFPTLTVRETLDFALRCK------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 954 gGVEEIRSevaqtlqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGR 1032
Cdd:cd03233 112 -GNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDVLK 169
|
170 180 190
....*....|....*....|....*....|
gi 113193620 1033 AVIFATHFM--DEAKYLSDSLVIMRNGRII 1060
Cdd:cd03233 170 TTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
861-1062 |
3.01e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL-------TGQIR-------------QSSGKVLlAGEHQ 920
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRvgditidtarslsQQKGLIR-QLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 921 VGVCWQDNILIPTLTAREH-LQLYAQIKIPPGGSGgVEEIRSEVAQTLQSlnfGKHESYPSwQLSGGYRRRLCVAIAFIA 999
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEA-TARARELLAKVGLA---GKETSYPR-RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1000 SPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
858-1071 |
3.08e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYG-SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQD-NILIPTLT 935
Cdd:PRK10522 324 ELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 936 AREHL--QLYaqikippgGSGGVEEIRSEVAQTLQSLNFG-----KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:PRK10522 404 TDFHLfdQLL--------GPEGKPANPALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1009 PCNGVDAKARKDIWQ-LIERLRQGRAVIFAT----HFMDEAkylsDSLVIMRNGRI-------IAQHSRDSLQRL 1071
Cdd:PRK10522 476 WAADQDPHFRREFYQvLLPLLQEMGKTIFAIshddHYFIHA----DRLLEMRNGQLseltgeeRDAASRDAVART 546
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
875-1067 |
3.62e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 875 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGE------------HQVGVCWQDN--ILIPTLtarEHL 940
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQpleawsaaelarHRAYLSQQQTppFAMPVF---QYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 QLYaqikIPPGGSggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGG--YRRRL---CVAIAFIASPS--VVILDEPCNGV 1013
Cdd:PRK03695 91 TLH----QPDKTR--TEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLaavVLQVWPDINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1014 DAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDS 1067
Cdd:PRK03695 165 DVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1669-1853 |
3.79e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1669 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPDVGQIYFEQPGIS------------YCPQSNPLDPLLTTTECIRFY 1736
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSdwsaaelarhraYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1737 GRLRGIRD-LDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV-------LMDEPTSDMDPVTRDMVY 1808
Cdd:COG4138 94 QPAGASSEaVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegqllLLDEPMNSLDVAQQAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1809 ATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1853
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
872-1071 |
4.58e-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: 64.77 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL------------AGEHqVGVCWQD----------NI 929
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreeLGRH-IGYLPQDvelfdgtiaeNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 930 liptltAR------EHLQLYAQI--------KIPPG-----GSGGVeeirsevaqtlqslnfgkhesypswQLSGGYRRR 990
Cdd:COG4618 427 ------ARfgdadpEKVVAAAKLagvhemilRLPDGydtriGEGGA-------------------------RLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 991 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRD 1066
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHrpsLLAAV----DKLLVLRDGRVQAFGPRD 551
|
....*.
gi 113193620 1067 S-LQRL 1071
Cdd:COG4618 552 EvLARL 557
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1644-1827 |
5.65e-10 |
|
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: 64.30 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------Q 1711
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdevR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1712 PGISYCPQsnplDP-LLTTT--ECIRFyGR-----------LRGIRdLDQFLDRVLDTYELRPYKDvqVRNLSGGNRRKL 1777
Cdd:TIGR02868 409 RRVSVCAQ----DAhLFDTTvrENLRL-ARpdatdeelwaaLERVG-LADWLRALPDGLDTVLGEG--GARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1778 TVAVTCCGCTPTVLMDEPTSDMDPVTRDmvyATIEQLL--LARRAVVLTSHS 1827
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETAD---ELLEDLLaaLSGRTVVLITHH 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1668-1800 |
6.61e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPGISYCPQS-NPLDPLLTTTECIRfyGRLRGIRdl 1745
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQSrDALDPNKTVWEEIS--GGLDIIK-- 417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1746 dqfldrvLDTYEL--RPY--------KDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1800
Cdd:PRK11819 418 -------VGNREIpsRAYvgrfnfkgGDQQkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
871-1068 |
7.22e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwQDnilIPTLTAREHLQLYAQIKI-- 948
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG--------QD---ITGLSGRELRPLRRRMQMvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 949 --PPG-------------------GSGGVEEIRSEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:COG4608 102 qdPYAslnprmtvgdiiaeplrihGLASKAERRERVAELLELvgLRPEHADRYPH-EFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1644-1855 |
8.75e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAVRAENLWLAY--RRG--------HYAVRNVNFSVQRGECFGLLGKNGAGKST----IFKLLTGQ------LQPD 1703
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpiRKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1704 VG-------------QIYFEQPGISYCPQsnpLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYELRPykDVQVR--- 1767
Cdd:PRK15134 350 HNlnrrqllpvrhriQVVFQDPNSSLNPR---LNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP--ETRHRypa 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1768 NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
....*....
gi 113193620 1847 IASDSPQRL 1855
Cdd:PRK15134 505 VEQGDCERV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1660-1846 |
9.15e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1660 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSnPLDPLLT----TTECIR- 1734
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN--GKDISPRS-PLDAVKKgmayITESRRd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 --FY-----------------GRLRGIRDLdqFLDRVLDTYELRPYKDVQVR---------NLSGGNRRKLTVAVTCCgC 1786
Cdd:PRK09700 350 ngFFpnfsiaqnmaisrslkdGGYKGAMGL--FHEVDEQRTAENQRELLALKchsvnqnitELSGGNQQKVLISKWLC-C 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1787 TPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK09700 427 CPEVIIfDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1625-1708 |
9.89e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1625 LDKLGQLKLVNIQSIFK--SCVDTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP 1702
Cdd:PRK10522 296 FNKLNKLALAPYKAEFPrpQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
....*.
gi 113193620 1703 DVGQIY 1708
Cdd:PRK10522 376 QSGEIL 381
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
858-1068 |
9.98e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.52 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNIL------- 930
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAR-----EHLQLYAQIKIppggsggveeIRSEVAQTLQSLNFGKHES--------------------YPSwQLSG 985
Cdd:PRK10619 87 LRLLRTRltmvfQHFNLWSHMTV----------LENVMEAPIQVLGLSKQEAreravkylakvgideraqgkYPV-HLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 986 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1064
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....
gi 113193620 1065 RDSL 1068
Cdd:PRK10619 236 PEQL 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
859-1039 |
1.18e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------HQVGVCW--QDN 928
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctYQKQLCFvgHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 929 ILIPTLTAREHlqLYAQIKIPPGGSGGVEEIRsevaqtlqSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDE 1008
Cdd:PRK13540 84 GINPYLTLREN--CLYDIHFSPGAVGITELCR--------LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 113193620 1009 PCNGVDAKARKDIWQLIERLR-QGRAVIFATH 1039
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRaKGGAVLLTSH 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1664-1853 |
1.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1664 YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycPQS-------------NPLDPLLTTT 1730
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT--DDNfeklrkhigivfqNPDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 ecIRF---YG---RLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:PRK13648 101 --VKYdvaFGlenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1805 DMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQ 1853
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTPT 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1672-1833 |
1.48e-09 |
|
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: 62.88 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1672 SVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPgISYCPQSNPLDPLLTTTECIR-----------FYGRLr 1740
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISYKPQYISPDYDGTVEEFLRsantddfgssyYKTEI- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1741 gIRDLDqfLDRVLDTYelrpykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRA 1820
Cdd:COG1245 440 -IKPLG--LEKLLDKN---------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
170
....*....|...
gi 113193620 1821 VVLTshsvseIEH 1833
Cdd:COG1245 508 TAMV------VDH 514
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
861-1060 |
2.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ--------VGVCWQD 927
Cdd:PRK13651 7 NIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkeKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 928 NILIPTLTAR------------------EHlQLYAQ-----IKIPPGGSGGVEEIRSEVAQTLQSLnFGKHESY---PSW 981
Cdd:PRK13651 87 LVIQKTRFKKikkikeirrrvgvvfqfaEY-QLFEQtiekdIIFGPVSMGVSKEEAKKRAAKYIEL-VGLDESYlqrSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 982 QLSGGYRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:PRK13651 165 ELSGGQKRR--VALAGILAmePDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
..
gi 113193620 1059 II 1060
Cdd:PRK13651 243 II 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1668-1831 |
2.44e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLqpDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTECIR 1734
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGdrlvngrpldssfQRSIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1735 FYGRLR-----GIRDLDQFLDRVLDTYELRPYKDVQV----RNLSGGNRRKLTVAVTCCGcTPTVL--MDEPTSDMDPVT 1803
Cdd:TIGR00956 859 FSAYLRqpksvSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVA-KPKLLlfLDEPTSGLDSQT 937
|
170 180
....*....|....*....|....*...
gi 113193620 1804 RDMVYATIEQLLLARRAVVLTSHSVSEI 1831
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
828-1059 |
2.78e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 828 VIGLAYQRYKKNNYSFVKVSRSQLDGKLGASLVNVSKLYGSKcaVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR 907
Cdd:PRK09700 237 IVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 908 QSSGKVLLAGEH----------QVGVCW-----QDNILIPTLTAREHLQLYAQIKIppGGSGG-------VEEIR-SEVA 964
Cdd:PRK09700 315 RAGGEIRLNGKDisprspldavKKGMAYitesrRDNGFFPNFSIAQNMAISRSLKD--GGYKGamglfheVDEQRtAENQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 965 QTLQSLNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDE 1043
Cdd:PRK09700 393 RELLALKCHSVNQNIT-ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPE 471
|
250
....*....|....*.
gi 113193620 1044 AKYLSDSLVIMRNGRI 1059
Cdd:PRK09700 472 IITVCDRIAVFCEGRL 487
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1676-1826 |
3.15e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1676 GECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI---------YFEQPGISYC-PQSNPLDPLLTTTEcirfygrlrgiRDL 1745
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLrADESPLQHLARLAP-----------QEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1746 DQFLDRVLDTYELRPYKDVQV-RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtRDMVYATIEQLLLARRAVVLT 1824
Cdd:PRK10636 407 EQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD---LDMRQALTEALIDFEGALVVV 483
|
..
gi 113193620 1825 SH 1826
Cdd:PRK10636 484 SH 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1650-1847 |
3.33e-09 |
|
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: 61.62 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENL--WLAYRRG--------HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFK-LLtgQLQPDVGQIYFEQPGISYCP 1718
Cdd:COG4172 276 LEARDLkvWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLL--RLIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QS--------------NP---LDPLLTTTECI----RFYGRLRGIRDLDQFLDRVLDTYELRPykdvQVRN-----LSGG 1772
Cdd:COG4172 354 RRalrplrrrmqvvfqDPfgsLSPRMTVGQIIaeglRVHGPGLSAAERRARVAEALEEVGLDP----AARHrypheFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1773 NR------RKLTVAvtccgctPTVLM-DEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAV 1840
Cdd:COG4172 430 QRqriaiaRALILE-------PKLLVlDEPTSALD-VS---VQAQILDLLrdLQREhglAYLFISHDLAVVRALAHRVMV 498
|
....*..
gi 113193620 1841 LRAGQVI 1847
Cdd:COG4172 499 MKDGKVV 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1650-1847 |
3.50e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI-SYCPQSNP------ 1722
Cdd:PRK11147 4 ISIHGAWLSFSD-APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvARLQQDPPrnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1723 ---------------------LDPLLTTTECIRFYGRLRGIRD-LD-----QFLDR---VLDTYELRPykDVQVRNLSGG 1772
Cdd:PRK11147 83 vydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQEqLDhhnlwQLENRineVLAQLGLDP--DAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1773 NRRKLTVA---VtccgCTPTVLM-DEPTSDMDPVTRDMvyatIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK11147 161 WLRKAALGralV----SNPDVLLlDEPTNHLDIETIEW----LEGFLKTfQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
858-1015 |
3.80e-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: 61.49 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAV-SNLSLDF---ARNQVsclLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT 933
Cdd:TIGR03719 6 TMNRVSKVVPPKKEIlKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHL---------------QLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESY----------PSW-----QL 983
Cdd:TIGR03719 83 KTVRENVeegvaeikdaldrfnEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQleiamdalrcPPWdadvtKL 162
|
170 180 190
....*....|....*....|....*....|..
gi 113193620 984 SGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 1015
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1665-1858 |
3.81e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLL----------------- 1727
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgvvfqfpesqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 TTTECIRFYGRLRGI--RDLDQFLDRVLDTYEL-RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1804
Cdd:PRK13643 101 TVLKDVAFGPQNFGIpkEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1805 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1665-1807 |
3.99e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.71 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------QsnplDPLLTTTEC 1732
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeykrakyigrvfQ----DPMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 I-----------RfyGRLRGIR------DLDQFLDRvLDTYEL----RPykDVQVRNLSGGNRRKLTVaVTCCGCTPTVL 1791
Cdd:COG1101 97 MtieenlalayrR--GKRRGLRrgltkkRRELFREL-LATLGLglenRL--DTKVGLLSGGQRQALSL-LMATLTKPKLL 170
|
170
....*....|....*..
gi 113193620 1792 M-DEPTSDMDPVTRDMV 1807
Cdd:COG1101 171 LlDEHTAALDPKTAALV 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1645-1846 |
4.97e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAV-RAENL--WLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGK----STIFKLLTGQLQpdvGQIYFE-QP---- 1712
Cdd:PRK13549 254 TIGEVIlEVRNLtaWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRWE---GEIFIDgKPvkir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 --------GISYCPQSNPLD---PLLTTTECI------RFYGRLR-----GIRDLDQFLDRvldtyeLR---PYKDVQVR 1767
Cdd:PRK13549 331 npqqaiaqGIAMVPEDRKRDgivPVMGVGKNItlaaldRFTGGSRiddaaELKTILESIQR------LKvktASPELAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1768 NLSGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK13549 405 RLSGGNQQKAVLA-KCLLLNPKILiLDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1646-1884 |
5.97e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1646 TGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QP 1712
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDdcdvakfgltdlRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 GISYCPQSnpldPLLtttecirFYGRLRgiRDLDQF-----------LDR--VLDTYELRPYK-DVQV----RNLSGGNR 1774
Cdd:PLN03232 1311 VLSIIPQS----PVL-------FSGTVR--FNIDPFsehndadlweaLERahIKDVIDRNPFGlDAEVseggENFSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1775 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQR 1854
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI-AHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
250 260 270
....*....|....*....|....*....|.
gi 113193620 1855 LKSEHG-GYYAVTCFCGPAQQAILSRSLNQR 1884
Cdd:PLN03232 1456 LLSRDTsAFFRMVHSTGPANAQYLSNLVFER 1486
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
878-1053 |
7.54e-09 |
|
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: 58.57 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 878 DFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgVCWQDNILIPTLTAREHLQLYAQIKippgGSGGVE 957
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---VSYKPQYIKADYEGTVRDLLSSITK----DFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 958 EIRSEVAQTLQSLNFGKHESYpswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR----KDIWQLIERLRQGRA 1033
Cdd:cd03237 94 YFKTEIAKPLQIEQILDREVP---ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNEKTAF 170
|
170 180
....*....|....*....|
gi 113193620 1034 VIFATHFMdeAKYLSDSLVI 1053
Cdd:cd03237 171 VVEHDIIM--IDYLADRLIV 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1650-1846 |
7.68e-09 |
|
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: 58.25 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRR--GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------------- 1710
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpisqyehkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1711 -------------QPGISYCPQSNPLDpllTTTECIRFYGRLRGIRDLdqfldrvldtyELRPYKDVQVRN--LSGGNRR 1775
Cdd:cd03248 92 lvgqepvlfarslQDNIAYGLQSCSFE---CVKEAAQKAHAHSFISEL-----------ASGYDTEVGEKGsqLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1776 KLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVyatiEQLL---LARRAVVLTSHSVSEIEHlCQRVAVLRAGQV 1846
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQV----QQALydwPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
982-1068 |
8.32e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 982 QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
....*...
gi 113193620 1061 AQHSRDSL 1068
Cdd:PRK13549 485 GDLINHNL 492
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1666-1834 |
1.01e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. 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: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPlLTTTECIRFygrlrGIrD 1744
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGrISFSSQFSWIMP-GTIKENIIF-----GV-S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1745 LDQFLDR-VLDTYELR------PYKDVQVR-----NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIE 1812
Cdd:cd03291 124 YDEYRYKsVVKACQLEeditkfPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV 203
|
170 180
....*....|....*....|..
gi 113193620 1813 QLLLARRAVVLTShsvSEIEHL 1834
Cdd:cd03291 204 CKLMANKTRILVT---SKMEHL 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1641-1858 |
1.12e-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: 60.69 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1641 KSCVDTGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDvGQIYFEqpGISYcpQ 1719
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQID--GVSW--N 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 SNPLDPL-----LTTTECIRFYGRLRGIRD-----LDQFLDRVLDTYELR------PYK-DVQVRN----LSGGNRRKLT 1778
Cdd:TIGR01271 1284 SVTLQTWrkafgVIPQKVFIFSGTFRKNLDpyeqwSDEEIWKVAEEVGLKsvieqfPDKlDFVLVDggyvLSNGHKQLMC 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1779 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
621-760 |
1.25e-08 |
|
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: 58.94 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 621 DVFKRGLYLAQGVQVAYLLGLVVFVALS------VRERIWMRESRNSMLMRSMGLKAHSELVAWALMSFLeLCVIFALIS 694
Cdd:pfam12698 146 PVESTPLFNPQSGYAYYLVGLILMIIILigaaiiAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLII 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 695 GVLYSGGILGYTNWFFMMFYCLSFGLCLISFCYMCTNFFNSAnIGAVASALLFFISLCPFIIVLMF 760
Cdd:pfam12698 225 LLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNS-EDAQSIIGIVILLLSGFFGGLFP 289
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
871-1060 |
1.32e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTA------REHLQL-- 942
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR-----------IDTLSPgklqalRRDIQFif 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 ---YAQIK---------IPP---GGSGGVEEIRSEVAQTLQSLNFGKHES--YPSwQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:PRK10261 408 qdpYASLDprqtvgdsiMEPlrvHGLLPGKAAAARVAWLLERVGLLPEHAwrYPH-EFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
881-1039 |
1.60e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDniliPTLTAR---------------EHLQLYAQ 945
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQD----PPRNVEgtvydfvaegieeqaEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 946 IkippggSGGVEEIRSE------------------------VAQTLQSLNFGKHESYPSwqLSGGYRRRLCVAIAFIASP 1001
Cdd:PRK11147 104 I------SHLVETDPSEknlnelaklqeqldhhnlwqlenrINEVLAQLGLDPDAALSS--LSGGWLRKAALGRALVSNP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1002 SVVILDEPCNGVDAKArkdiwqlIERLR------QGrAVIFATH 1039
Cdd:PRK11147 176 DVLLLDEPTNHLDIET-------IEWLEgflktfQG-SIIFISH 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1666-1847 |
1.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGISYCPQS-------------NPLdPLL 1727
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIelrrrvqmvfqipNPI-PNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 TTTECIRFYGRLRGI----RDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:PRK14247 98 SIFENVALGLKLNRLvkskKELQERVRWALEKAQL--WDEVKDRldapagKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1798 DMDPVTRdmvyATIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK14247 176 NLDPENT----AKIESLFLELKkdmTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
887-1022 |
1.66e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDN--ILIPTLT-----AREHLQLYAQIKIPPGGSGG---- 955
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpaLPQPALEyvidgDREYRQLEAQLHDANERNDGhaia 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 956 ----------VEEIRSEVAQTLQSLNFGKHE-SYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARkdIW 1022
Cdd:PRK10636 112 tihgkldaidAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV--IW 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1632-1826 |
1.71e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1632 KLVNIQSIFKSCVDTGEAVR--AENLWLAYRRGH-YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY 1708
Cdd:COG2401 9 VLMRVTKVYSSVLDLSERVAivLEAFGVELRVVErYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1709 FEQPgisycpqSNPLDPLLTTTECIrfyGRLRGIRDLDQFLDRV--LDTYE-LRPYKdvqvrNLSGGNRRKLTVAVTCCG 1785
Cdd:COG2401 89 VDVP-------DNQFGREASLIDAI---GRKGDFKDAVELLNAVglSDAVLwLRRFK-----ELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1786 CTPTVLMDEPTSDMDPVTRDMVYATIeqLLLARRA----VVLTSH 1826
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNL--QKLARRAgitlVVATHH 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1658-1800 |
1.81e-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: 59.56 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1658 AYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGIS--YCPQSNPLDPLLTTTECI-- 1733
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIKvgYLPQEPQLDPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1734 ----------RF--------------------YGRLRGI------RDLDQFLDRVLDTyeLR-PYKDVQVRNLSGGNRRK 1776
Cdd:TIGR03719 92 gvaeikdaldRFneisakyaepdadfdklaaeQAELQEIidaadaWDLDSQLEIAMDA--LRcPPWDADVTKLSGGERRR 169
|
170 180 190
....*....|....*....|....*....|
gi 113193620 1777 ltVAVtccgC-----TPTV-LMDEPTSDMD 1800
Cdd:TIGR03719 170 --VAL----CrlllsKPDMlLLDEPTNHLD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1667-1831 |
1.83e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1667 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTECIRFY 1736
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppAERGVGMVFQSYALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1737 GRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTV-LMDEPTSDMDPVTR--------- 1804
Cdd:PRK11000 100 LKLAGAkkEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA-EPSVfLLDEPLSNLDAALRvqmrieisr 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 113193620 1805 -------DMVYAT---IEQLLLARRAVVLTSHSVSEI 1831
Cdd:PRK11000 179 lhkrlgrTMIYVThdqVEAMTLADKIVVLDAGRVAQV 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
874-1068 |
1.92e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.74 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------EH-----QVGVCWQ----------DNILIp 932
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyDHhylhrQVALVGQepvlfsgsvrENIAY- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 933 TLTAREHLQLYAQIKippggSGGVEEIRSEVAQTLQSlNFGKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:TIGR00958 578 GLTDTPDEEIMAAAK-----AANAHDFIMEFPNGYDT-EVGEKGS----QLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1013 VDAKARKDIWQLieRLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:TIGR00958 648 LDAECEQLLQES--RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
861-1014 |
2.24e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEhQVGVCWQDNiliptltAREHL 940
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-TVKLAYVDQ-------SRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 941 Q----LYAQIkippggSGGVEEI---------RSEVAqtlqSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 1006
Cdd:PRK11819 400 DpnktVWEEI------SGGLDIIkvgnreipsRAYVG----RFNFkGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
....*...
gi 113193620 1007 DEPCNGVD 1014
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1668-1855 |
2.47e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTECIRFYG 1737
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgedvthrsiQQRDICMVFQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1738 RLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDPVTRDMVYATIEQL 1814
Cdd:PRK11432 104 KMLGVpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI-LKPKVLLfDEPLSNLDANLRRSMREKIREL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 113193620 1815 llaRRAVVLTS----HSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK11432 183 ---QQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1666-1849 |
2.58e-08 |
|
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: 56.00 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV--GQIYFE-------------QPGISYCPQSNPldpllttt 1730
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKgeditdlppeeraRLGIFLAFQYPP-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 ecirfygRLRGIRDLDqFLdrvldtyelrpyKDVQVrNLSGGNRRK---LTVAVTccgcTPT-VLMDEPTSDMDPVTRDM 1806
Cdd:cd03217 88 -------EIPGVKNAD-FL------------RYVNE-GFSGGEKKRneiLQLLLL----EPDlAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1807 VYATIEQLLLARRAVVLTSHSVSEIEHL-CQRVAVLRAGQVIAS 1849
Cdd:cd03217 143 VAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1659-1834 |
2.62e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1659 YRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY---------FEQPGISYCPQSNplDPLLTT 1729
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavFSQHHVDGLDLSS--NPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1730 TECirFYG----RLRGirDLDQFldRVLDTYELRPykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtRD 1805
Cdd:PLN03073 596 MRC--FPGvpeqKLRA--HLGSF--GVTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LD 661
|
170 180
....*....|....*....|....*....
gi 113193620 1806 MVYATIEQLLLARRAVVLTSHSvseiEHL 1834
Cdd:PLN03073 662 AVEALIQGLVLFQGGVLMVSHD----EHL 686
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1665-1864 |
2.79e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.82 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpL---------DPLL---TTTEC 1732
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS-LrrniavvfqDAGLfnrSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 IRFyGR-------LRGIRDLDQ---FLDRVLDTYelrpykDVQV----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:PRK13657 429 IRV-GRpdatdeeMRAAAERAQahdFIERKPDGY------DTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLkSEHGGYYA 1864
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDEL-VARGGRFA 564
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
847-1014 |
2.98e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 847 SRSqldGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehQVG---- 922
Cdd:PRK11147 313 SRS---GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HCGtkle 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 923 VCWQDN---ILIPTLTAREHLqlyaqikippggSGGVEEI-----RSEVAQTLQSLNFG-KHESYPSWQLSGGYRRRLCV 993
Cdd:PRK11147 384 VAYFDQhraELDPEKTVMDNL------------AEGKQEVmvngrPRHVLGYLQDFLFHpKRAMTPVKALSGGERNRLLL 451
|
170 180
....*....|....*....|.
gi 113193620 994 AIAFIASPSVVILDEPCNGVD 1014
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1680-1800 |
3.02e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1680 GLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGIS--YCPQSNPLDPLLTTTECI------------RF---------- 1735
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIKvgYLPQEPQLDPEKTVRENVeegvaevkaaldRFneiyaayaep 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1736 ----------YGRLRGI------RDLDQFLDRVLDTyeLR-PYKDVQVRNLSGGNRRKltVAVtccgC-----TPTV-LM 1792
Cdd:PRK11819 116 dadfdalaaeQGELQEIidaadaWDLDSQLEIAMDA--LRcPPWDAKVTKLSGGERRR--VAL----CrllleKPDMlLL 187
|
....*...
gi 113193620 1793 DEPTSDMD 1800
Cdd:PRK11819 188 DEPTNHLD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1645-1849 |
3.11e-08 |
|
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: 58.68 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1645 DTGEAV-RAENL--WLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQLQpdvGQIYFEQ------ 1711
Cdd:TIGR02633 252 EIGDVIlEARNLtcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTelvqALFGAYPGKFE---GNVFINGkpvdir 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1712 -------PGISYCPQSNPLD---PLLTTTECI------RFYGRLRgirdLD-----QFLDRVLDTYELRPYK-DVQVRNL 1769
Cdd:TIGR02633 329 npaqairAGIAMVPEDRKRHgivPILGVGKNItlsvlkSFCFKMR----IDaaaelQIIGSAIQRLKVKTASpFLPIGRL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1770 SGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:TIGR02633 405 SGGNQQKAVLA-KMLLTNPRVLiLDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
.
gi 113193620 1849 S 1849
Cdd:TIGR02633 484 D 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1666-1834 |
4.44e-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: 58.77 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPlLTTTECIRFygrlrGIrD 1744
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGrISFSPQTSWIMP-GTIKDNIIF-----GL-S 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1745 LDQFLDR-VLDTYELR------PYKDVQVR-----NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT-RDMVYATI 1811
Cdd:TIGR01271 513 YDEYRYTsVIKACQLEedialfPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESCL 592
|
170 180
....*....|....*....|...
gi 113193620 1812 EQLLLARRAVVLTshsvSEIEHL 1834
Cdd:TIGR01271 593 CKLMSNKTRILVT----SKLEHL 611
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
872-1068 |
4.46e-08 |
|
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: 57.91 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-QSSGKVLLAGeHQV-----------GVCW------QDNIlIPT 933
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING-KPVdirnpaqairaGIAMvpedrkRHGI-VPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHLQLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 1012
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1013 VDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL 490
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
884-1060 |
5.30e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 884 VSCLLGRNGAGKSTLIKLLTGqiRQSSGKVllAGEHQV--------------GVCWQDNILIPTLTAREHLQLYAQIKIP 949
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDIRIsgfpkkqetfarisGYCEQNDIHSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 950 PGGSGgvEEIRSEVAQTLQSLNFGKHES----YPSWQ-LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1024
Cdd:PLN03140 984 KEVSK--EEKMMFVDEVMELVELDNLKDaivgLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190
....*....|....*....|....*....|....*....
gi 113193620 1025 IER-LRQGRAVIFATH--FMDEAKYLSDSLVIMRNGRII 1060
Cdd:PLN03140 1062 VRNtVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVI 1100
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
869-1055 |
6.05e-08 |
|
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: 54.29 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 869 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKlltgQIrqssgKVLLAGEHqvgvcwqdniliptltarehlqlyaqiki 948
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD----AI-----GLALGGAQ----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 949 PPGGSGGVEEIRSEVAQTLQSLNFGKHesypswQLSGGYRRRLCVAIAF----IASPSVVILDEPCNGVDAKARKDIWQL 1024
Cdd:cd03227 50 SATRRRSGVKAGCIVAAVSAELIFTRL------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|..
gi 113193620 1025 IERLRQGRA-VIFATHFMDEAKyLSDSLVIMR 1055
Cdd:cd03227 124 ILEHLVKGAqVIVITHLPELAE-LADKLIHIK 154
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1652-1830 |
7.32e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.86 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1652 AENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------QPGISYcpQSNP 1722
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegpgaERGVVF--QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1723 LDPLLTTTECIRFYGRLRGIRDLD------QFLDRV-LDTYELRPykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1795
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQrleiahQMLKKVgLEGAEKRY-----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 113193620 1796 TSDMDPVTRDMvyatIEQLLL-----ARRAVVLTSHSVSE 1830
Cdd:PRK11248 156 FGALDAFTREQ----MQTLLLklwqeTGKQVLLITHDIEE 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1662-1858 |
7.39e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1731
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPaenrhvntvfQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1732 CIRFYGRLRGIRDlDQFLDRVLDTY---ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTV-LMDEPTSDMDPVTR 1804
Cdd:PRK09452 106 NVAFGLRMQKTPA-AEITPRVMEALrmvQLEEFAQRKPHQLSGGQQQRVAIAravVN----KPKVlLLDESLSALDYKLR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1805 DMVYATIEQLllaRRAVVLT----SHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:PRK09452 181 KQMQNELKAL---QRKLGITfvfvTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
858-1015 |
8.67e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKLYGSKCAV-SNLSLDF---ARNQVsclLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT 933
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 934 LTAREHlqlyaqikippggsggVEEIRSEVAQTLQSLN-----FGKHESY------------------------------ 978
Cdd:PRK11819 85 KTVREN----------------VEEGVAEVKAALDRFNeiyaaYAEPDADfdalaaeqgelqeiidaadawdldsqleia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 979 ------PSW-----QLSGGYRRRlcVAIA--FIASPSVVILDEPCNGVDA 1015
Cdd:PRK11819 149 mdalrcPPWdakvtKLSGGERRR--VALCrlLLEKPDMLLLDEPTNHLDA 196
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
869-1070 |
9.65e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 869 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-QSSGKV------LLAGEHqvgvcWQDNI-------LIPTL 934
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyQGSLKIngielrELDPES-----WRKHLswvgqnpQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 TAREHLQLyAQIKIPPggsggvEEIRSEVAQT-----LQSLNFGKHesYP----SWQLSGGYRRRLCVAIAFIASPSVVI 1005
Cdd:PRK11174 438 TLRDNVLL-GNPDASD------EQLQQALENAwvsefLPLLPQGLD--TPigdqAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1006 LDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLsDSLVIMRNGRIIAQHSRDSLQR 1070
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1653-1863 |
1.06e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQs 1720
Cdd:PRK10790 344 DNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplsslshsvlRQGVAMVQQ- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1721 nplDP-LLTTTecirFYGRLRGIRDLD-QFLDRVLDTYEL----RPYKD-------VQVRNLSGGNRRKLTVAVTCCGcT 1787
Cdd:PRK10790 423 ---DPvVLADT----FLANVTLGRDISeEQVWQALETVQLaelaRSLPDglytplgEQGNNLSVGQKQLLALARVLVQ-T 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1788 PTVL-MDEPTSDMDPVTRDmvyaTIEQLLLARRA---VVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1863
Cdd:PRK10790 495 PQILiLDEATANIDSGTEQ----AIQQALAAVREhttLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGRYW 569
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1644-1855 |
1.11e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAVRAENLWLAY---RRGHYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLL-------------------- 1696
Cdd:PRK10261 7 LDARDVLAVENLNIAFmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcdkmllrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1697 --------TGQLQ----PDVGQIyFEQPGISycpqsnpLDPLLTT----TECIRFY---GRLRGIRDLDQFLDRV----- 1752
Cdd:PRK10261 87 vielseqsAAQMRhvrgADMAMI-FQEPMTS-------LNPVFTVgeqiAESIRLHqgaSREEAMVEAKRMLDQVripea 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1753 ---LDTYelrPYKdvqvrnLSGGNRRKLTVAVTcCGCTPTVLM-DEPTSDMDpVTrdmVYATIEQLLLARR-----AVVL 1823
Cdd:PRK10261 159 qtiLSRY---PHQ------LSGGMRQRVMIAMA-LSCRPAVLIaDEPTTALD-VT---IQAQILQLIKVLQkemsmGVIF 224
|
250 260 270
....*....|....*....|....*....|..
gi 113193620 1824 TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK10261 225 ITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
861-1060 |
1.24e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSK--CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwqDNILIPTLTA-R 937
Cdd:PRK11176 346 NVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---------HDLRDYTLASlR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 938 EHLQLYAQ------------IKIPPGGSGGVEEIrSEVAQTLQSLNFGKH----------ESYPSwqLSGGYRRRLCVAI 995
Cdd:PRK11176 417 NQVALVSQnvhlfndtiannIAYARTEQYSREQI-EEAARMAYAMDFINKmdngldtvigENGVL--LSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 996 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRII 1060
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1665-1849 |
1.37e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqlqpdV-------GQIYF-------------EQPGISYCPQSNPLD 1724
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-----VyphgsyeGEILFdgevcrfkdirdsEALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1725 PLLTTTECIrFYG---RLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT-- 1796
Cdd:NF040905 91 PYLSIAENI-FLGnerAKRGVIDWNETNRRareLLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTaa 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1797 -SDMDPvtrdmvyATIEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1849
Cdd:NF040905 170 lNEEDS-------AALLDLLLELKAqgitSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
859-1049 |
1.56e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 859 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 926
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrQQVSYCAQt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 ---------DNILIPTLTAREHLQLYAQIKippggsggvEEIRSEVAQTL--QSLNfgkhesypswQLSGGYRRRlcvaI 995
Cdd:PRK10247 90 ptlfgdtvyDNLIFPWQIRNQQPDPAIFLD---------DLERFALPDTIltKNIA----------ELSGGEKQR----I 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 996 AFIAS----PSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSD 1049
Cdd:PRK10247 147 SLIRNlqfmPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADK 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1665-1855 |
1.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLL----------------- 1727
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRkkvgivfqfpehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 TTTECIRFYGRLRGIRDLD--QFLDRVLDTYELRPykDVQVRN---LSGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDP 1801
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDakQKAREMIELVGLPE--ELLARSpfeLSGGQMRRVAIA-GVLAMEPEVLvLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1802 VTR----DMVYAtieqllLARRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13634 179 KGRkemmEMFYK------LHKEKgltTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1673-1826 |
1.87e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1673 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVG--------------------QIYFE-----QPGISYCPQSNPLDP-- 1725
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelQNYFKklyngEIKVVHKPQYVDLIPkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 -------LLTTTEcirfygrLRGIrdldqfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:PRK13409 176 fkgkvreLLKKVD-------ERGK------LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*...
gi 113193620 1799 MDPVTRdMVYATIEQLLLARRAVVLTSH 1826
Cdd:PRK13409 243 LDIRQR-LNVARLIRELAEGKYVLVVEH 269
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1661-1847 |
2.27e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1661 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfeQPGISYCPQSNPLDplltttecirfyGRLR 1740
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI---RVGDITIDTARSLS------------QQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1741 GIRDLDQFLDRVLDTYELRPYK--------------------------------------DVQVRNLSGGNRRKLTVAVT 1782
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRtvleniiegpvivkgepkeeatararellakvglagkeTSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1783 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1654-1814 |
2.28e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1654 NLWLAYRRGH---YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP----------------- 1712
Cdd:PRK11629 10 NLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgQPmsklssaakaelrnqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1713 GISYcpQSNPLDPLLTTTECIRFyGRLRGIRDLDQFLDRVLDT-----YELRPYKdvQVRNLSGGNRRKLTVAVTCCGCT 1787
Cdd:PRK11629 90 GFIY--QFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMlaavgLEHRANH--RPSELSGGERQRVAIARALVNNP 164
|
170 180
....*....|....*....|....*..
gi 113193620 1788 PTVLMDEPTSDMDPVTRDMVYATIEQL 1814
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGEL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1661-1847 |
2.33e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1661 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------------NP---L 1723
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdiqfifqDPyasL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DPLLTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRPYKDVQV-RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1799
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVawlLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 113193620 1800 DPVTRDMVyatIEQLLLARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1847
Cdd:PRK10261 495 DVSIRGQI---INLLLDLQRdfgiAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1649-1855 |
2.55e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 54.27 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGIsYCPQSNPL 1723
Cdd:COG1117 11 KIEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLDGEDI-YDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1724 DplltttecIR------F---------------YG-RLRGIRDLDQFLDRVLDTyeLRP---YKDVQVR------NLSGG 1772
Cdd:COG1117 89 E--------LRrrvgmvFqkpnpfpksiydnvaYGlRLHGIKSKSELDEIVEES--LRKaalWDEVKDRlkksalGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1773 NRRKL----TVAVTccgctPTV-LMDEPTSDMDPVtrdmvyAT--IEQLLLA---RRAVVLTSHSVSEIEHLCQRVAVLR 1842
Cdd:COG1117 159 QQQRLciarALAVE-----PEVlLMDEPTSALDPI------STakIEELILElkkDYTIVIVTHNMQQAARVSDYTAFFY 227
|
250
....*....|...
gi 113193620 1843 AGQVIASDSPQRL 1855
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1674-1826 |
2.56e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1674 QRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI--------------------YFE-----QPGISYCPQSNPLDPLlt 1728
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdYFKklangEIKVAHKPQYVDLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 tteciRFYGRLRGI-RDLDQF--LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1805
Cdd:COG1245 175 -----VFKGTVRELlEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180
....*....|....*....|.
gi 113193620 1806 MVYATIEQLLLARRAVVLTSH 1826
Cdd:COG1245 250 NVARLIRELAEEGKYVLVVEH 270
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1665-1886 |
2.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-------------------YCPQSNPLDP 1725
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikqirkkvglvfQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 llTTTECIRF----YG--------------RLRGIRDldqfldrvlDTYELRPYKdvqvrnLSGGNRRKLTVAvTCCGCT 1787
Cdd:PRK13649 102 --TVLKDVAFgpqnFGvsqeeaealareklALVGISE---------SLFEKNPFE------LSGGQMRRVAIA-GILAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1788 PTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQR-------LKSEH 1859
Cdd:PRK13649 164 PKILvLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDifqdvdfLEEKQ 243
|
250 260
....*....|....*....|....*...
gi 113193620 1860 GGYYAVTCFCgpaqQAILSRSLN-QRLP 1886
Cdd:PRK13649 244 LGVPKITKFA----QRLADRGISfSSLP 267
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
874-1060 |
2.71e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS--SGKVLLAGEhqvgvcwqdNILIPTLTAREHLQLYAQIKIP-- 949
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGE---------SILDLEPEERAHLGIFLAFQYPie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 950 -PGGSG---------------GVEEIrsEVAQTLQSLN-----FGKHESYPSWQL----SGGYRRRLCVAIAFIASPSVV 1004
Cdd:CHL00131 96 iPGVSNadflrlaynskrkfqGLPEL--DPLEFLEIINeklklVGMDPSFLSRNVnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLV-IMRNGRII 1060
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDYIKPDYVhVMQNGKII 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1644-1855 |
4.01e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAVRAENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-YCPQ-- 1719
Cdd:PRK10253 2 TESVARLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1720 --------SNPLDPLLTTTECIRFYGRL-------RGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCC 1784
Cdd:PRK10253 80 arrigllaQNATTPGDITVQELVARGRYphqplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113193620 1785 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR---RAVVLtsHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKgytLAAVL--HDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
872-1039 |
4.08e-07 |
|
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: 51.77 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehqvGVCWQDNIL-------IPTLTAREHLqlya 944
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLflpqrpyLPLGTLREQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 945 qikippggsggveeirsevaqtlqslnfgkheSYPsWQ--LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIW 1022
Cdd:cd03223 85 --------------------------------IYP-WDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*..
gi 113193620 1023 QLIERLrqGRAVIFATH 1039
Cdd:cd03223 132 QLLKEL--GITVISVGH 146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
883-1054 |
4.40e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 883 QVSCLLGRNGAGKSTLIKLLTGQIRQSSGKvllageHQVGVCWQDNI-------LIPTLTAREHLQLYAQIK------IP 949
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGK------FDDPPDWDEILdefrgseLQNYFTKLLEGDVKVIVKpqyvdlIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 950 PGGSGGVEEIRSEVAQT------LQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1023
Cdd:cd03236 101 KAVKGKVGELLKKKDERgkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|..
gi 113193620 1024 LIERL-RQGRAVIFATHFMDEAKYLSDSLVIM 1054
Cdd:cd03236 181 LIRELaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1653-1841 |
4.94e-07 |
|
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: 51.39 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPDV-GQIYF-EQPGISYCPQSnpldPLLTTt 1730
Cdd:cd03223 4 ENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMpEGEDLLFLPQR----PYLPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 ecirfyGRLRgirdlDQFldrvldtyeLRPYKDVqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1810
Cdd:cd03223 78 ------GTLR-----EQL---------IYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1811 IEQLLLarrAVVLTSHSvSEIEHLCQRVAVL 1841
Cdd:cd03223 134 LKELGI---TVISVGHR-PSLWKFHDRVLDL 160
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1683-1831 |
8.39e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1683 GKNGAGKSTIFKLLTGQLQPDVGQIYF--------EQPGISYCPQSNPLDPLLTTTECIRFYGRlrgIRDLDQFLDRVLD 1754
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYkncninniAKPYCTYIGHNLGLKLEMTVFENLKFWSE---IYNSAETLYAAIH 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1755 TYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEI 1831
Cdd:PRK13541 110 YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSI 186
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
872-1057 |
9.07e-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: 51.95 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL----LAGEHQVGVCWQDNILIPTLTAREHLQLYAQIK 947
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 --IPPGGSGGVEEIRSEV-AQTLQS----LNFGKHESYPS--WQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1018
Cdd:cd03290 97 enITFGSPFNKQRYKAVTdACSLQPdidlLPFGDQTEIGErgINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 113193620 1019 KDIWQ--LIERLRQG-RAVIFATHfmdEAKYL--SDSLVIMRNG 1057
Cdd:cd03290 177 DHLMQegILKFLQDDkRTLVLVTH---KLQYLphADWIIAMKDG 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1662-1846 |
9.46e-07 |
|
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: 51.76 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1662 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLD----------------P 1725
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID--GLKLTDDKKNINelrqkvgmvfqqfnlfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1726 LLTTTECIRFYGR-LRGIRDLD------QFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1798
Cdd:cd03262 90 HLTVLENITLAPIkVKGMSKAEaeeralELLEKV----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1846
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
881-1054 |
1.09e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSsgkvllAGEHQVGVCWqDNILiptltarEH-----LQLY------AQIK-- 947
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSW-DEVL-------KRfrgteLQNYfkklynGEIKvv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 --------IPPGGSGGVEEI---------RSEVAQTLQSLNFGKHESYpswQLSGGYRRRLCVAIAFIASPSVVILDEPC 1010
Cdd:PRK13409 164 hkpqyvdlIPKVFKGKVRELlkkvdergkLDEVVERLGLENILDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 113193620 1011 NGVDAKARKDIWQLIERLRQGRAVIFATHfmDEA--KYLSDSLVIM 1054
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKYVLVVEH--DLAvlDYLADNVHIA 284
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1650-1830 |
1.28e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1650 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLL--TGQLQPDV---GQIYFEQPGIsYCPQSNPLD 1724
Cdd:PRK14243 11 LRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNL-YAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1725 -------------PLLTTT-ECIRFYGRLRGIR-DLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTC 1783
Cdd:PRK14243 89 vrrrigmvfqkpnPFPKSIyDNIAYGARINGYKgDMDELVERSLRQAAL--WDEVKDKlkqsglSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 113193620 1784 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSE 1830
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHNMQQ 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
871-1058 |
1.36e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVC---W-----------QDNI--LIPTL 934
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWravrsdiqmifQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 TA----REHLQLYaQIKIPPggsggvEEIRSEVAQTL-------QSLNFGKHEsypswqLSGGYRRRLCVAIAFIASPSV 1003
Cdd:PRK15079 116 TIgeiiAEPLRTY-HPKLSR------QEVKDRVKAMMlkvgllpNLINRYPHE------FSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGR 1058
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1673-1841 |
1.49e-06 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.65 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1673 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQsnpldplltttecirfygrlrgirdldqfldrv 1752
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ--------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1753 ldtyelrpYKDvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLL-ARRAVVLTSHSVSEI 1831
Cdd:cd03222 69 --------YID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEeGKKTALVVEHDLAVL 135
|
170
....*....|
gi 113193620 1832 EHLCQRVAVL 1841
Cdd:cd03222 136 DYLSDRIHVF 145
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1668-1855 |
1.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1668 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPGISYCPQSN-----------------PLDPLLTTT 1730
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI--TIAGYHITPETGnknlkklrkkvslvfqfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 --ECIRFYGRLRGIRDLD------QFLDRV---LDTYELRPYKdvqvrnLSGGNRRKLTVAvTCCGCTPTVL-MDEPTSD 1798
Cdd:PRK13641 103 vlKDVEFGPKNFGFSEDEakekalKWLKKVglsEDLISKSPFE------LSGGQMRRVAIA-GVMAYEPEILcLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 1799 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
983-1059 |
2.22e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 2.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 983 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1646-1864 |
2.83e-06 |
|
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: 52.51 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1646 TGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN---- 1721
Cdd:COG5265 354 GGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlraa 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1722 ----PLDPLL---TTTECIRfYGRL--------RGIR--DLDQFLDRVLDTYELRpykdVQVR--NLSGGNRRKLTVAVT 1782
Cdd:COG5265 434 igivPQDTVLfndTIAYNIA-YGRPdaseeeveAAARaaQIHDFIESLPDGYDTR----VGERglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1783 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQllLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQRLkSEHGG 1861
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLViAHRLSTIVD-ADEILVLEAGRIVERGTHAEL-LAQGG 584
|
...
gi 113193620 1862 YYA 1864
Cdd:COG5265 585 LYA 587
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1667-1864 |
3.21e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.42 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1667 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QPGISYCPQSNPLDPLLTTTECIRFYGRLRgirdl 1745
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgVPLVQYDHHYLHRQVALVGQEPVLFSGSVR----- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1746 dqflDRVldTYELRPYKDVQVRN----------------------------LSGGNRRKLTVAVTCCGcTPTVL-MDEPT 1796
Cdd:TIGR00958 573 ----ENI--AYGLTDTPDEEIMAaakaanahdfimefpngydtevgekgsqLSGGQKQRIAIARALVR-KPRVLiLDEAT 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113193620 1797 SDMDpvtrdmvyATIEQLL-----LARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYYA 1864
Cdd:TIGR00958 646 SALD--------AECEQLLqesrsRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1653-1857 |
3.41e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1653 ENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQ----LQPDV---GQ------------ 1706
Cdd:PRK15134 9 ENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpvvyPSGDIrfhGEsllhaseqtlrg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1707 -------IYFEQPGISycpqsnpLDPLLTTTEciRFYGRL---RGIR------DLDQFLDRVLDTYELRPYKDVQvRNLS 1770
Cdd:PRK15134 89 vrgnkiaMIFQEPMVS-------LNPLHTLEK--QLYEVLslhRGMRreaargEILNCLDRVGIRQAAKRLTDYP-HQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1771 GGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQ 1845
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VS---VQAQILQLLreLQQElnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250
....*....|..
gi 113193620 1846 VIASDSPQRLKS 1857
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
887-1034 |
3.62e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTLTAREhlQLYAQIKIPpggsgGVEE--IRSEVA 964
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNP--LLYMMRCFP-----GVPEqkLRAHLG 612
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 965 QTLQSLNFGKHesyPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKArkdiwqlIERLRQGRAV 1034
Cdd:PLN03073 613 SFGVTGNLALQ---PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA-------VEALIQGLVL 672
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
887-1059 |
4.15e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 887 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----HQVGV---CWQDNILIPTLTAREHLQ-------LYAQIKIPPG 951
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIqndSLRENILFGKALNEKYYQqvleacaLLPDLEILPS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 952 GSggveeiRSEVAQtlQSLNfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI---ERL 1028
Cdd:TIGR00957 749 GD------RTEIGE--KGVN-----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGV 809
|
170 180 190
....*....|....*....|....*....|...
gi 113193620 1029 RQGRAVIFATHFMdeaKYL--SDSLVIMRNGRI 1059
Cdd:TIGR00957 810 LKNKTRILVTHGI---SYLpqVDVIIVMSGGKI 839
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1647-1852 |
5.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1647 GEAVRAENLWLAYRRGH----YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ----PGISYCP 1718
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1719 QSNPLDPlltttECIRFYGRLRG-IRDLDQFLDRVL--DT----------------YELR--------------PYKDVQ 1765
Cdd:PRK13631 99 LITNPYS-----KKIKNFKELRRrVSMVFQFPEYQLfkDTiekdimfgpvalgvkkSEAKklakfylnkmglddSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1766 VRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAG 1844
Cdd:PRK13631 174 PFGLSGGQKRRVAIA-GILAIQPEILIfDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
....*...
gi 113193620 1845 QVIASDSP 1852
Cdd:PRK13631 253 KILKTGTP 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
983-1066 |
5.51e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 983 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1061
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPELLGMCDRIYVMNEGRITG 484
|
....*
gi 113193620 1062 QHSRD 1066
Cdd:NF040905 485 ELPRE 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1666-1890 |
5.89e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQ----PDVGQIYFEqpGIS-------------YCPQSNPLDPLLT 1728
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYD--GITpeeikkhyrgdvvYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1729 TTECIRFYGRLRGIRDLDQFLDR----------VLDTYELRPYKDVQV-----RNLSGGNRRKLTVA-VTCCGcTPTVLM 1792
Cdd:TIGR00956 155 VGETLDFAARCKTPQNRPDGVSReeyakhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAeASLGG-AKIQCW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1793 DEPTSDMDPVTR-DMVYATIEQLLLARRAVVLTSHSVSE-IEHLCQRVAVLRAGQVIASDSPQRLKS--EHGGYyavtcF 1868
Cdd:TIGR00956 234 DNATRGLDSATAlEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPADKAKQyfEKMGF-----K 308
|
250 260
....*....|....*....|....*...
gi 113193620 1869 CGPAQ------QAILSRSLNQRLPGARD 1890
Cdd:TIGR00956 309 CPDRQttadflTSLTSPAERQIKPGYEK 336
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
872-1039 |
5.92e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 872 VSNLSLDFARNQvSCLL-GRNGAGKSTLIKLLTGQIRQSSGKVLL-AGEHqvgvcwqdnIL-------IPTLTAREHLqL 942
Cdd:COG4178 379 LEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR---------VLflpqrpyLPLGTLREAL-L 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 943 YaqikipPGGSGGVEEirSEVAQTLQSLNFGK-----HESYPsWQ--LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 1015
Cdd:COG4178 448 Y------PATAEAFSD--AELREALEAVGLGHlaerlDEEAD-WDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....
gi 113193620 1016 KARKDIWQLIERLRQGRAVIFATH 1039
Cdd:COG4178 519 ENEAALYQLLREELPGTTVISVGH 542
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
871-1068 |
7.21e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdNILIPTLTAREHLQLYAQIKIP- 949
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ---------DLLKADPEAQKLLRQKIQIVFQn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 950 PGGSggvEEIRSEVAQTLQ-----SLNFGKHES--------------------YPSwQLSGGYRRRLCVAIAFIASPSVV 1004
Cdd:PRK11308 101 PYGS---LNPRKKVGQILEeplliNTSLSAAERrekalammakvglrpehydrYPH-MFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1005 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1068
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1665-1855 |
7.67e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG---------------------QLQP---------DVGQIYFEqpgi 1714
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidllRLSPrerrklvghNVSMIFQE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1715 sycPQSNpLDP-------LLTTTECIRFYGRL---------RGIrdldQFLDRVldtyELRPYKDVqVRN----LSGGNR 1774
Cdd:PRK15093 98 ---PQSC-LDPservgrqLMQNIPGWTYKGRWwqrfgwrkrRAI----ELLHRV----GIKDHKDA-MRSfpyeLTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1775 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAtieqlLLAR------RAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1848
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFR-----LLTRlnqnnnTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
....*..
gi 113193620 1849 SDSPQRL 1855
Cdd:PRK15093 240 TAPSKEL 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1659-1716 |
8.25e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.79 E-value: 8.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1659 YRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISY 1716
Cdd:PRK15112 21 FRRQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 79
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
874-1060 |
1.08e-05 |
|
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: 48.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwQDNILIPTLTAREHLQLYAQIKIPPGGS 953
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--------IDISTIPLEDLRSSLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 954 ggveeIRSEV--------AQTLQSLNFGKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI 1025
Cdd:cd03369 98 -----IRSNLdpfdeysdEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 113193620 1026 ERLRQGRAVIFATHFMDE-AKYlsDSLVIMRNGRII 1060
Cdd:cd03369 169 REEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVK 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
883-1054 |
1.78e-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: 49.78 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 883 QVSCLLGRNGAGKSTLIKLLTGQIRQSsgkvllAGEHQVGVCWqDNILiptltarEH-----LQLYAQ------IK---- 947
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPN------LGDYDEEPSW-DEVL-------KRfrgteLQDYFKklangeIKvahk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 ------IPPGGSGGVEEIRS---------EVAQTLqSLNfgkhesyPSW-----QLSGGYRRRLCVAIAFIASPSVVILD 1007
Cdd:COG1245 166 pqyvdlIPKVFKGTVRELLEkvdergkldELAEKL-GLE-------NILdrdisELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1008 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHfmDEA--KYLSDSLVIM 1054
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELaEEGKYVLVVEH--DLAilDYLADYVHIL 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
871-1045 |
1.86e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVgvcwqdnILIPT-----LTAREHLQLyaq 945
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-------IAISSglngqLTGIENIEL--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 946 ikipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN-GVDAKARKDIW 1022
Cdd:PRK13545 109 ----KGLMMGLtkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSvGDQTFTKKCLD 184
|
170 180
....*....|....*....|...
gi 113193620 1023 QLIERLRQGRAVIFATHFMDEAK 1045
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVK 207
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
889-1031 |
1.88e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 889 GRNGAGKSTLIKLLTGQIRQSSGK--------VLLAGEHQ---VGVCWQDN---ILIPT-----LTAREHLQlyaqikip 949
Cdd:PRK10938 36 GANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLqklVSDEWQRNntdMLSPGeddtgRTTAEIIQ-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 950 pggsggvEEIRSEV--AQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIER 1027
Cdd:PRK10938 108 -------DEVKDPArcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
....
gi 113193620 1028 LRQG 1031
Cdd:PRK10938 181 LHQS 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
875-1061 |
1.99e-05 |
|
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: 49.41 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 875 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTAREHLQLYAQI-------K 947
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL-----------DGQPVTADNREAYRQLFSAVfsdfhlfD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 948 IPPGGSGGVEEirSEVAQTLQSLNFGKHESY-----PSWQLSGGYRRRLCVAIAFIASPSVVILDEpcngvdakarkdiW 1022
Cdd:COG4615 420 RLLGLDGEADP--ARARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDE-------------W 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1023 --------------QLIERLR-QGRAVIFATHfmDEaKY--LSDSLVIMRNGRIIA 1061
Cdd:COG4615 485 aadqdpefrrvfytELLPELKaRGKTVIAISH--DD-RYfdLADRVLKMDYGKLVE 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
861-1014 |
2.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI--LIPTLTARE 938
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAydFENDLTLFD 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 939 HLQLYAQIKippggsGGVEEIRSevaqTLQSLNFGKHESYPSWQ-LSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 1014
Cdd:PRK15064 404 WMSQWRQEG------DDEQAVRG----TLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1650-1700 |
2.69e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 2.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1650 VRAENLWLAyRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQL 1700
Cdd:PRK13547 2 LTADHLHVA-RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL 51
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1669-1709 |
3.00e-05 |
|
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: 49.03 E-value: 3.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 113193620 1669 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF 1709
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1665-1852 |
3.48e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI----YFEQPGISYCPQSNPLDPLL------------- 1727
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKEIglvfqfpeyqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1728 TTTECIRFYGRLRGIRDLDQFLDRVLDTYEL----RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1803
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 113193620 1804 RDMVYATIEQL-LLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1852
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1681-1851 |
4.52e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.95 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1681 LLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------------EQPGISYCPQSNPLDPLLTTTecirfyGRLR-GIR 1743
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaekgiclppEKRRIGYVFQDARLFPHYKVR------GNLRyGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1744 --DLDQFlDRVLDTYELRPYKDVQVRNLSGGNR------RKLTVAvtccgctPTVL-MDEPTSDMD-PVTRD-MVYatIE 1812
Cdd:PRK11144 103 ksMVAQF-DKIVALLGIEPLLDRYPGSLSGGEKqrvaigRALLTA-------PELLlMDEPLASLDlPRKRElLPY--LE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1813 QLllARRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1851
Cdd:PRK11144 173 RL--AREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1737-1857 |
5.70e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1737 GRLRGIRDLDQFLDRVLDTyelrPYKdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLL 1816
Cdd:PRK14271 142 ARLTEVGLWDAVKDRLSDS----PFR------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LA 210
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 113193620 1817 ARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:PRK14271 211 DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
871-1060 |
6.34e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEH----------QVGVC--WQDNILIPTLTA 936
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdirdseALGIViiHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 937 REHLQLYAQIkippgGSGGV---EEIRSEVAQTLQSLnfGKHESyPSWQLS--GGYRRRLcVAIAFIASPSV--VILDEP 1009
Cdd:NF040905 96 AENIFLGNER-----AKRGVidwNETNRRARELLAKV--GLDES-PDTLVTdiGVGKQQL-VEIAKALSKDVklLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1010 C---NGVDAKARKDiwqLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:NF040905 167 TaalNEEDSAALLD---LLLELKaQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1665-1862 |
6.73e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1665 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDP---------LLTTT----- 1730
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQvalvsqnvhLFNDTianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1731 --ECIRFYGRLRGIR--------DLDQFLDRVLDTyelrpykdVQVRN---LSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1797
Cdd:PRK11176 438 ayARTEQYSREQIEEaarmayamDFINKMDNGLDT--------VIGENgvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113193620 1798 DMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGY 1862
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
978-1058 |
1.13e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.64 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 978 YPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMR 1055
Cdd:PRK09473 158 YPH-EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMY 236
|
...
gi 113193620 1056 NGR 1058
Cdd:PRK09473 237 AGR 239
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
889-1068 |
1.30e-04 |
|
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: 47.12 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 889 GRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREHLQlYAQikipPGGSGgvE 957
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqaslrAAIGIVPQDTVLFND-TIAYNIA-YGR----PDASE--E 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 958 EIRsEVAQTLQSLNFgkHESYPS-WQ---------LSGGYRRRlcVAIA--FIASPSVVILDEPCNGVDAKARKDIWQLI 1025
Cdd:COG5265 463 EVE-AAARAAQIHDF--IESLPDgYDtrvgerglkLSGGEKQR--VAIArtLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 113193620 1026 ERLRQGRAVIFATHfmdeakYLS-----DSLVIMRNGRIIAQHSRDSL 1068
Cdd:COG5265 538 REVARGRTTLVIAH------RLStivdaDEILVLEAGRIVERGTHAEL 579
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
871-1059 |
1.56e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 871 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqVGVCWQDNILIPTLTAREHLQL------YA 944
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--VSVIAISAGLSGQLTGIENIEFkmlcmgFK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 945 QikippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN-GVDAKARKDIWQ 1023
Cdd:PRK13546 117 R-----------KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSvGDQTFAQKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 113193620 1024 LIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1059
Cdd:PRK13546 186 IYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1669-1846 |
1.83e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1669 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPG------ISYCPQSNPLDPLLTTTEC 1732
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeEARAklrakhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1733 IRFYGRLRGIRDLD--QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDmvyaT 1810
Cdd:PRK10584 109 VELPALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD----K 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 113193620 1811 IEQLL--LARR---AVVLTSHSvSEIEHLCQRVAVLRAGQV 1846
Cdd:PRK10584 185 IADLLfsLNREhgtTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
867-1073 |
2.18e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTlikLLTGQIRQSSGKvllaGEHQV-GVCWQD---------------NIL 930
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLLSTE----GEIQIdGVSWNSvtlqtwrkafgvipqKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 931 IPTLTAREHLQLYAQIKIppggsggvEEI---------RSEVAQTLQSLNFGKHESypSWQLSGGYRRRLCVAIAFIASP 1001
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSD--------EEIwkvaeevglKSVIEQFPDKLDFVLVDG--GYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113193620 1002 SVVILDEPCNGVDAKArkdiWQLIER-LRQGRA---VIFATHFMDEAKYLSDSLVImrNGRIIAQHsrDSLQRLCT 1073
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVT----LQIIRKtLKQSFSnctVILSEHRVEALLECQQFLVI--EGSSVKQY--DSIQKLLN 1440
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
861-1060 |
2.26e-04 |
|
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: 45.95 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTG--QIRQSSGKVLlageHQVGVCWQ-DNILIP----- 932
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRII----YHVALCEKcGYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 933 -------TLTARE--------------------HLQ----LYAQIKI--------PPGGSGGVEEIRSEVaQTLQSLNFG 973
Cdd:TIGR03269 81 pcpvcggTLEPEEvdfwnlsdklrrrirkriaiMLQrtfaLYGDDTVldnvlealEEIGYEGKEAVGRAV-DLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 974 KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSL 1051
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 113193620 1052 VIMRNGRII 1060
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
881-1060 |
3.20e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAgehqvgvcwqdniliptltarehlqlyaqikippggsgGVEEIR 960
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------DGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 961 SEVAQTLQSLNFGKHEsypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIE-------RLRQGRA 1033
Cdd:smart00382 43 EEVLDQLLLIIVGGKK----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLT 118
|
170 180
....*....|....*....|....*..
gi 113193620 1034 VIFATHfmDEAKYLSDSLVIMRNGRII 1060
Cdd:smart00382 119 VILTTN--DEKDLGPALLRRRFDRRIV 143
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
874-1087 |
3.35e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 874 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS--------SGKVLLAGE--HQV---------GVCWQDNILIPTL 934
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplAAIdaprlarlrAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 935 TAREHLQLYaqiKIPPGGSGGVEEIRS-EVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF---------IASPSV 1003
Cdd:PRK13547 99 SAREIVLLG---RYPHARRAGALTHRDgEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1004 VILDEPCNGVDAKARKDIWQLIERL-RQGR-AVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS-RDSLQ-RLCTSNYSIR 1079
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLaRDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGApADVLTpAHIARCYGFA 255
|
....*...
gi 113193620 1080 LRCADATG 1087
Cdd:PRK13547 256 VRLVDAGD 263
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
983-1068 |
3.47e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 983 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMdEAKYLSDSLVIMRNGRIIAQ 1062
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQR 530
|
....*.
gi 113193620 1063 HSRDSL 1068
Cdd:PRK10789 531 GNHDQL 536
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
861-927 |
3.55e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 3.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 861 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQD 927
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQD 72
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1649-1864 |
4.63e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1649 AVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS------------ 1715
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglmdlrkvlg 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1716 YCPQSnpldPLLtttecirFYGRLRgiRDLDQFLDR----VLDTYELRPYKDVQVR--------------NLSGGNRRKL 1777
Cdd:PLN03130 1317 IIPQA----PVL-------FSGTVR--FNLDPFNEHndadLWESLERAHLKDVIRRnslgldaevseageNFSVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1778 TVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKS 1857
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII-AHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
....*..
gi 113193620 1858 EHGGYYA 1864
Cdd:PLN03130 1462 NEGSAFS 1468
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1666-1714 |
4.71e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 4.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV--GQIYFEQPGI 1714
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDILFKGESI 73
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1657-1711 |
7.44e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 7.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 113193620 1657 LAYRRGhyaVR----NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ 1711
Cdd:PRK10636 7 LQIRRG---VRvlldNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1670-1707 |
7.73e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 7.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 113193620 1670 NFSVQRGEC--FGLLGKNGAGKSTIFKLLTGQLQPDVGQI 1707
Cdd:PRK15064 19 NISVKFGGGnrYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1663-1855 |
8.94e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.42 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1663 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS---------NPLDPL------- 1726
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkNQLRLLrtrltmv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1727 ---------LTTTECI-----------RFYGRLRGIRDLDQ--FLDRVLDTYELrpykdvqvrNLSGGNRRKLTVAVTCC 1784
Cdd:PRK10619 98 fqhfnlwshMTVLENVmeapiqvlglsKQEARERAVKYLAKvgIDERAQGKYPV---------HLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113193620 1785 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1855
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1676-1845 |
9.49e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1676 GECFGLLGKNGAGKSTIFKLLTGQLQPD--VGQIYFEQPGIS--------YCPQSNPLDPLLTTTECIRFYGRLRGIRDL 1745
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTkqilkrtgFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1746 DQ-----FLDRVLDTYELRPYKDVQV-----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL 1815
Cdd:PLN03211 174 TKqekilVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190
....*....|....*....|....*....|.
gi 113193620 1816 LARRAVVLTSHS-VSEIEHLCQRVAVLRAGQ 1845
Cdd:PLN03211 254 QKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
858-1060 |
1.41e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 858 SLVNVSKL---YGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI----RQSSGKVLLAGEH------- 919
Cdd:PRK11022 2 ALLNVDKLsvhFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDlqrisek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 920 --------QVGVCWQDNI--LIPTLTAreHLQLYAQIKIPPGGSggvEEIRSEVAQTLQSL-----NFGKHESYPSwQLS 984
Cdd:PRK11022 82 errnlvgaEVAMIFQDPMtsLNPCYTV--GFQIMEAIKVHQGGN---KKTRRQRAIDLLNQvgipdPASRLDVYPH-QLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113193620 985 GGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRII 1060
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1644-1864 |
1.50e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.59 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1644 VDTGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTI----FKLLtgqlqpDV--GQIYFEQPGISY 1716
Cdd:cd03288 14 VGLGGEIKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV------DIfdGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1717 CPQSNPLDPL-LTTTECIRFYGRLRGIRDLDQFL--DRVLDTYELRPYKDVqVRNLSG---------------GNRRKLT 1778
Cdd:cd03288 88 LPLHTLRSRLsIILQDPILFSGSIRFNLDPECKCtdDRLWEALEIAQLKNM-VKSLPGgldavvteggenfsvGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1779 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIeQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1858
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
....*.
gi 113193620 1859 HGGYYA 1864
Cdd:cd03288 245 EDGVFA 250
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
976-1054 |
1.54e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.97 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 976 ESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVI 1053
Cdd:COG4170 153 NSYP-HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTITV 231
|
.
gi 113193620 1054 M 1054
Cdd:COG4170 232 L 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
982-1056 |
1.70e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113193620 982 QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYlSDSLVIMRN 1056
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRY-ANTIFVLSN 654
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1663-1709 |
1.92e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 113193620 1663 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF 1709
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
881-919 |
3.26e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.60 E-value: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLL-------TGQIRQSSGKvllaGEH 919
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALlpeldlrTGEISEKLGR----GRH 146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
867-1079 |
3.77e-03 |
|
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: 41.38 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 867 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTL----IKLLTGQirqssgkvllaGEHQV-GVCWQ--------------- 926
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----------GDIQIdGVSWNsvplqkwrkafgvip 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 927 DNILIPTLTAREHLQlyaqikipPGGSGGVEEI---------RSEVAQTLQSLNFgkHESYPSWQLSGGYRRRLCVAIAF 997
Cdd:cd03289 84 QKVFIFSGTFRKNLD--------PYGKWSDEEIwkvaeevglKSVIEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 998 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMdEAKYLSDSLVIMRNGRIiaqHSRDSLQRLCTSNYS 1077
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV---RQYDSIQKLLNEKSH 229
|
..
gi 113193620 1078 IR 1079
Cdd:cd03289 230 FK 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
977-1068 |
4.67e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 977 SYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIM 1054
Cdd:PRK15093 154 SFP-YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWADKINVL 232
|
90
....*....|....
gi 113193620 1055 RNGRIIAQHSRDSL 1068
Cdd:PRK15093 233 YCGQTVETAPSKEL 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1666-1851 |
5.79e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1666 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQpGISYCPQS----NPldpllTTTECIRFYGRLRG 1741
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-SIAYVPQQawimNA-----TVRGNILFFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1742 IR------------DLDQfLDRVLDTyELRPyKDVqvrNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVya 1809
Cdd:PTZ00243 750 ARladavrvsqleaDLAQ-LGGGLET-EIGE-KGV---NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV-- 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 113193620 1810 tIEQLLLARRA---VVLTSHSVseieHLCQR---VAVLRAGQVIASDS 1851
Cdd:PTZ00243 822 -VEECFLGALAgktRVLATHQV----HVVPRadyVVALGDGRVEFSGS 864
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
881-912 |
8.67e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 8.67e-03
10 20 30
....*....|....*....|....*....|....*....
gi 113193620 881 RNQVSCLLGRNGAGKSTLIKLL-------TGQIRQSSGK 912
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALlpelvlaTGEISEKLGR 122
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1669-1840 |
9.88e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1669 VNFS-VQRGECFGLLGKNGAGKSTIFKLLTGQLqpdvgqiYFEQPGIsycPQSNPLDPLLTTTEC---IRFYGRLRGIR- 1743
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAITYAL-------YGKTPRY---GRQENLRSVFAPGEDtaeVSFTFQLGGKKy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113193620 1744 --------DLDQFLDRVL------DTYELRPYKdvqvrNLSGGNRRKLTVA--------VTCCGCTP--TVLMDEPTSDM 1799
Cdd:cd03279 90 rversrglDYDQFTRIVLlpqgefDRFLARPVS-----TLSGGETFLASLSlalalsevLQNRGGARleALFIDEGFGTL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 113193620 1800 DPVTRDMVYATIEQLLLARRAVVLTSHsVSEI-EHLCQRVAV 1840
Cdd:cd03279 165 DPEALEAVATALELIRTENRMVGVISH-VEELkERIPQRLEV 205
|
|
| |
