|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
179-1850 |
7.05e-130 |
|
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: 454.47 E-value: 7.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 179 ETFVKL-GVL---LCGHPFPNTDTIPLVNEILESE-------DFSQANDA-EIDAMPTKYCKRLYRDVTSTNQGKLTWNT 246
Cdd:TIGR01257 310 ETFTQLmGILsdlLCGYPEGGGSRVFSFNWYEDNNykaflgiDSTRKDPIySYDKRTTSFCNALIQSLESNPLTKIAWRA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 247 IKPIIQGRILYTPANAMTESVVKFSNASFEELDRLKQLSRAAATILTKL---HTNATFQEAFDNLLKlakSPLVKSLVgd 323
Cdd:TIGR01257 390 AKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIwyfFDKSTQMTMIRDTLQ---NPTVKDFI-- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 324 DFDIGE----IERVFEYI----RTNQL----------IYDI----LTTVADLMDCVSADRFEAVESVEELHKRAYELNQN 381
Cdd:TIGR01257 465 NRQLGEegitAEAVLNFLyngpREKQAddmtnfdwrdIFNItdrfLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 382 KLFLAALNLEDVGLKQAS------YRLHMDTDNTQPTFENRNRFWFPGPADSMVIDLKY-HRGFVQLKQMVDLGIIKSKR 454
Cdd:TIGR01257 545 NRFWAGVVFPDMYPWTSSlpphvkYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYiWGGFAYLQDMVEQGITRSQM 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 455 EEAgfapeedgpesgrslsglfsikqvendtpdeddddfdlsleesgdekaAPkvsasasdheattispssldgvtteev 534
Cdd:TIGR01257 625 QAE------------------------------------------------PP--------------------------- 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 535 rvtteqtvvsgdpdllllknedvlkrskrqglfdllggfggsgdankknkfevdnMQFYTKQFPYPAFLNDVFKrgLYLA 614
Cdd:TIGR01257 630 -------------------------------------------------------VGIYLQQMPYPCFVDDSFM--IILN 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 615 QGVQVAYLLGLVVFVALSVRERIWMRESRNSMLMRSMGLKAHSELVAWALMSFLELCVIFALISGVLYSGGILGYTNWFF 694
Cdd:TIGR01257 653 RCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFI 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 695 MMFYCLSFGLCLISFCYMCTNFFNSANIGAVASALLFFISLCPFIIVLMFDAKLSVFESFLVDLSFTTAFAKGWGELIRM 774
Cdd:TIGR01257 733 LFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRF 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 775 ELQQEGLTVRHLIQVGPARSECA--MALLMFLLDLLLYAVIGLAYQRYKKNNYS-----FVKVSRSQLDGKLGAS----- 842
Cdd:TIGR01257 813 EEQGLGLQWSNIGNSPLEGDEFSflLSMKMMLLDAALYGLLAWYLDQVFPGDYGtplpwYFLLQESYWLGGEGCStreer 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 -----------------------------------------LVNVSKLYGsKCAVSNLSLDFARNQVSCLLGRNGAGKST 881
Cdd:TIGR01257 893 alekteplteemedpehpegindsfferelpglvpgvcvknLVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTT 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 882 LIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNILIPTLTAREHLQLYAQIKippGGSGgvEEIRSEVAQTL 951
Cdd:TIGR01257 972 TLSILTGLLPPTSGTVLVGGKdietnldavrQSLGMCPQHNILFHHLTVAEHILFYAQLK---GRSW--EEAQLEMEAML 1046
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 952 QSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYL 1031
Cdd:TIGR01257 1047 EDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLL 1126
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1032 SDSLVIMRNGRIIA--------------------------QHSRDSLQRLCT-SNYSIRLRCA----------------- 1067
Cdd:TIGR01257 1127 GDRIAIISQGRLYCsgtplflkncfgtgfyltlvrkmkniQSQRGGCEGTCScTSKGFSTRCParvdeitpeqvldgdvn 1206
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1068 -----------DATGVTFVIQKAQQLLPQTQVTHSGAADYPHSLTIN------ASYAEHLTPGAVEFLELLQSqVTAGSI 1130
Cdd:TIGR01257 1207 elmdlvyhhvpEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETladlglSSFGISDTPLEEIFLKVTED-ADSGSL 1285
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1131 sdveltTSSSLEQEFEQLNRNGEDAGPRR--------PASDRSGVVAGPAMITDEPPTACKQFRL-------------LM 1189
Cdd:TIGR01257 1286 ------FAGGAQQKRENANLRHPCSGPTEkagqtpqaSHTCSPGQPAAHPEGQPPPEPEDPGVPLntgarlilqhvqaLL 1359
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1190 GKRLRHLSRNYRLLLYVLLLPALFELCAM-------------------WFVSYR-------------------------- 1224
Cdd:TIGR01257 1360 VKRFQHTIRSHKDFLAQIVLPATFVFLALmlsiiippfgeypaltlhpWMYGQQytffsmdepnsehlevladvllnkpg 1439
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1225 -----LEDDFDTVLPL-------SRSLYPQTAQFLSHERAT----------SFSEKLY-------------PQLRT--SC 1267
Cdd:TIGR01257 1440 fgnrcLKEEWLPEYPCgnstpwkTPSVSPNITHLFQKQKWTaahpspscrcSTREKLTmlpecpegagglpPPQRTqrST 1519
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1268 DHLGECRVFNTSQ---QSYDWVLNS------WgeYSERRYGGYGLNG-------------------------SGA----- 1308
Cdd:TIGR01257 1520 EILQDLTDRNISDflvKTYPALIRSslkskfW--VNEQRYGGISIGGklpaipitgealvgflsdlgqmmnvSGGpvtre 1597
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1309 ------------------TVWYNNKGYHSMMAWLNDLNSELLRTTM----NDSESSILTLNEPWKLGFAELSTSSILRQA 1366
Cdd:TIGR01257 1598 askempdflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLpkdrDPEEYGITVISQPLNLTKEQLSEITVLTTS 1677
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1367 GDGSMVFILLIAFGLVVASGSVYLVNERVNGEKLQQRLCGVSAVTYWLVALVWDYLVMVLGLIVCLVVILMFGMPVFVDR 1446
Cdd:TIGR01257 1678 VDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSP 1757
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1447 QQLVGIIGLSLAFSFACVPSVHVAEKIFSDSSIAIVSIFCANLIVPLVTMGIILILGVVGDGPAWDDWRHALNQAFLIFP 1526
Cdd:TIGR01257 1758 ENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFP 1837
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1527 IHALGDGFLELCKNYMVALVFRRYDIDSYKHPLASDLLGRHFTALLLVGVAALIINVLIEWHLLRRLW---QRVERLLDc 1603
Cdd:TIGR01257 1838 HFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWiaePAKEPIFD- 1916
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1604 tyrrELDKLGQLKlvniQSIFKSCVDTgEAVRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG 1682
Cdd:TIGR01257 1917 ----EDDDVAEER----QRIISGGNKT-DILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1683 QLQPDVG-----------QIYFEQPGISYCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQ 1749
Cdd:TIGR01257 1988 DTTVTSGdatvagksiltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVpaEEIEKVANWSIQSLGLSLYADRL 2067
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1750 VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:TIGR01257 2068 AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
2010 2020
....*....|....*....|.
gi 221500365 1830 VIASDSPQRLKSEHGGYYAVT 1850
Cdd:TIGR01257 2148 FQCLGTIQHLKSKFGDGYIVT 2168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1634-1840 |
2.98e-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: 2.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYC 1701
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIRFYGRLRGIRDLDQFL--DRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1779
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEevELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1780 TSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1840
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
842-1056 |
7.82e-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: 7.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQ-VGVCW 909
Cdd:cd03263 2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaaRQsLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQIKippGGSggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:cd03263 82 QFDALFDELTVREHLRFYARLK---GLP--KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQhsrDSLQRLC 1056
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCI---GSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
845-1054 |
2.74e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 213.00 E-value: 2.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNIL 914
Cdd:COG1131 5 GLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKippGGSGgvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:COG1131 85 YPDLTVRENLRFFARLY---GLPR--KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 995 NGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG1131 160 SGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1634-1843 |
7.17e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.99 E-value: 7.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYCP 1702
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvaRDPAevrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1780
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1781 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
842-1043 |
3.39e-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: 187.22 E-value: 3.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 911
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLyaqikippggsggveeirsevaqtlqslnfgkhesypswqlSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:cd03230 82 PSLYENLTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 992 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
845-1059 |
6.40e-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: 186.22 E-value: 6.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH----------QVGVCWQDNIL 914
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkeprearrQIGVLPDERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:COG4555 86 YDRLTVRENIRYFAELYGLFD-----EELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 995 NGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL-QRLCTSN 1059
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELrEEIGEEN 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1635-1844 |
5.92e-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: 166.19 E-value: 5.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQP-----GISYCPQ 1703
Cdd:COG4555 3 EVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedvrKEPrearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHG 1844
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
845-1046 |
4.11e-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: 159.69 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDNILI 915
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTAREHLQLYAQIKIPPggsggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:cd03268 85 PNLTARENLRLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 996 GVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03268 156 GLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1634-1840 |
2.23e-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: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLwlAYRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYC 1701
Cdd:cd03265 1 IEVENL--VKKYGDFeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvREPRevrrrIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVL-MDE 1778
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-RPEVLfLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1779 PTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1840
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1634-1830 |
5.98e-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: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYCP 1702
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLgkdikkepeevKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECIRfygrlrgirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:cd03230 80 EEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
845-1053 |
7.52e-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: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQDNIL 914
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPG-----AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 995 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1053
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
845-1046 |
1.71e-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: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDn 912
Cdd:COG1122 5 NLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrRKVGLVFQN- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 iliPtltarEHlQLYA------------QIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 980
Cdd:COG1122 84 ---P-----DD-QLFAptveedvafgpeNLGLPR------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
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 ... |
842-1050 |
3.57e-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: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSK----CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVGVCWQD 911
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgPDRGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIKIPPGGsggveEIRSEVAQTLQSLNFGKHE-SYPsWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:cd03293 82 DALLPWLTVLDNVALGLELQGVPKA-----EARERAEELLELVGLSGFEnAYP-HQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 991 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIAQHSRD 1050
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
842-1046 |
1.34e-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: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFArNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ----------VGVCWQD 911
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkqpqklrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIK-IPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKgIPSK------EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
842-1023 |
1.40e-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: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 911
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG4133 84 DGLKPELTVRENLRFWAALY-------GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 221500365 992 EPCNGVDAKARKDIWQLIER-LRQGRAVIFATH 1023
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
842-1042 |
4.47e-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: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniliptltar 921
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 ehlqlyaqikipPGGSGGVEEIRSEVAQTlqslnfgkhesypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:cd00267 62 ------------DIAKLPLEELRRRIGYV--------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1002 RKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
Cdd:cd00267 116 RERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1645-1869 |
4.73e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.90 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1645 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-----------FEQPGISYCPQSNPLDPLLTT 1713
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvpararLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1714 TECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMV 1791
Cdd:PRK13536 132 RENLLVFGRYFGMstREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1792 YATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVTCFCG-PAQQAILSRSLNQRL 1869
Cdd:PRK13536 212 WERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGdPHELSSLVKPYARRI 290
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1634-1832 |
1.15e-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: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPG--------ISYCPQSN 1705
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnrIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 PLDPLLTTTECIRFYGRLRG--IRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1783
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1784 DPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
843-1045 |
2.66e-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: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDNI 913
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvppERrnIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLyaqikipPGGSGGV--EEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:cd03259 83 LFPHLTVAENIAF-------GLKLRGVpkAEIRARVRELLELVGLEGLLNrYPH-ELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 991 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1634-1839 |
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 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS--------- 1704
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD--GKDITKKNlrelrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ----NPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvtccgctpTVL- 1775
Cdd:COG1122 79 lvfqNPDDQLFAPTveEDVAFGPENLGLprEEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA--------GVLa 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1776 -------MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:COG1122 151 mepevlvLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
842-1042 |
2.11e-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: 137.60 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGS--KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVC 908
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQD---NILIPTLT-----AREHLQLyaqikiPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 980
Cdd:cd03225 81 FQNpddQFFGPTVEeevafGLENLGL------PE------EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
842-1065 |
3.01e-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: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSK----CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVG 906
Cdd:COG1124 3 EVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQD--NILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKH--ESYPSwQLSGGYRRRLCVAIAFI 982
Cdd:COG1124 83 MVFQDpyASLHPRHTVDRILAEPLRIH-------GLPDREERIAELLEQVGLPPSflDRYPH-QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQRLCTSNY 1060
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*
gi 221500365 1061 SIRLR 1065
Cdd:COG1124 235 TRELL 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
842-1045 |
7.89e-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: 137.91 E-value: 7.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVGVCWQD 911
Cdd:COG1116 9 ELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIKippggsgGV--EEIRSEVAQTLQSLNFGKHE-SYPsWQLSGGYRRRlcVAIA--FIASPS 986
Cdd:COG1116 89 PALLPWLTVLDNVALGLELR-------GVpkAERRERARELLELVGLAGFEdAYP-HQLSGGMRQR--VAIAraLANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIA 1045
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
842-1054 |
1.25e-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: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGV 907
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 908 CWQDNILIPTLTA--------REHLQLYAqikippggsggvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVA 978
Cdd:cd03261 82 LFQSGALFDSLTVfenvafplREHTRLSE------------EEIREIVLEKLEAVGLrGAEDLYPA-ELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 979 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1646-1921 |
1.35e-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: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-------GISYCPQSNPLDPLLTTTECI 1717
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgEPldpedrrRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1718 RFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRK--LTVAVTccgCTPTVL-MDEPTSDMDPVTRDMvy 1792
Cdd:COG4152 93 VYLARLKGLskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKvqLIAALL---HDPELLiLDEPFSGLDPVNVEL-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1793 atIEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGG-YYAVTCfcgPAQQAILsrslnQ 1867
Cdd:COG4152 168 --LKDVIRELAAkgttVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRnTLRLEA---DGDAGWL-----R 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1868 RLPGARDLQHYAHSLRFLVrvrsPGSLGDAPLLSELFAIlcdvcVNVARFSLSR 1921
Cdd:COG4152 238 ALPGVTVVEEDGDGAELKL----EDGADAQELLRALLAR-----GPVREFEEVR 282
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1647-1844 |
1.37e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 138.78 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1647 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF---EQPG--------ISYCPQSNPLDPLLTTTE 1715
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgePVPSrarharqrVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFYGRLRG-----IRDLDQFLdrvLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDM 1790
Cdd:PRK13537 100 NLLVFGRYFGlsaaaARALVPPL---LEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1791 VYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL-KSEHG 1844
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIG 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1634-1824 |
1.48e-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: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAyRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI-----------SYCP 1702
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHlCQRVAV 1824
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA-ARVLDL 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
842-1046 |
3.76e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 137.24 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQD 911
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIKippGGSGGveEIRSEVAQTLQslnFGKHES---YPSWQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:PRK13537 89 DNLDPDFTVRENLLVFGRYF---GLSAA--AARALVPPLLE---FAKLENkadAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 989 ILDEPCNGVDAKARKDIWqliERLR----QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMW---ERLRsllaRGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1633-1837 |
5.90e-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: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPG------ISYCPQSN 1705
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPrrarrrIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 PLDPLLTTT--ECIR--FYGR---LRGIRDLD-QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1777
Cdd:COG1121 85 EVDWDFPITvrDVVLmgRYGRrglFRRPSRADrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1778 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLrAGQVIASDSPQ 1837
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
845-1052 |
6.68e-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: 134.34 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNIL 914
Cdd:TIGR03864 6 GLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHdlrrapraalARLGVVFQQPTL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKippGGSGGVEEIRSEVAQTLQSLNFGKHEsyPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:TIGR03864 86 DLDLSVRQNLRYHAALH---GLSRAEARARIAELLARLGLAERADD--KVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 995 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALarDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1636-1833 |
1.57e-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: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLWLAYRRGHyAVRNVNFSVQRGeCFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG-----ISYCPQS 1704
Cdd:cd03264 3 LENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQklrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIpsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1783 MDPVTRdMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:cd03264 161 LDPEER-IRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
843-1042 |
2.13e-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: 127.69 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCW 909
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLyaqikippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:cd03229 83 QDFALFPHLTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1632-1836 |
2.73e-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: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1632 EAVRAENLWLAYRRGH---------------------YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQ 1690
Cdd:COG1134 3 SMIEVENVSKSYRLYHepsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1691 IyfeqpgISYCPQSNPL------DPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLT 1762
Cdd:COG1134 83 V------EVNGRVSALLelgagfHPELTGRENIYLNGRLLGLsrKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1763 VAV-TCcgCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1836
Cdd:COG1134 157 FAVaTA--VDPDILlVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
842-1044 |
2.88e-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: 133.30 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDN 912
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppEKrnVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQ--LYAQiKIPPggsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA--FIASPSV 987
Cdd:COG3842 87 ALFPHLTVAENVAfgLRMR-GVPK------AEIRARVAELLELVGLEGLADrYPH-QLSGGQQQR--VALAraLAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
845-1044 |
3.49e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.02 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH--------------QVGVCW 909
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipylrrRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLN-FGKHESYPSwQLSGGYRRRLCVAIAFIASPSV 987
Cdd:COG2884 86 QDFRLLPDRTVYENVALPLRVtGKSR------KEIRRRVREVLDLVGlSDKAKALPH-ELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATH---FMDEAKYlsdSLVIMRNGRII 1044
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHdleLVDRMPK---RVLELEDGRLV 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
842-1046 |
3.72e-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: 126.39 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniLIPTLTAR 921
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-----------EVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 EHLQLyaqikippggsgGVEEIrsevaqtlqslnfgkhesypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:cd03216 71 DARRA------------GIAMV---------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1002 RKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03216 118 VERLFKVIRRLRaQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1635-1837 |
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 221500365 1635 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------QP------GISYC 1701
Cdd:cd03219 2 EVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPheiarlGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIR------------FYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCG 1769
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1770 CTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
842-1046 |
5.14e-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: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 910
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelaRRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTARE--------HLQLYAQIKippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 982
Cdd:COG1120 83 EPPAPFGLTVRElvalgrypHLGLFGRPS---------AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
845-1046 |
5.57e-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: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVC--WQDN 912
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppHEIarlGIGrtFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQIK-----IPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 987
Cdd:cd03219 85 RLFPELTVLENVMVAAQARtgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
842-1054 |
7.57e-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: 7.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGV 907
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 908 CWQDNILIPTLTAREHLQ--LYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA--FI 982
Cdd:COG1127 87 LFQGGALFDSLTVFENVAfpLREHTDLSE------AEIRELVLEKLELVGLPGAADkMPS-ELSGGMRKR--VALAraLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
843-1046 |
9.96e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 131.11 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH----------QVGVCWQDN 912
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlaraRIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYaqikippGGSGGVEEIRSE-VAQTLqsLNFGKHES---YPSWQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:PRK13536 124 NLDLEFTVRENLLVF-------GRYFGMSTREIEaVIPSL--LEFARLESkadARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 989 ILDEPCNGVDAKARKDIWqliERLR----QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIW---ERLRsllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
842-1046 |
1.18e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.63 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTAR 921
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-----------LASLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 EHLQlyaqikippggsggveeIRSEVAQTLQSLNFG--KHESYpsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 999
Cdd:cd03214 70 ELAR-----------------KIAYVPQALELLGLAhlADRPF--NELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1000 KARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03214 131 AHQIELLELLRRLarERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
845-1054 |
1.40e-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: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDN 912
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelrRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKHE---SYPsWQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:cd03295 85 GLFPHMTVEENIALVPKLlKWPK------EKIRERADELLALVGLDPAEfadRYP-HELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
842-1052 |
1.70e-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: 134.65 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------- 902
Cdd:COG1123 262 EVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 HQVGVCWQD--NILIPTLTAREH----LQLYaqikippgGSGGVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRR 974
Cdd:COG1123 342 RRVQMVFQDpySSLNPRMTVGDIiaepLRLH--------GLLSRAERRERVAELLERVGLPPDlaDRYP-HELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 975 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
845-1046 |
1.85e-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: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVC--WQDN 912
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglppHRIarlGIArtFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQIKIPPGGSGGV----------EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 982
Cdd:COG0411 89 RLFPELTVLENVLVAAHARLGRGLLAALlrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
845-1046 |
2.07e-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: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQVGVCWQDNILIPT 917
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarNRIGYLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLQLYAQIK-IPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:cd03269 85 MKVIDQLVYLAQLKgLKK------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 997 VDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
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 ... |
1634-1833 |
2.54e-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: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYR---RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-----GIS 1699
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkEPaearrRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1700 YCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1777
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLkgDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1778 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
842-1048 |
2.96e-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: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSK----CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 902
Cdd:COG1136 6 ELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 HQVGVCWQDNILIPTLTAREhlqlyaQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF 981
Cdd:COG1136 86 RHIGFVFQFFNLLPELTALE------NVALPLLLAGvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHS 1048
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
842-1043 |
3.35e-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: 125.68 E-value: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 902
Cdd:cd03255 2 ELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 HQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAF 981
Cdd:cd03255 82 RHIGFVFQSFNLLPDLTALENVELPLLLAGVPK-----KERRERAEELLERVGLGDRLNhYPS-ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYlSDSLVIMRNGRI 1043
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
845-1046 |
9.25e-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: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVG 906
Cdd:cd03257 6 NLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrKEIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQD--NILIPTLTAREHLQ--LYAQikippGGSGGVEEIRSEVAQTLQSLNFGKH--ESYPSwQLSGGYRRRLCVAIA 980
Cdd:cd03257 86 MVFQDpmSSLNPRMTIGEQIAepLRIH-----GKLSKKEARKEAVLLLLVGVGLPEEvlNRYPH-ELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1635-1829 |
1.32e-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: 123.73 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1704
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 --NPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDE 1778
Cdd:cd03225 81 fqNPDDQFFGPTveEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1779 PTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1213-1584 |
2.32e-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: 127.51 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1213 FELCAMWFVSYRLEDDFDT---VLPLSRS-LYPQTAQFLSHERATSFSEKlypqlrtscdhlgecrvFNTSQQSYDWVLN 1288
Cdd:pfam12698 14 LILLLGLIFSNAVNDPEELpvaVVDEDNSsLSRQLVRALEASPTVNLVQY-----------------VDSEEEAKEALKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1289 SWGEYSERRYGGYGLN-----GSGATVWYNNKGYHSMMAWLNDLNSELLRTTMNDSESSILTLNEPWKLGFAELSTSSIL 1363
Cdd:pfam12698 77 GKIDGLLVIPKGFSKDllkgeSATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1364 RQAGDGSMVFILLIAFGLVVASGSVYLVNERVNGEKLQQRLCGVSAVTYWLVALVWDYLVMVLGLIVCLvvILMFGMPVF 1443
Cdd:pfam12698 157 SGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL--LLLFGIGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1444 VDrqQLVGIIGLSLAFSFACVPSVHVAEKIFSDSSIAIVSIFCANLIVplvtMGIILILGVVGDGPAWddwrhaLNQAFL 1523
Cdd:pfam12698 235 FG--NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLL----SGFFGGLFPLEDPPSF------LQWIFS 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1524 IFPIHALGDGFLELCKNYmvalvfrrydidsykhPLASdlLGRHFTALLLVGVAALIINVL 1584
Cdd:pfam12698 303 IIPFFSPIDGLLRLIYGD----------------SLWE--IAPSLIILLLFAVVLLLLALL 345
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
842-1050 |
3.73e-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: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqVGVCWQD---------- 911
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-PRRARRRigyvpqraev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPtLTAREHLQLYAQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG1121 87 DWDFP-ITVRDVVLMGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 992 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMrNGRIIAQHSRD 1050
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
842-1043 |
4.06e-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: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDN 912
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPK-----AEIKERVAEALDLVQLEGYANrKPS-QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 992 EPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1635-1834 |
4.36e-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: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-------EQPGISYCPQSNPL 1707
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DPL--LTTTECI--RFYGRLRGIRDLD----QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1779
Cdd:cd03235 80 DRDfpISVRDVVlmGLYGHKGLFRRLSkadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1780 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLrAGQVIASD 1834
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
842-1045 |
7.37e-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: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQD 911
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprERRVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLN---FGKHesYPSwQLSGGYRRRlcVAIA--FIASPS 986
Cdd:COG1118 84 YALFPHMTVAENIAFGLRVRPPSK-----AEIRARVEELLELVQlegLADR--YPS-QLSGGQRQR--VALAraLAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1649-1837 |
2.33e-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: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTE 1715
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglpphriaRLGIARTFQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CI-----------------RFYGRLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVLM-D 1777
Cdd:COG0411 99 NVlvaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT-EPKLLLlD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1778 EPTSDMDPV-TRDMVyATIEQLllaRR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:COG0411 178 EPAAGLNPEeTEELA-ELIRRL---RDergiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1635-1829 |
2.87e-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: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpldpllttt 1714
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 ecirfygRLRGIRDLDQfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1794
Cdd:cd00267 71 -------LRRRIGYVPQ---------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 221500365 1795 IEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
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 ... |
842-1052 |
3.07e-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: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVCW-- 909
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppHERaraGIGYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQIKIPPGGSGGVEEI----------RSEVAQTlqslnfgkhesypswqLSGGYRRRLCVAI 979
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfprlkerRKQLAGT----------------LSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1646-1833 |
3.93e-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: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLD------------PLLTT 1713
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD--GKSYQKNIEALRrigalieapgfyPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1714 TECIRFYGRLRGIRDLDQflDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPV-TRDMvy 1792
Cdd:cd03268 90 RENLRLLARLLGIRKKRI--DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDgIKEL-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 1793 atiEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:cd03268 166 ---RELILSLRDqgitVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
845-1046 |
6.64e-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: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------HQVG-VCWQDNIL--I 915
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGyVPQRRSIDrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PtLTAREHLQLYAQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:cd03235 84 P-ISVRDVVLMGLYGHKGLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 996 GVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSlVIMRNGRIIAQ 1046
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 ... |
844-1044 |
7.72e-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: 7.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 844 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNIL 914
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKiPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEP 993
Cdd:cd03296 86 FRHMTVFDNVAFGLRVK-PRSERPPEAEIRAKVHELLKLVQLdWLADRYPA-QLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 994 CNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1634-1834 |
1.42e-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: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGH---------------------YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY 1692
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1693 --------FEqPGISycpqsnpLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLT 1762
Cdd:cd03220 81 vrgrvsslLG-LGGG-------FNPELTGRENIYLNGRLLGLsrKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1763 VAV-TCCGCtPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1834
Cdd:cd03220 153 FAIaTALEP-DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
842-1054 |
1.52e-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: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQVGVCWQDNI-------- 913
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPEDRRRIgylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLYAQIKippggsgGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG4152 82 LYPKMKVGEQLVYLARLK-------GLskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 992 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
842-1044 |
2.08e-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: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI-----RQSSGKVLLAGE-------------H 903
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiydldvdvlelrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 904 QVGVCWQdnilIPTLTareHLQLYAQIKIPP--GGSGGVEEIRSEVAQTLQSLNFGKHESYPSW--QLSGGYRRRLCVAI 979
Cdd:cd03260 82 RVGMVFQ----KPNPF---PGSIYDNVAYGLrlHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
842-1052 |
2.69e-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: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH----------QVGVCW-- 909
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkraRLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSK-----KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1633-1837 |
2.71e-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: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG--------------I 1698
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--GrdlaslsrrelarrI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1699 SYCPQSNPLDPLLTTTECIRfYGRLRGIRDLDQF-------LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1771
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVA-LGRYPHLGLFGRPsaedreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1772 PTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHsvsEIEH---LCQRVAVLRAGQVIASDSPQ 1837
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLH---DLNLaarYADRLVLLKDGRIVAQGPPE 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
842-1055 |
2.95e-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: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCW 909
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQikipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRrlCVAI--AFIASP 985
Cdd:COG1129 86 QELNLVPNLSVAENIFLGRE----PRRGGLIdwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ--LVEIarALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 986 SVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH-----SRDSLQRL 1055
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
843-1043 |
3.48e-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: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNI 913
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkDRDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPK-----DEIDERVREVAELLQIEHLlDRKPK-QLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 993 PCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
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 ... |
855-1045 |
7.02e-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: 7.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------EHQVGVCWQDNILIPTLTAREHL 924
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaeaRRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYaqikippGGSGGVE--EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:cd03266 100 EYF-------AGLYGLKgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1003 KDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:cd03266 173 RALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1634-1839 |
1.36e-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: 116.10 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ------P-------GISY 1700
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPmhkrarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1701 CPQSNPLDPLLTTTECIR----FYGRLRGIRdlDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM 1776
Cdd:cd03218 80 LPQEASIFRKLTVEENILavleIRGLSKKER--EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIA-RALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1777 -DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:cd03218 157 lDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1646-1833 |
1.80e-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: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPqSNPLDplltttecirfyGRLRG 1725
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--GKEVSF-ASPRD------------ARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1726 IRDLDQfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAV 1805
Cdd:cd03216 77 IAMVYQ---------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180
....*....|....*....|....*...
gi 221500365 1806 VLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
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 ... |
1635-1842 |
2.48e-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: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-------GISYC 1701
Cdd:cd03224 2 EVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditgLPpheraraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTY-ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVLM- 1776
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIAralMS----RPKLLLl 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1777 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1634-1831 |
6.42e-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: 113.75 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------Q 1695
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1696 PGISYCPQsNP---LDPLLTT----TECIRFYGR--------------LRGIRDLDQFLDRvldtyelRPYKdvqvrnLS 1754
Cdd:cd03257 82 KEIQMVFQ-DPmssLNPRMTIgeqiAEPLRIHGKlskkearkeavlllLVGVGLPEEVLNR-------YPHE------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1755 GGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDPVTRdmvyATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAG 1828
Cdd:cd03257 148 GGQRQRVAIARALA-LNPKLLIaDEPTSALDVSVQ----AQILDLLkkLQEElglTLLFITHDLGVVAKIADRVAVMYAG 222
|
...
gi 221500365 1829 QVI 1831
Cdd:cd03257 223 KIV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
845-1054 |
8.21e-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: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQV-------GVCWQDNI 913
Cdd:COG4525 8 HVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVtgpgadrGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLYAQIKippggsgGVE--EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG4525 87 LLPWLNVLDNVAFGLRLR-------GVPkaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 992 EPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIM--RNGRIIAQHSRDSLQR 1054
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLELDFSRR 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1629-1839 |
9.50e-28 |
|
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: 9.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAVRAENLWLAY----RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------- 1694
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklsrr 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1695 -----QPGISYCPQsNP---LDPLLTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRP-YKDVQVRNLSGGNRRKLT 1762
Cdd:COG1123 336 slrelRRRVQMVFQ-DPyssLNPRMTVGDIIAEPLRLHGLLSRAERRERVaelLERVGLPPdLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1763 VA---VTccgcTPTVLM-DEPTSDMDPVtrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:COG1123 415 IAralAL----EPKLLIlDEPTSALDVS----VQAQILNLLrdLQRElglTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
....*.
gi 221500365 1834 DSPQRL 1839
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 ... |
858-1044 |
1.59e-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: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----HQVGVCW---QD-NILIPTLTAREhlQLYA 928
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakERRKSIGyvmQDvDYQLFTDSVRE--ELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 929 QIKIPPGGSGGVEEIrsevaqtLQSLN-FGKHESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1007
Cdd:cd03226 96 GLKELDAGNEQAETV-------LKDLDlYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 221500365 1008 LIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03226 168 LIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
844-1052 |
2.16e-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: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 844 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS---SGKVLLAGE-----------HQVGVCW 909
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRdllelsealrgRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QD--NILIPtLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 987
Cdd:COG1123 90 QDpmTQLNP-VTVGDQIAEALENLGLSR-----AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
842-1054 |
2.21e-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: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---HQVGVCWQDNI---- 913
Cdd:COG4988 338 ELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsDLDPASWRRQIawvp 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 ---LIPTLTAREHLQLYAqikipPGGSGgvEEIRSEVAQT-----LQSLNFGKH----ESypSWQLSGGYRRRLCVAIAF 981
Cdd:COG4988 418 qnpYLFAGTIRENLRLGR-----PDASD--EELEAALEAAgldefVAALPDGLDtplgEG--GRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLA 560
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
842-1043 |
1.16e-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: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH---------QVGVCWQDN 912
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrNIAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRlcVAI--AFIASPSVV 988
Cdd:COG3839 85 ALYPHMTVYENIAFPLKLrKVPK------AEIDRRVREAAELLGLEDLlDRKPK-QLSGGQRQR--VALgrALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 989 ILDEPCNGVDAKARkdiWQLIERLRQ-----GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
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 ... |
858-1046 |
1.29e-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: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARN-QVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------------EHQVGVCWQDNILIPTLTAR 921
Cdd:cd03297 14 TLKIDFDLNeEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 EHLqLYAQIKIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:cd03297 94 ENL-AFGLKRKRNR------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1002 RKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
856-995 |
4.47e-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: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTLTAREHL 924
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 925 QLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFG----KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:pfam00005 81 RLGLLLKGLSK-----REKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
855-1054 |
7.39e-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: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREH 923
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrRRIAVVPQRPHLFDT-TLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 924 LQLYAqikipPGGSggvEEirsEVAQTLQSLNFGKH-ESYP----SW------QLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:COG4987 429 LRLAR-----PDAT---DE---ELWAALERVGLGDWlAALPdgldTWlgeggrRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 993 PCNGVDAKARKDIWQLIERLRQGRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGRTVLLITHrlaGLERM----DRILVLEDGRIVEQGTHEELLA 558
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1650-1781 |
7.46e-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: 105.04 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQSNPLDPLLTTTECI 1717
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderkslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1718 RFYGRLRGI--RDLDQFLDRVLDTYELRPYKD----VQVRNLSGGNRRKLTVAVTCCgCTPTVL-MDEPTS 1781
Cdd:pfam00005 81 RLGLLLKGLskREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALL-TKPKLLlLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
850-1052 |
7.73e-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: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GVCW--QDNILIPT 917
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglppHRIarlGIGYvpEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLQLYAQikiPPGGSGGVEEIRSEVAQTLQSLnfGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGV 997
Cdd:COG0410 93 LTVEENLLLGAY---ARRDRAEVRADLERVYELFPRL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 998 DAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG0410 168 APLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1635-1837 |
1.68e-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: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ------P-------GISYC 1701
Cdd:COG1137 5 EAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQsnplDPL----LTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPT-V 1774
Cdd:COG1137 84 PQ----EASifrkLTVEDNILAVLELRKLskKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA-RALATNPKfI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1775 LMDEPTSDMDPVT----RDMVYAtieqllLARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKIIRH------LKERgiGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1635-1831 |
1.84e-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: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS---------YCPQsN 1705
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksigYVMQ-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 PLDPLLTTT---ECirfygrLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVT-CCGCtPTVLMDE 1778
Cdd:cd03226 80 VDYQLFTDSvreEL------LLGLKELDAGNEQaetVLKDLDLYALKERHPLSLSGGQKQRLAIAAAlLSGK-DLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1779 PTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
845-1046 |
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 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------H---QVGVCW--QDN 912
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmHeraRLGIGYlpQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQ--LYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:TIGR04406 86 SIFRKLTVEENIMavLEIRKDLDR------AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAE 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
842-1046 |
3.55e-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: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG--------------EH 903
Cdd:cd03258 3 ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 904 QVGVCWQDNILIPTLTAREHLQLYAQIkippggsGGVE--EIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIA 980
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEI-------AGVPkaEIEERVLELLELVGLeDKADAYPA-QLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
842-1043 |
4.19e-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: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 910
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTlTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGkhESYPSWQ---LSGGYRRRLCVAIAFIASPSV 987
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLR-------ERKFDRERALELLERLGLP--PDILDKPverLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
829-1044 |
4.71e-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: 106.96 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 829 KVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------ 902
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaams 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 ---------HQVGVCWQDNILIPTLTAREHLQLYAQIKippggsgGV-EEIRSEVA-QTLQSLNFGKHE-SYPSwQLSGG 970
Cdd:cd03294 93 rkelrelrrKKISMVFQSFALLPHRTVLENVAFGLEVQ-------GVpRAEREERAaEALELVGLEGWEhKYPD-ELSGG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 971 YRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1634-1829 |
4.89e-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: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPG-----------ISY 1700
Cdd:cd03228 1 IEFKNVSFSYPgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1701 CPQsnplDP-LLTTTecirfygrlrgIRDldqfldrvldtyelrpykdvqvrN-LSGGNRRKLTVAVTCCGCTPTVLMDE 1778
Cdd:cd03228 81 VPQ----DPfLFSGT-----------IRE-----------------------NiLSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1779 PTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQ 1829
Cdd:cd03228 123 ATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1649-1834 |
6.85e-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: 105.49 E-value: 6.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-------------YFEQPGISYcPQSNPLDPLLTTTE 1715
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVF-GQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFygrLRGIRDLDQF-----LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTVL-MDEPTSDMDPVTRD 1789
Cdd:cd03267 115 SFYL---LAAIYDLPPArfkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH-EPEILfLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1790 MVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1834
Cdd:cd03267 191 NIRNFLKEYNRERGTtVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1580-1847 |
7.11e-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: 112.62 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1580 IINVLIEWHLLRRLWQRVERLLDctyrRELDKLGQLKLVNIQSIfkscvdTGEaVRAENLWLAYR-RGHYAVRNVNFSVQ 1658
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILD----LPPEREEGRSKLSLPRL------KGD-IELENVSFRYPgDSPPVLDNISLTIK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1659 RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpgISYCPQSNPL------------DPLLT 1712
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIdgidlrqidpaslrRQ--IGVVLQDVFLfsgtirenitlgDPDAT 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 T---TECIRFYGrlrgirdLDQFLDRVLDTYELrpykdvQV----RNLSGGNRRKLTVA---VTccgcTPTVL-MDEPTS 1781
Cdd:COG2274 578 DeeiIEAARLAG-------LHDFIEALPMGYDT------VVgeggSNLSGGQRQRLAIAralLR----NPRILiLDEATS 640
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1782 DMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1847
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 ... |
1635-1833 |
7.42e-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: 103.28 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPqsnpldpllttt 1714
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 ecIRFYGRLRGIrdLDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1794
Cdd:cd03214 68 --PKELARKIAY--VPQALELL----GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 221500365 1795 IEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:cd03214 140 LRRLARERgKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
856-1044 |
7.66e-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: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS---SGKVLLAGE----HQVGVCW----QDNILIPTLTAREHL 924
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpDQFQKCVayvrQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYAQIKIPPGGSGGVEEIRSEVAqTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKD 1004
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKRVEDV-LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1005 IWQLIERL-RQGRAVIFATHF-MDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03234 182 LVSTLSQLaRRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
845-1043 |
8.21e-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: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCW 909
Cdd:cd03292 5 NVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylrRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPP-----REIRKRVPAALELVGLsHKHRALPA-ELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
845-1042 |
1.06e-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: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTARE 922
Cdd:cd03228 5 NVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----------DGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 hlqLYAQIKIPP------GGSggveeIRSEVaqtlqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:cd03228 74 ---LRKNIAYVPqdpflfSGT-----IRENI-------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 997 VDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIMRNGR 1042
Cdd:cd03228 127 LDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
845-1045 |
1.18e-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: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGsKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDNILI 915
Cdd:cd03299 5 NLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekRDISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEP 993
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDK-----KEIERKVLEIAEMLGID-HllNRKPE-TLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 994 CNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1598-1950 |
1.31e-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: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1598 ERLLDCTYRRELDKLGQLKLV-NIQSIFKSCvdtgeavraenlwlayrrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTI 1676
Cdd:TIGR01257 911 EGINDSFFERELPGLVPGVCVkNLVKIFEPS------------------GRPAVDRLNITFYENQITAFLGHNGAGKTTT 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1677 FKLLTGQLQPDVGQIYFE-----------QPGISYCPQSNPLDPLLTTTECIRFYGRLRGiRDLDQF---LDRVLDTYEL 1742
Cdd:TIGR01257 973 LSILTGLLPPTSGTVLVGgkdietnldavRQSLGMCPQHNILFHHLTVAEHILFYAQLKG-RSWEEAqleMEAMLEDTGL 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1743 RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRdmvyATIEQLLL---ARRAVVLTSHSVSEIEHLC 1819
Cdd:TIGR01257 1052 HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RSIWDLLLkyrSGRTIIMSTHHMDEADLLG 1127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1820 QRVAVLRAGQVIASDSPQRLKSEHG-GYYAV-----------------TCFCG--------PA------QQAILSRSLNQ 1867
Cdd:TIGR01257 1128 DRIAIISQGRLYCSGTPLFLKNCFGtGFYLTlvrkmkniqsqrggcegTCSCTskgfstrcPArvdeitPEQVLDGDVNE 1207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1868 -------RLPGARDLQHYAHSLRFLVRVRSPGSLGDAPLLSELFAILCDvcVNVARFSLSRCRFETVFERILDSSESnGS 1940
Cdd:TIGR01257 1208 lmdlvyhHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLAD--LGLSSFGISDTPLEEIFLKVTEDADS-GS 1284
|
410
....*....|
gi 221500365 1941 NGVHKDQQQQ 1950
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 ... |
1634-1832 |
1.45e-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: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------QPGISYCPQ 1703
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgpGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPLLTTTECIRFYGRLRGIRD------LDQFLDRV-LDTYE-LRPykdvqvRNLSGGNRRKL----TVAVtccgcT 1771
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKaearerAEELLELVgLSGFEnAYP------HQLSGGMRQRValarALAV-----D 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1772 PTV-LMDEPTSDMDPVTRdmvyATIEQLLLA-----RRAVVLTSHSVSEIEHLCQRVAVL--RAGQVIA 1832
Cdd:cd03293 150 PDVlLLDEPFSALDALTR----EQLQEELLDiwretGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
850-1028 |
1.68e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.70 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTL--TAREHLQLY 927
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 928 AQIKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1007
Cdd:NF040873 82 RWARRGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|..
gi 221500365 1008 LI-ERLRQGRAVIFATHFMDEA 1028
Cdd:NF040873 161 LLaEEHARGATVVVVTHDLELV 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
824-1046 |
2.24e-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: 103.95 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 824 NYSFVKVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE- 902
Cdd:cd03267 5 NLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 ---------HQVGVCW-QDNILIPTLTAREHLQLYAQI-KIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGY 971
Cdd:cd03267 85 pwkrrkkflRRIGVVFgQKTQLWWDLPVIDSFYLLAAIyDLPPA------RFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 972 RRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1649-1846 |
2.29e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.32 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpgiSYCP----------------QSNPLDPLLT 1712
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL----GYVPfkrrkefarrigvvfgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKltvavtccgC--------TPTVL-MDEPTS 1781
Cdd:COG4586 113 AIDSFRLLKAIYRIpdAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMR---------CelaaallhRPKILfLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGY 1846
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1646-1829 |
3.08e-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: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpgisycpqsnplDPLLTTTECIRfygrlrg 1725
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------------GEDLTDLEDEL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1726 iRDLDQFLDRVLDTYELRPYKDVQ---VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL-LA 1801
Cdd:cd03229 72 -PPLRRRIGMVFQDFALFPHLTVLeniALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQaQL 150
|
170 180
....*....|....*....|....*...
gi 221500365 1802 RRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:cd03229 151 GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
851-1044 |
3.31e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.86 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR--QSSGKVLLAGE--------HQVGVCWQDNILIPTLTA 920
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRpldkrsfrKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 921 REHLQLYAQIKippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1000
Cdd:cd03213 100 RETLMFAAKLR----------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1001 ARKDIWQLIERLRQ-GRAVIFATH-FMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03213 146 SALQVMSLLRRLADtGRTIICSIHqPSSEIFELFDKLLLLSQGRVI 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
842-1046 |
6.03e-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: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL------LAGE------HQVGVC- 908
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEdvwelrKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 --WQDNILiPTLTAREHLQ--LYAQIKIPPGGSggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIAS 984
Cdd:COG1119 85 paLQLRFP-RDETVLDVVLsgFFDSIGLYREPT---DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
845-1046 |
7.40e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.53 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 910
Cdd:PRK13632 12 NVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkeirKKIGIIFQn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 -DNILIpTLTAREHLQL-YAQIKIPPggsGGVEEIRSEVAQTLQSLNFGKHESYpswQLSGGYRRRlcVAIAFIAS--PS 986
Cdd:PRK13632 92 pDNQFI-GATVEDDIAFgLENKKVPP---KKMKDIIDDLAKKVGMEDYLDKEPQ---NLSGGQKQR--VAIASVLAlnPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAkYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
842-1046 |
8.13e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.41 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ-----VGVCW 909
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmHKrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDniliPT----LTAREHLQLYAQIKIPPggsggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 985
Cdd:COG1137 85 QE----ASifrkLTVEDNILAVLELRKLS-----KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 986 SVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1636-1839 |
8.24e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-------------GISYCP 1702
Cdd:PRK10895 6 AKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECIRFYGRLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1779
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRaneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1780 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1634-1832 |
1.17e-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: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQ 1703
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPLLTTTECIRFYGRLRGIR--DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRA-VVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:cd03259 160 ALDAKLREELREELKELQRELGItTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1635-1841 |
1.23e-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: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------QP-------GISYC 1701
Cdd:COG0410 5 EVENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeditgLPphriarlGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIR--FYGRlRGIRDLDQFLDRVLDTY-ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVL 1775
Cdd:COG0410 84 PEGRRIFPSLTVEENLLlgAYAR-RDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGralMS----RPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1776 M-DEPTSDMDPVTRDMVYATIEQllLARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:COG0410 159 LlDEPSLGLAPLIVEEIFEIIRR--LNREgvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
842-1043 |
1.39e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.03 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------HQVGVCWQDN 912
Cdd:PRK09452 16 ELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQ--LYAQiKIPPggsggvEEIRSEVAQTL---QSLNFGKHEsyPSwQLSGGYRRRLCVAIAFIASPSV 987
Cdd:PRK09452 96 ALFPHMTVFENVAfgLRMQ-KTPA------AEITPRVMEALrmvQLEEFAQRK--PH-QLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERL-RQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALqRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1633-1878 |
2.28e-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: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFEQ------------P 1696
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 GISYCPQS--NPLDPlLTTTECIRFYGRLRGIrDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1771
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGL-SRAEARARVLELLEavgLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1772 PTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVT 1850
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVP 241
|
250 260
....*....|....*....|....*...
gi 221500365 1851 CFCGPAQQAILSRSLNQRLPGARDLQHY 1878
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLLEVRNLSKR 269
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
837-1044 |
2.70e-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: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 837 GKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEH-QVGVCWQDN-IL 914
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvKIGYFDQHQeEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAqikipPGGSggveeiRSEVAQTLQSLNFGKHESY-PSWQLSGGYRRRLCVAIAFIASPSVVILDEP 993
Cdd:COG0488 391 DPDKTVLDELRDGA-----PGGT------EQEVRGYLGRFLFSGDDAFkPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 994 CNGVDAKARKdiwQLIERLR--QGrAVIFATH---FMDEakyLSDSLVIMRNGRII 1044
Cdd:COG0488 460 TNHLDIETLE---ALEEALDdfPG-TVLLVSHdryFLDR---VATRILEFEDGGVR 508
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
868-1046 |
2.75e-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: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 868 VSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQ--VGVCWQDNILIPTLTAREHLqLYAQIKI 932
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflppHRrrIGYVFQEARLFPHLSVRGNL-LYGRKRA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 933 PPGGSggveeiRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRlcVAI--AFIASPSVVILDEPCNGVDAKARKDIWQLI 1009
Cdd:COG4148 106 PRAER------RISFDEVVELLGIGHLlDRRPA-TLSGGERQR--VAIgrALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 221500365 1010 ERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG4148 177 ERLRDELDipILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1641-1840 |
2.85e-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: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS---------------YCPQS 1704
Cdd:cd03261 6 LTKSFGGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaelyrlrrrmgMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NPLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:cd03261 86 GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1782 DMDPVTRDMVYATIeqLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLK 1840
Cdd:cd03261 166 GLDPIASGVIDDLI--RSLKKElglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1629-1844 |
4.07e-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: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QP 1696
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlsdldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 GISYCPQsNPLdpLLTTT--ECIRFYGR-------LRGIR--DLDQFLDRV---LDTyelrpykdvQV----RNLSGGNR 1758
Cdd:COG4988 412 QIAWVPQ-NPY--LFAGTirENLRLGRPdasdeelEAALEaaGLDEFVAALpdgLDT---------PLgeggRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1759 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQR 1838
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
....*.
gi 221500365 1839 LKSEHG 1844
Cdd:COG4988 558 LLAKNG 563
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1633-1843 |
4.16e-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: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNP-LDPL 1710
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD--GQDITGLSEKeLYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1711 ----------------LTTTECIRF----YGRL--RGIRDL-DQFLDRV--LDTYELRPykdvqvRNLSGGNRRKltVA- 1764
Cdd:COG1127 81 rrrigmlfqggalfdsLTVFENVAFplreHTDLseAEIRELvLEKLELVglPGAADKMP------SELSGGMRKR--VAl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1765 ----VTccgcTPTVLM-DEPTSDMDPVTRDMVYATIEQLllaRRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1835
Cdd:COG1127 153 aralAL----DPEILLyDEPTAGLDPITSAVIDELIREL---RDElgltSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*....
gi 221500365 1836 PQRL-KSEH 1843
Cdd:COG1127 226 PEELlASDD 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1649-1832 |
4.77e-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: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQsnplDPLLtttec 1716
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldpadlRRNIGYVPQ----DVTL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 irFYGRLRG-------------------IRDLDQFLDRVLDTYELrpykdvQV----RNLSGGNRRKLTVAVTCCGCTPT 1773
Cdd:cd03245 90 --FYGTLRDnitlgapladderilraaeLAGVTDFVNKHPNGLDL------QIgergRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1774 VLMDEPTSDMDPVTRDMVyatIEQL--LLARRAVVLTSHSVSEIEhLCQRVAVLRAGQVIA 1832
Cdd:cd03245 162 LLLDEPTSAMDMNSEERL---KERLrqLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVA 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
844-1054 |
4.78e-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: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 844 VNVSKLYGSKCAvsNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQ--VGVC 908
Cdd:TIGR02142 3 ARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppEKrrIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQDNILIPTLTAREHLqLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:TIGR02142 81 FQEARLFPHLSVRGNL-RYGMKRARP------SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1629-1844 |
5.77e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 107.13 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAVRAENLWLayRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-FEQP---------- 1696
Cdd:NF033858 262 DDEPAIEARGLTM--RFGDFtAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGQPvdagdiatrr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 GISYCPQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTV 1774
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNLELHARLFHLpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIH-KPEL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1775 L-MDEPTSDMDPVTRDMVYatieQLL--LARRAVV---LTSHSVSEIEhLCQRVAVLRAGQVIASDSPQRLKSEHG 1844
Cdd:NF033858 419 LiLDEPTSGVDPVARDMFW----RLLieLSREDGVtifISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
842-1055 |
8.56e-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: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCW 909
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaiaLGIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYAqiKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAI--AFIASPSV 987
Cdd:COG3845 87 QHFMLVPNLTVAENIVLGL--EPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR--VEIlkALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRII-----AQHSRDSLQRL 1055
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdtAETSEEELAEL 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1634-1844 |
1.12e-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: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPG-----------ISYC 1701
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIrdisrkslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQsnplDPLL---TTTECIRfYGRLRGIRD----------LDQFLDRVLDTYelrpykDVQVR----NLSGGNRRKLTVA 1764
Cdd:cd03254 83 LQ----DTFLfsgTIMENIR-LGRPNATDEevieaakeagAHDFIMKLPNGY------DTVLGenggNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1765 VTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHG 1844
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIII-AHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
842-1046 |
1.12e-22 |
|
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: 97.00 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVcwQDNI--LIPT 917
Cdd:cd03247 2 SINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALssLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLqlyaqikippggsggveeirseVAQTLQSlNFGKhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGV 997
Cdd:cd03247 80 LNQRPYL----------------------FDTTLRN-NLGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 998 DAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLsDSLVIMRNGRIIAQ 1046
Cdd:cd03247 130 DPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
845-1043 |
1.17e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQ----- 910
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlharDRKVGFVFQhyalf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 ------DNIL--IPTLTAREHLQLYAqikippggsggveeIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIA 980
Cdd:PRK10851 87 rhmtvfDNIAfgLTVLPRRERPNAAA--------------IKAKVTQLLEMVQLA-HlaDRYPA-QLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDI--W--QLIERLRqgRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELrrWlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
858-1041 |
1.18e-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: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhQVG-------VCWQDNILIPTLTAREHLQLYAQI 930
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-QITepgpdrmVVFQNYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 931 KIPPGGSGGVEEIrseVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDiwqLIE 1010
Cdd:TIGR01184 82 VLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN---LQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 221500365 1011 RLRQ-----GRAVIFATHFMDEAKYLSDSLVIMRNG 1041
Cdd:TIGR01184 156 ELMQiweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
841-1046 |
1.70e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.59 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 841 ASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKV-LLAGE-----HQVGVCWQdnI- 913
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDmadarHRRAVCPR--Ia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 ---------LIPTLTAREHLQ----LYAQikippggsgGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIA 980
Cdd:NF033858 80 ympqglgknLYPTLSVFENLDffgrLFGQ---------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRA---VIFATHFMDEAKYLsDSLVIMRNGRIIAQ 1046
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAERF-DWLVAMDAGRVLAT 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
855-1044 |
1.74e-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: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCW-QDNILIPTLTAREH 923
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkefaRRIGVVFgQRSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 924 LQLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:COG4586 117 FRLLKAIyRIPD------AEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1003 KDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG4586 191 EAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
845-1052 |
1.82e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.45 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ------------VGVCWQDN 912
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaagVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLyAQIkipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK11288 89 HLVPEMTVAENLYL-GQL---PHKGGIVnrRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH------SRDSL 1052
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFddmaqvDRDQL 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1646-1833 |
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 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP------------GISYCPQSNPLDPLLT 1712
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPvrfrsprdaqaaGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIrFYGRL---RGI-------RDLDQFLDRV-LDtyeLRPykDVQVRNLSGGNR------RKLTVavtccgcTPTVL 1775
Cdd:COG1129 96 VAENI-FLGREprrGGLidwramrRRARELLARLgLD---IDP--DTPVGDLSVAQQqlveiaRALSR-------DARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1776 -MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:COG1129 163 iLDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
852-1044 |
2.64e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.01 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 852 SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCWQ--DNILIPT 917
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdiRNKAGMVFQnpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVILDEPCN 995
Cdd:PRK13633 102 IVEEDVAFGPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAmrPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 996 GVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYlSDSLVIMRNGRII 1044
Cdd:PRK13633 174 MLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
845-1044 |
2.82e-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: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGS-KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCW 909
Cdd:cd03256 5 NLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHL--QLYAQIKIPPGGSGGVEEIRSEVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPS 986
Cdd:cd03256 85 QQFNLIERLSVLENVlsGRLGRRSTWRSLFGLFPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
829-1052 |
3.10e-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: 104.15 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 829 KVSRSQLDGKLgaSLVNVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---- 902
Cdd:COG2274 464 KLSLPRLKGDI--ELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrq 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 -------HQVGVCWQDNILIPTlTAREHLQLyaqikippgGSGGV--EEIRsEVAQTLQSLNF---------------GK 958
Cdd:COG2274 542 idpaslrRQIGVVLQDVFLFSG-TIRENITL---------GDPDAtdEEII-EAARLAGLHDFiealpmgydtvvgegGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 959 hesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKyLSDSLVIM 1038
Cdd:COG2274 611 -------NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIR-LADRIIVL 682
|
250
....*....|....
gi 221500365 1039 RNGRIIAQHSRDSL 1052
Cdd:COG2274 683 DKGRIVEDGTHEEL 696
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
855-1028 |
5.19e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.05 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGVCWQDNILIPTLTAREHL 924
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdagdiatrRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYAQI-KIPPggsggvEEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:NF033858 361 ELHARLfHLPA------AEIAARVAEMLERFDLADVaDALPD-SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180
....*....|....*....|....*...
gi 221500365 1003 KDIWQLIERL-RQGRAVIF-ATHFMDEA 1028
Cdd:NF033858 434 DMFWRLLIELsREDGVTIFiSTHFMNEA 461
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1634-1836 |
5.98e-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: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF------EQPG------ISYC 1701
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedirEQDPvelrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIRF------YGRLRGIRDLDQFLDRV-LDTYElrpYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1774
Cdd:cd03295 81 IQQIGLFPHMTVEENIALvpkllkWPKEKIRERADELLALVgLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1775 LMDEPTSDMDPVTRDMV---YATIEQLLlaRRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1836
Cdd:cd03295 158 LMDEPFGALDPITRDQLqeeFKRLQQEL--GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
843-1054 |
7.29e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 7.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH------QVGVCWQDNILIP 916
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 917 TLTAREHLQLYAQIkippggsGGVE-EIRSEVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:PRK11248 84 WRNVQDNVAFGLQL-------AGVEkMQRLEIAhQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 995 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMR--NGRIIAQHSRDSLQR 1054
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLNFARR 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
851-1046 |
8.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ---DNILIP 916
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrKFVGLVFQnpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 917 TLTarehlqlyAQIKIPPGGSGGVEE-IRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:PRK13652 95 TVE--------QDIAFGPINLGLDEEtVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 996 GVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
829-1045 |
8.77e-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: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 829 KVSRSQLDGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvGVC 908
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WqdniLI-------PTLTAREHLQLYAQIKippGGSGgvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF 981
Cdd:cd03220 87 S----LLglgggfnPELTGRENIYLNGRLL---GLSR--KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
845-1052 |
1.06e-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: 95.76 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDN 912
Cdd:cd03254 7 NVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTlTAREHLQLyaqikippGGSGGVEEIRSEVAQTLQSLNFGKH-----ESYPSWQ---LSGGYRRRLCVAIAFIAS 984
Cdd:cd03254 87 FLFSG-TIMENIRL--------GRPNATDEEVIEAAKEAGAHDFIMKlpngyDTVLGENggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
842-1046 |
1.72e-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: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------H 903
Cdd:COG1135 3 ELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalserelraarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 904 QVGVCWQ-----------DNILIPtltarehLQLyaqIKIPPggsggvEEIRSEVAQTLQslnF----GKHESYPSwQLS 968
Cdd:COG1135 83 KIGMIFQhfnllssrtvaENVALP-------LEI---AGVPK------AEIRKRVAELLE---LvglsDKADAYPS-QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 969 GGYRRRlcVAIA--FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG1135 143 GGQKQR--VGIAraLANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
..
gi 221500365 1045 AQ 1046
Cdd:COG1135 221 EQ 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1634-1830 |
1.80e-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: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG------------- 1697
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD--Gtdisklsekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1698 -----ISYCPQSNPLDPLLTTTECIRFYGRLRGIRDLD------QFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVT 1766
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKErreraeELLERV----GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1767 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL-LARRAVVLTSHSVsEIEHLCQRVAVLRAGQV 1830
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1634-1831 |
2.13e-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: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfeQPG----ISYCPQSN-PLD 1708
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---KLGetvkIGYFDQHQeELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1709 PLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYElrpykDVQ--VRNLSGGNRR-----KLTVAvtccgcTPTVL-MDEPT 1780
Cdd:COG0488 392 PDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGD-----DAFkpVGVLSGGEKArlalaKLLLS------PPNVLlLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1781 SDMDPVTRDMvyatIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:COG0488 461 NHLDIETLEA----LEEALDDfPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
845-1027 |
2.86e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTLTAREHL 924
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 ---------------QLYAQIKIPPGGSGGVEE------------IRSEVAQTLQSLNFGKHEsypsWQ-----LSGGYR 972
Cdd:COG0488 83 ldgdaelraleaeleELEAKLAEPDEDLERLAElqeefealggweAEARAEEILSGLGFPEED----LDrpvseLSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 973 RRLCVAIAFIASPSVVILDEPCNGVDAKARkdIWqLIERLRQGR-AVIFATH---FMDE 1027
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESI--EW-LEEFLKNYPgTVLVVSHdryFLDR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
859-1046 |
5.73e-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: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 859 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNILIPTLTAREHLQLyaq 929
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappaDRPVSMLFQENNLFAHLTVEQNVGL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 930 ikippGGSGGV---EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIW 1006
Cdd:cd03298 94 -----GLSPGLkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1007 QLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:cd03298 169 DLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
842-1046 |
5.75e-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: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 910
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpsrelaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTARE--------HlqlyaqikippggSGGV--EEIRSEVAQTLQSLNFG--KHEsYPSwQLSGGYRRRLCVA 978
Cdd:COG4604 83 ENHINSRLTVRElvafgrfpY-------------SKGRltAEDREIIDEAIAYLDLEdlADR-YLD-ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 979 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVI-------FATHFmdeakylSDSLVIMRNGRIIAQ 1046
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLadELGKTVVivlhdinFASCY-------ADHIVAMKDGRVVAQ 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
843-1048 |
7.40e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEHQVGVCWQDNILIPT 917
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHL-------QLYAQ-----IKIPPGGSGG-VEEIRSEVAQTLQSLNFGKHESYPS-WQLSGGYRRRLCVAIAFIA 983
Cdd:PRK13645 88 LRKEIGLvfqfpeyQLFQEtiekdIAFGPVNLGEnKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 984 SPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1048
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 ... |
842-1027 |
1.19e-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: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLlagehqvgvcWQDNILIPTLTar 921
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT----------WGSTVKIGYFE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 ehlqlyaqikippggsggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:cd03221 70 --------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190
....*....|....*....|....*....|
gi 221500365 1002 RKdiwQLIERLRQ-GRAVIFATH---FMDE 1027
Cdd:cd03221 106 IE---ALEEALKEyPGTVILVSHdryFLDQ 132
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1634-1839 |
1.92e-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: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG-----QLQPDVGQIYFEQPGIsYCPQSNPL- 1707
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDI-YDLDVDVLe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 ------------DPL-LTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRPY-KD-VQVRNLSGGNRRKL----TVAV 1765
Cdd:cd03260 79 lrrrvgmvfqkpNPFpGSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDEvKDrLHALGLSGGQQQRLclarALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1766 tccgcTPTV-LMDEPTSDMDPVTRdmvyATIEQLL--LARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:cd03260 159 -----EPEVlLLDEPTSALDPIST----AKIEELIaeLKKEyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
845-1046 |
2.52e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTARE-- 922
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP-----------ISMLSSRQla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 -HLQLYAQIKIPPGGSgGVEEI-------------------RSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 982
Cdd:PRK11231 76 rRLALLPQHHLTPEGI-TVRELvaygrspwlslwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
843-1054 |
2.57e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQVGVC--WQDNI 913
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiQQRDICmvFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPtltareHLQLYAQIkippgGSG----GV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSV 987
Cdd:PRK11432 89 LFP------HMSLGENV-----GYGlkmlGVpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1660-1834 |
3.15e-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: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1660 GECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------------EQPGISYCPQSNPLDPLLTTTECIRF-YGR 1722
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkinlppQQRKIGLVFQQYALFPHLNVRENLAFgLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1723 LRGIRDLDQFlDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR 1802
Cdd:cd03297 103 KRNREDRISV-DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 221500365 1803 RAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASD 1834
Cdd:cd03297 182 NIPVIfVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1646-1837 |
3.23e-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: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTE 1715
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditnlppEKRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFYGRLRgIRDLDQFLDRVLDTYEL---RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVy 1792
Cdd:cd03299 91 NIAYGLKKR-KVDKKEIERKVLEIAEMlgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1793 atIEQLLLARRAVVLT----SHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:cd03299 169 --REELKKIRKEFGVTvlhvTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
846-1047 |
3.33e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 846 VSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG--------------EHQVGVCWQ 910
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTarehlqLYAQIKIP---PGGSGgvEEIRSEVAQTLQSLN-FGKHESYPSwQLSGGYRRRLCVAIAFIASPS 986
Cdd:PRK10908 87 DHHLLMDRT------VYDNVAIPliiAGASG--DDIRRRVSAALDKVGlLDKAKNFPI-QLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQH 1047
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
853-1046 |
4.12e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 853 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-------------QVGVCWQdnilIPtlt 919
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsdirkKVGLVFQ----YP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 arEHlQL-----YAQIKIPPGGSG-GVEEIRSEVAQTLQ--SLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVI 989
Cdd:PRK13637 93 --EY-QLfeetiEKDIAFGPINLGlSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRR--VAIAGVVAmePKILI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1632-1837 |
5.00e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1632 EAVRAENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISY--------- 1700
Cdd:PRK13548 1 AMLEARNL--SVRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrLNGRPLADWspaelarrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1701 --CPQSNPLDPLLTTTECIRFyGRL---RGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVA-----VTCCGC 1770
Cdd:PRK13548 79 avLPQHSSLSFPFTVEEVVAM-GRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqLWEPDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1771 TPTVLM-DEPTSDMDPvtrdmvYATIEQLLLARR-------AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:PRK13548 158 PPRWLLlDEPTSALDL------AHQHHVLRLARQlaherglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1649-1833 |
7.35e-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: 88.91 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQpgisycpqsnplDPLLTTTECIRFYgrlrgIRD 1728
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG------------VPVSDLEKALSSL-----ISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1729 LDQfldrvldtyelRPYK-DVQVRN-----LSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRdmvYATIEQLL--L 1800
Cdd:cd03247 80 LNQ-----------RPYLfDTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE---RQLLSLIFevL 145
|
170 180 190
....*....|....*....|....*....|...
gi 221500365 1801 ARRAVVLTSHSVSEIEHLcQRVAVLRAGQVIAS 1833
Cdd:cd03247 146 KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
855-1046 |
8.46e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQ---DNILIPTL 918
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrKTVGIVFQnpdDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 ---TAREHLQLyaqiKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIAFIAS--PSVVILDEP 993
Cdd:PRK13639 97 eedVAFGPLNL----GLSK------EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR--VAIAGILAmkPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 994 CNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1633-1839 |
1.08e-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: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCP 1702
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglppEKRNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNR-RkltVA-----VtccgCTPTV 1774
Cdd:COG3842 84 QDYALFPHLTVAENVAFGLRMRGVpkAEIRARVAELLELVGLEGLADRYPHQLSGGQQqR---VAlaralA----PEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1775 -LMDEPTSDMDPVTRDMVYATIEQLLlaRRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:COG3842 157 lLLDEPLSALDAKLREEMREELRRLQ--RELgitFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
855-1044 |
1.39e-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: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE---------------HQVGVCWQD--NIL 914
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEdllklsekelrkirgREIQMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNFGKHE----SYPSwQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:COG0444 100 NPVMTVGD--QIAEPLRIHGGLSK--AEARERAIELLERVGLPDPErrldRYPH-ELSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
837-1052 |
1.67e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 837 GKLGASLVNVSKLY---GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR------QSSGKVLLAGE----- 902
Cdd:PRK14246 4 GKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 ------HQVGVCWQDNILIPtltareHLQLYAQIKIPPGGSGGVE--EIRSEVAQTLQSLNFGKhESY-----PSWQLSG 969
Cdd:PRK14246 84 daiklrKEVGMVFQQPNPFP------HLSIYDNIAYPLKSHGIKEkrEIKKIVEECLRKVGLWK-EVYdrlnsPASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 970 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSR 1049
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
...
gi 221500365 1050 DSL 1052
Cdd:PRK14246 237 NEI 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
858-1064 |
1.77e-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: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQVGVCWQDNI--LIPTLTAR 921
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrkqrrafrRDVQLVFQDSPsaVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 ----EHLQLYAQIKIPPGGSGGVE-----EIRSEVAQtlqslnfgkheSYPSwQLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:TIGR02769 109 qiigEPLRHLTSLDESEQKARIAElldmvGLRSEDAD-----------KLPR-QLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 993 PCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQhsRDSLQRLCTSNYSIRL 1064
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE--CDVAQLLSFKHPAGRN 248
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
855-1046 |
2.30e-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: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDNILIPTlTAREH 923
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 924 LQLyaqikippgGSGGVEEIRSEVAQTLQSLN--FGKHESYPSWQ-------LSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:cd03245 98 ITL---------GAPLADDERILRAAELAGVTdfVNKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 995 NGVDAKARKdiwQLIERLRQ---GRAVIFATH---FMDeakyLSDSLVIMRNGRIIAQ 1046
Cdd:cd03245 169 SAMDMNSEE---RLKERLRQllgDKTLIIITHrpsLLD----LVDRIIVMDSGRIVAD 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
843-1054 |
2.43e-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: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAvsNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ--VGVCWQDNI 913
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppAErpVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLyaqiKIPPGGSGGVEEiRSEVAQTLQSLNFGKHESY-PSwQLSGGYRRRlcVAIA--FIASPSVVIL 990
Cdd:COG3840 82 LFPHLTVAQNIGL----GLRPGLKLTAEQ-RAQVEQALERVGLAGLLDRlPG-QLSGGQRQR--VALArcLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 991 DEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
842-1043 |
4.51e-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: 87.59 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVC 908
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkninelrQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQDNILIPTLTAREHLQLyAQIKIPpggsgGVEEIRSEvAQTLQSLN----FGKHESYPSwQLSGGYRRRLCVAIAFIAS 984
Cdd:cd03262 82 FQQFNLFPHLTVLENITL-APIKVK-----GMSKAEAE-ERALELLEkvglADKADAYPA-QLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
851-1023 |
4.74e-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: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH--QVGVCWQDNILI--------PTLTA 920
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaEQRDEPHENILYlghlpglkPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 921 REHLQLYAQIkippggsGGVEeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1000
Cdd:TIGR01189 91 LENLHFWAAI-------HGGA--QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 221500365 1001 ARKDIWQLIE-RLRQGRAVIFATH 1023
Cdd:TIGR01189 162 GVALLAGLLRaHLARGGIVLLTTH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
858-1046 |
4.91e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.33 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLTARE 922
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaelrnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 HLQLYAQI-KIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:PRK11629 107 NVAMPLLIgKKKPA------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1002 RKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLViMRNGRIIAQ 1046
Cdd:PRK11629 181 ADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1649-1839 |
6.68e-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: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------------QSNPLDPLLT 1712
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrelrrkkismvfQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR-D 1789
Cdd:cd03294 119 VLENVAFGLEVQGVprAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRrE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1790 MvyatiEQLLLA-----RRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:cd03294 199 M-----QDELLRlqaelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1633-1848 |
7.06e-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: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpgI 1698
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleslrRQ--I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1699 SYCPQsnplDP-LLTTT--ECIRfYGRLrGIRD-----------LDQFLDRV---LDTYelrpykdVQVR--NLSGGNRR 1759
Cdd:COG1132 417 GVVPQ----DTfLFSGTirENIR-YGRP-DATDeeveeaakaaqAHEFIEALpdgYDTV-------VGERgvNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1760 KLTVAvtccgcTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRL 1839
Cdd:COG1132 484 RIAIArallkdPPILILDEATSALDTETEALIQEALER-LMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
....*....
gi 221500365 1840 kSEHGGYYA 1848
Cdd:COG1132 562 -LARGGLYA 569
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
855-1043 |
7.32e-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: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdniLIPTLTAREHLQLyaqikipp 934
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK-----------PVTRRSPRDAIRA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 935 gGSGGVEEIRSEVAqTLQSLNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR- 1013
Cdd:cd03215 76 -GIAYVPEDRKREG-LVLDLSVAENIALSS-LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAd 152
|
170 180 190
....*....|....*....|....*....|
gi 221500365 1014 QGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:cd03215 153 AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
855-1052 |
8.19e-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: 87.93 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQDNILIpTLTAREH 923
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 924 LQLyaqikIPPGGSggVEEIrSEVAQTLQSLNFGKH--ESYPSW------QLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:cd03252 96 IAL-----ADPGMS--MERV-IEAAKLAGAHDFISElpEGYDTIvgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 996 GVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
845-1043 |
8.44e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGEhqvgvcwqdnilIPTLTAREHL 924
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGT------------APLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYAQIK--------IPPGGSGGVEEIRSEVAQTLQSLnfGKHESYPSW--QLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:PRK11247 84 RLMFQDArllpwkkvIDNVGLGLKGQWRDAALQALAAV--GLADRANEWpaALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 995 NGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK11247 162 GALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
840-1042 |
9.01e-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: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 840 GASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehQVGVC----W------ 909
Cdd:cd03250 5 DASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVsqepWiqngti 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILiptLTAREHLQLYAQ----------IKIPPGGsggveeIRSEVAQtlQSLNfgkhesypswqLSGGYRRRLCVAI 979
Cdd:cd03250 83 RENIL---FGKPFDEERYEKvikacalepdLEILPDG------DLTEIGE--KGIN-----------LSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQ--LIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGR 1042
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
855-1048 |
1.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTAREHL---------- 924
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-----------DDITITHKTKDKYIrpvrkrigmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 ------QLYA-----QIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK13646 91 fqfpesQLFEdtverEIIFGPKNFKmNLDEVKNYAHRLLMDLGFSRDvmSQSP-FQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDE-AKYlSDSLVIMRNGRIIAQHS 1048
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEvARY-ADEVIVMKEGSIVSQTS 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
813-1046 |
1.02e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 813 IGLAYQRYKKNNYSFVKvsrsqldgklgaSLVNVSKL-YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR 891
Cdd:COG1134 10 VSKSYRLYHEPSRSLKE------------LLLRRRRTrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 892 QSSGKVLLAG------EHQVGvcwqdniLIPTLTAREHLQLYAQIKippGGSggveeiRSEVAQTLQS-LNF---GKHES 961
Cdd:COG1134 78 PTSGRVEVNGrvsallELGAG-------FHPELTGRENIYLNGRLL---GLS------RKEIDEKFDEiVEFaelGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 962 YPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA----KARKdiwQLIERLRQGRAVIFATHFMDEAKYLSDSLVI 1037
Cdd:COG1134 142 QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLA---RIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
....*....
gi 221500365 1038 MRNGRIIAQ 1046
Cdd:COG1134 219 LEKGRLVMD 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
850-1046 |
1.06e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQDNilip 916
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllalrQQVATVFQDP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 917 tltarEHLQLYAQIKIPPGGS---GGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:PRK13638 87 -----EQQIFYTDIDSDIAFSlrnLGVpeAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 992 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
841-1046 |
1.29e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 841 ASLVNVSKL---YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQV---GV 907
Cdd:PRK11300 3 QPLLSVSGLmmrFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpgHQIarmGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 908 C--WQDNILIPTLTAREHLqLYAQ------------IKIPpGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRR 973
Cdd:PRK11300 83 VrtFQHVRLFREMTVIENL-LVAQhqqlktglfsglLKTP-AFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 974 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
855-1046 |
1.37e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQD-NILIPTLTARE 922
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekwvrSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 hlqlyaQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKA 1001
Cdd:PRK13647 100 ------DVAFGPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1002 RKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13647 174 QETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
842-1047 |
1.52e-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: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAV----SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------- 902
Cdd:COG4181 10 ELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedararlra 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 HQVGVCWQDNILIPTLTAREHLQLYAQIKippggsgGVEEIRSEVAQTLQSLNFGKHES-YPSwQLSGGYRRRlcVAIA- 980
Cdd:COG4181 90 RHVGFVFQSFQLLPTLTALENVMLPLELA-------GRRDARARARALLERVGLGHRLDhYPA-QLSGGEQQR--VALAr 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 981 -FIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHfmDEAkyL---SDSLVIMRNGRIIAQH 1047
Cdd:COG4181 160 aFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH--DPA--LaarCDRVLRLRAGRLVEDT 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
857-1023 |
1.66e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.01 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 857 SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------------HQVGVcwqdnilIPTLT 919
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdllylgHQPGI-------KTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLYAQIkippGGSGGVEEIrsevAQTLQSLNFGKHESYPSWQLSGGYRRRlcVAIA--FIASPSVVILDEPCNGV 997
Cdd:PRK13538 91 ALENLRFYQRL----HGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 221500365 998 DAKARKDIWQLIER-LRQGRAVIFATH 1023
Cdd:PRK13538 161 DKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
845-1044 |
2.34e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDNILI 915
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTAREHLQL-YAQIKIPPGgsggveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:PRK11607 104 PHMTVEQNIAFgLKQDKLPKA------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 995 NGVDAKARkDIWQL-----IERLrqGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK11607 178 GALDKKLR-DRMQLevvdiLERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
842-1023 |
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 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT--LT 919
Cdd:PRK09544 6 SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTlpLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLYAQIKippggsggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 999
Cdd:PRK09544 86 VNRFLRLRPGTK------------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180
....*....|....*....|....*.
gi 221500365 1000 KARKDIWQLIERLRQ--GRAVIFATH 1023
Cdd:PRK09544 154 NGQVALYDLIDQLRRelDCAVLMVSH 179
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1635-1838 |
2.66e-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: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYC----------- 1701
Cdd:COG4559 3 EAENL--SVRLGGRTLlDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrLNGRPLAAWSpwelarrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPLDPLLTTTECIRFyGRLRGIR---DLDQFLDRVLDTYELRPYKDVQVRNLSGGNR------RKLT-VAVTCCGCT 1771
Cdd:COG4559 81 PQHSSLAFPFTVEEVVAL-GRAPHGSsaaQDRQIVREALALVGLAHLAGRSYQTLSGGEQqrvqlaRVLAqLWEPVDGGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1772 PTVLMDEPTSDMDP--------VTRDmvyatieqllLARR--AVV-------LTShsvseieHLCQRVAVLRAGQVIASD 1834
Cdd:COG4559 160 RWLFLDEPTSALDLahqhavlrLARQ----------LARRggGVVavlhdlnLAA-------QYADRILLLHQGRLVAQG 222
|
....
gi 221500365 1835 SPQR 1838
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) ... |
1656-1824 |
2.99e-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: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1656 SVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSnpLDPLLTTTECIRFYGRLRGIRDLDQFLDR 1735
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY--IKADYEGTVRDLLSSITKDFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1736 VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLL-ARRAVVLTSHSVSE 1814
Cdd:cd03237 99 IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEnNEKTAFVVEHDIIM 178
|
170
....*....|
gi 221500365 1815 IEHLCQRVAV 1824
Cdd:cd03237 179 IDYLADRLIV 188
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1634-1830 |
3.77e-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: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------Q 1703
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdiamvfQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVpkDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1782 DMDPVTRDMVYATIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
855-1046 |
4.45e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------------HQVGVCWQ--DNILIPTlt 919
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESVGMVFQdpDNQLFSA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 arehlQLYAQIKIPPGGSGGVE-EIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 998
Cdd:PRK13636 99 -----SVYQDVSFGAVNLKLPEdEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 999 AKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1634-1831 |
5.18e-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: 87.42 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGH---YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFE------------- 1694
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDgedllklsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1695 ---QPGISYCPQsNP---LDPLLTT----TECIRFYGRLRGiRDLDQFLDRVLDTYELRPYKDV------QvrnLSGGNR 1758
Cdd:COG0444 82 kirGREIQMIFQ-DPmtsLNPVMTVgdqiAEPLRIHGGLSK-AEARERAIELLERVGLPDPERRldryphE---LSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1759 RKLTVAVTCCgCTPTVL-MDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:COG0444 157 QRVMIARALA-LEPKLLiADEPTTALD-VT---IQAQILNLLkdLQRElglAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1634-1834 |
6.35e-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: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGE-CFgLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-----------EQP----- 1696
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkrrEIPylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 -GISYcpQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTccgc 1770
Cdd:COG2884 81 iGVVF--QDFRLLPDRTVYENVALPLRVTGKsrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAralVN---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1771 TPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASD 1834
Cdd:COG2884 155 RPELLLaDEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
842-1038 |
7.05e-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: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE---------HQVGVCW 909
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRrltalpaeqRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLqLYAqikIPPGGSGgvEEIRSEVAQTLQSLNF-GKHESYPSwQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:COG4136 83 QDDLLFPHLSVGENL-AFA---LPPTIGR--AQRRARVEQALEEAGLaGFADRDPA-TLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 989 ILDEPCNGVDAKARKDIWQLI-ERLRQ-GRAVIFATHfmDEAKYLSDSLVIM 1038
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVfEQIRQrGIPALLVTH--DEEDAPAAGRVLD 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1649-1833 |
8.73e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYcpqsNPLDPLLTTTECIR---------- 1718
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NINY----NKLDHKLAAQLGIGiiyqelsvid 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 --------FYGRLR-----GIRDLD-----QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1780
Cdd:PRK09700 94 eltvlenlYIGRHLtkkvcGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1781 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
857-1023 |
9.14e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 857 SNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--HQVGVCWQDNILI--------PTLTAREHLQL 926
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLYlghapgikTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 YAQIkippGGSGGVEEirsevaqTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKArkdIW 1006
Cdd:cd03231 97 WHAD----HSDEQVEE-------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG---VA 162
|
170 180
....*....|....*....|.
gi 221500365 1007 QLIERLR----QGRAVIFATH 1023
Cdd:cd03231 163 RFAEAMAghcaRGGMVVLTTH 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1636-1831 |
9.74e-18 |
|
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: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPG--ISYCPQSNPLDPLLT 1712
Cdd:COG0488 1 LENLSKSF--GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGlrIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIrfYGRLRGIRDLDQFLDRV-----------------------LDTYELRP--------------YKDVQVRNLSG 1755
Cdd:COG0488 78 VLDTV--LDGDAELRALEAELEELeaklaepdedlerlaelqeefeaLGGWEAEAraeeilsglgfpeeDLDRPVSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1756 GNRRKLTVA---VtccgCTPTVLM-DEPTSDMDpvtrdmVYATI--EQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAG 1828
Cdd:COG0488 156 GWRRRVALAralL----SEPDLLLlDEPTNHLD------LESIEwlEEFLKNYPgTVLVVSHDRYFLDRVATRILELDRG 225
|
...
gi 221500365 1829 QVI 1831
Cdd:COG0488 226 KLT 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
845-1023 |
1.10e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGvcwQDNI 913
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaeacHYLG---HRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREHLQLYAQIKippGGSggveeiRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEP 993
Cdd:PRK13539 84 MKPALTVAENLEFWAAFL---GGE------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 994 CNGVDAKARKDIWQLI-ERLRQGRAVIFATH 1023
Cdd:PRK13539 155 TAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1633-1825 |
1.11e-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: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY------------FEQPGISY 1700
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadadSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1701 CPQSnpldPLL---TTTECIRFY----------------GRLRGIRDLDQFLDRVLDTyelrpykdvQVRNLSGGNRRKL 1761
Cdd:TIGR02857 401 VPQH----PFLfagTIAENIRLArpdasdaeirealeraGLDEFVAALPQGLDTPIGE---------GGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1762 TVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVsEIEHLCQRVAVL 1825
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
842-1051 |
1.14e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------------Q 904
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkairelrrN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQDNILIPTLTAREHLqLYAQIKIPpggsgGV--EEIRSEVAQTLQSLNFGKH-ESYPsWQLSGGYRRRLCVAIAF 981
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNL-IEAPCRVL-----GLskDQALARAEKLLERLRLKPYaDRFP-LHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDS 1051
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
852-1046 |
1.19e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 852 SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVCWQ--DNILIPTl 918
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvRRQVGMVFQnpDNQFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 TAREHLQL-YAQIKIPPggsggvEEIRSEVAQTLQSLN---FGKHEsyPSwQLSGGYRRRlcVAIAFI--ASPSVVILDE 992
Cdd:PRK13635 98 TVQDDVAFgLENIGVPR------EEMVERVDQALRQVGmedFLNRE--PH-RLSGGQKQR--VAIAGVlaLQPDIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 993 PCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQ 1046
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
842-1038 |
1.49e-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: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGV---CWQDNIL--- 914
Cdd:TIGR02857 323 EFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadSWRDQIAwvp 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 -IPTLTA---REHLQLYAqikipPGGSGgvEEIRS--------EVAQTL-QSLNF--GKHESypswQLSGGYRRRLCVAI 979
Cdd:TIGR02857 403 qHPFLFAgtiAENIRLAR-----PDASD--AEIREaleragldEFVAALpQGLDTpiGEGGA----GLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHfMDEAKYLSDSLVIM 1038
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH-RLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
842-1052 |
1.52e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLY--GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVC 908
Cdd:PRK11160 340 TLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrQAISVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQdNILIPTLTAREHLQLYAqikipPGGSggvEEIRSEVaqtLQSLNFGKH----ESYPSW------QLSGGYRRRLCVA 978
Cdd:PRK11160 420 SQ-RVHLFSATLRDNLLLAA-----PNAS---DEALIEV---LQQVGLEKLleddKGLNAWlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 979 IAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltGLEQF----DRICVMDNGQIIEQGTHQEL 560
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
855-1045 |
1.64e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------------EHQVGVCWQdnilIPTLT 919
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLyAQIKIPPGGSG-GVEEIRSEVAQTLQSLNFGKH--ESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:PRK13643 97 LFEETVL-KDVAFGPQNFGiPKEKAEKIAAEKLEMVGLADEfwEKSP-FELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 997 VDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
850-1044 |
1.68e-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: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKL------LTGQIRqSSGKVLLAGE-------------HQVGVCWQ 910
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndLIPGAR-VEGEILLDGEdiydpdvdvvelrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 ----------DNILIPtltAREHlqlyaQIKippgGSGGVEEI--RS--------EVAQTLQSLNFGkhesypswqLSGG 970
Cdd:COG1117 100 kpnpfpksiyDNVAYG---LRLH-----GIK----SKSELDEIveESlrkaalwdEVKDRLKKSALG---------LSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 971 YRRRLCVAIAfIA-SPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG1117 159 QQQRLCIARA-LAvEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
858-1055 |
2.64e-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: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTG--QIRQSSGKVLLAGEhqvgvcwqdNI--LIPTLTAREHLQLYAQ--IK 931
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE---------DItdLPPEERARLGIFLAFQypPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 IPpggsgGVEeirseVAQTLQSLNFGkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIER 1011
Cdd:cd03217 89 IP-----GVK-----NADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1012 LR-QGRAVIFATHFMDEAKYLSDSLV-IMRNGRIIAQHSRDSLQRL 1055
Cdd:cd03217 150 LReEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGDKELALEI 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1649-1833 |
3.32e-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: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP------------GISYCPQSNPLDPLLTTTE 1715
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPvrirsprdaialGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CI------RFYGRLRgIRDLDQFLDRVLDTYELR--PykDVQVRNLSGGNR----------RKltvavtccgctPTVL-M 1776
Cdd:COG3845 100 NIvlglepTKGGRLD-RKAARARIRELSERYGLDvdP--DAKVEDLSVGEQqrveilkalyRG-----------ARILiL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1777 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1633-1833 |
3.37e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.78 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY---------FEQPGISYCPQ 1703
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqaLQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLD---PLLttTECIRFYGR------LRGIRDLD-QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPT 1773
Cdd:PRK15056 86 SEEVDwsfPVL--VEDVVMMGRyghmgwLRRAKKRDrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1774 VLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQrVAVLRAGQVIAS 1833
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLAS 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1634-1842 |
4.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYC-----PQSNPLD 1708
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS--GIDTGdfsklQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1709 PLLTTTECIRFYGR--------------LRGIrDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1774
Cdd:PRK13644 80 GIVFQNPETQFVGRtveedlafgpenlcLPPI-EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1775 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIeHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
845-1048 |
4.88e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYG-----SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH---------------Q 904
Cdd:PRK13641 7 NVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlkklrkK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQdnilIPTLTAREHLQLyAQIKIPPGGSGGVE-EIRSEVAQTLQSLNFGKHESYPS-WQLSGGYRRRLCVAIAFI 982
Cdd:PRK13641 87 VSLVFQ----FPEAQLFENTVL-KDVEFGPKNFGFSEdEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQL-IERLRQGRAVIFATHFMDE-AKYLSDSLViMRNGRIIAQHS 1048
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDvAEYADDVLV-LEHGKLIKHAS 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
840-1065 |
5.00e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 840 GASLVNVSKLY---GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH------------- 903
Cdd:PRK11831 4 VANLVDMRGVSftrGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 904 -------QVGVCWQD-----NILIPTltaREHLQLYAQIkippggsggveeIRSEVAQTLQSLNF-GKHESYPSwQLSGG 970
Cdd:PRK11831 84 krmsmlfQSGALFTDmnvfdNVAYPL---REHTQLPAPL------------LHSTVMMKLEAVGLrGAAKLMPS-ELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 971 YRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1048
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|....*..
gi 221500365 1049 RDSLQrlctSNYSIRLR 1065
Cdd:PRK11831 228 AQALQ----ANPDPRVR 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1640-1831 |
5.63e-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: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1640 WLAYRRghyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD---VGQIYFE---------QPGISYCPQSNPL 1707
Cdd:cd03234 16 WNKYAR---ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNgqprkpdqfQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYE------LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVllrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRAVVLTSHS-VSEIEHLCQRVAVLRAGQVI 1831
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1641-1843 |
7.31e-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: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAVRnVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-----------EQPgISYCPQSNPLDP 1709
Cdd:COG3840 7 LTYRYGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalppaERP-VSMLFQENNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIRFygrlrGIRD-----------LDQFLDRV-LDTYELR-PykdvqvRNLSGGNRRKltVAVTCCGC--TPTV 1774
Cdd:COG3840 85 HLTVAQNIGL-----GLRPglkltaeqraqVEQALERVgLAGLLDRlP------GQLSGGQRQR--VALARCLVrkRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1775 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
871-1046 |
7.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEHQ----------------VGVCWQdnilIPtltarEHlQLYAQ----- 929
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkknkklkplrkkVGIVFQ----FP-----EH-QLFEEtvekd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 930 IKIPPGGSGGVEEIRSEVAQTLQSLnFGKHESYPS---WQLSGGYRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKD 1004
Cdd:PRK13634 107 ICFGPMNFGVSEEDAKQKAREMIEL-VGLPEELLArspFELSGGQMRR--VAIAGVLAmePEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1005 IWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13634 184 MMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
842-1046 |
8.08e-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: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------------Q 904
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpsekairllrqK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQDNILIPTLTAREHLqLYAQIKIPpGGSGgvEEIRSEVAQTLQSLNFG-KHESYPSwQLSGGYRRRLCVAIAFIA 983
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENL-IEAPCKVL-GLSK--EQAREKAMKLLARLRLTdKADRFPL-HLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 984 SPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
865-1023 |
8.14e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLTAREHLQLYAQ 929
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklraKHVGFVFQSFMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 930 IKippGGSGGveEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI 1009
Cdd:PRK10584 115 LR---GESSR--QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170
....*....|....*.
gi 221500365 1010 ERL--RQGRAVIFATH 1023
Cdd:PRK10584 190 FSLnrEHGTTLILVTH 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1636-1811 |
1.05e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLwLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-----------YFEQpgISYCPQS 1704
Cdd:PRK13539 5 GEDL-ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiddpdVAEA--CHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NPLDPLLTTTECIRFYGRLRGIRDLDqfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1784
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 1785 PVTRDMvyatIEQLLLARRA----VVLTSHS 1811
Cdd:PRK13539 160 AAAVAL----FAELIRAHLAqggiVIAATHI 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1634-1836 |
1.19e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRG----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLDP 1709
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID--GVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LL-----------------TTTECIRFYGRLRGIRDlDQFLDRVLDTYEL-----RPYKDVQVRNLSGGNRRKLTVAvTC 1767
Cdd:PRK13637 81 IRkkvglvfqypeyqlfeeTIEKDIAFGPINLGLSE-EEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIA-GV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1768 CGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1836
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 ... |
843-1044 |
1.20e-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: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLY-----GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKV-LLAGEHQV----------- 905
Cdd:TIGR03269 282 VRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVdmtkpgpdgrg 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 906 ------GVCWQDNILIPTLTAREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHES------YPSwQLSGGYRR 973
Cdd:TIGR03269 362 rakryiGILHQEYDLYPHRTVLDNLTEAIGLELPD------ELARMKAVITLKMVGFDEEKAeeildkYPD-ELSEGERH 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 974 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
859-1054 |
1.22e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 859 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTLTAREhlqLY 927
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafaRKVAYLPQQLPAAEGMTVRE---LV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 928 AQIKIPPGGS----GGVEEIRSEVAQTLQSLNFGKHESYPSwqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARK 1003
Cdd:PRK10575 107 AIGRYPWHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDS--LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1004 DIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:PRK10575 185 DVLALVHRLSQERGltVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
842-1052 |
1.35e-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: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC--AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-----------EHQVGVC 908
Cdd:cd03251 2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQDNILIPTlTAREHLqLYAQikipPGGSggVEEIRsEVAQTLQSLNF--GKHESYPSW------QLSGGYRRRLCVAIA 980
Cdd:cd03251 82 SQDVFLFND-TVAENI-AYGR----PGAT--REEVE-EAARAANAHEFimELPEGYDTVigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1634-1847 |
1.37e-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: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN------- 1705
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 -PLDPLL---TTTECIRfYGRLRGIRD----------LDQFLDRVLDTYElrpyKDVQVR--NLSGGNRRKLTVAVTCCG 1769
Cdd:cd03251 81 vSQDVFLfndTVAENIA-YGRPGATREeveeaaraanAHEFIMELPEGYD----TVIGERgvKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1770 CTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1847
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVI-AHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1634-1842 |
1.69e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1704
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ----NPLDPLL--TTTECIRFyGRLRGIRDLDQFLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVL 1775
Cdd:PRK13639 82 ivfqNPDDQLFapTVEEDVAF-GPLNLGLSKEEVEKRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1776 MDEPTSDMDPvtrdMVYATIEQLL--LARRA--VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK13639 161 LDEPTSGLDP----MGASQIMKLLydLNKEGitIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
843-1046 |
1.75e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.93 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------------HQ 904
Cdd:PRK11153 4 LKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQ-----------DNILIPtltarehLQLYAQIKippggsggvEEIRSEVAQTLQSLNFG-KHESYPSwQLSGGYR 972
Cdd:PRK11153 84 IGMIFQhfnllssrtvfDNVALP-------LELAGTPK---------AEIKARVTELLELVGLSdKADRYPA-QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 973 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1634-1848 |
1.91e-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: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-----------GISYC 1701
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSNPL--DpllTTTECIRfYGRL----------RGIRDLDQFLDRVLDTYELRpykdVQVRN--LSGGNRRKLTVAVTC 1767
Cdd:cd03253 81 PQDTVLfnD---TIGYNIR-YGRPdatdeevieaAKAAQIHDKIMRFPDGYDTI----VGERGlkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1768 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1847
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
.
gi 221500365 1848 A 1848
Cdd:cd03253 231 E 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
871-1043 |
2.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.70 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ--DNILIPTlTAREHLQLYAQIK-IPpgg 936
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdirHKIGMVFQnpDNQFVGA-TVEDDVAFGLENKgIP--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 937 sggVEEIRSEVAQTLQ---SLNFGKHEsyPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR 1013
Cdd:PRK13650 114 ---HEEMKERVNEALElvgMQDFKERE--PA-RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR 187
|
170 180 190
....*....|....*....|....*....|..
gi 221500365 1014 Q--GRAVIFATHFMDEAKyLSDSLVIMRNGRI 1043
Cdd:PRK13650 188 DdyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
842-1055 |
2.72e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL------------LAGEHQVGVCW 909
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNILIPTLTAREHLQLYaqiKIPPGGSGGV-----EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIAS 984
Cdd:PRK09700 87 QELSVIDELTVLENLYIG---RHLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNG-----RIIAQHSRDSLQRL 1055
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVRL 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1632-1830 |
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 221500365 1632 EAVRAENLWlayrrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGI 1698
Cdd:cd03215 3 PVLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaiRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1699 SYCPQSnpldplltttecirfygRLR-GIrdldqFLDR-VLDTYELRPYkdvqvrnLSGGNRRKLTVAVTCCGCTPTVLM 1776
Cdd:cd03215 78 AYVPED-----------------RKReGL-----VLDLsVAENIALSSL-------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1777 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1649-1833 |
3.23e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQP------------GISYCPQSNPLDPLLTTTE 1715
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEmrfasttaalaaGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIrFYGRL---RGIRDLDQFLDRVLDTYE-----LRPykDVQVRNLSGGNRRKLTVAvtccgctpTVLM--------DEP 1779
Cdd:PRK11288 99 NL-YLGQLphkGGIVNRRLLNYEAREQLEhlgvdIDP--DTPLKYLSIGQRQMVEIA--------KALArnarviafDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1780 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1649-1837 |
3.41e-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: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTECIR 1718
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphkrpvntvfQNYALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 FYGRLRGIR--DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR-DMvyaTI 1795
Cdd:cd03300 95 FGLRLKKLPkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRkDM---QL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 1796 EQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
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 ... |
1649-1842 |
3.49e-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: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------QPGI-----------------SYCP 1702
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtKPGPdgrgrakryigilhqeyDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLlttTECIRF-----YGRLRGIRDL------DQFLDRVLDTYElrpykdvqvRNLSGGNRRKLTVAVTCCGCT 1771
Cdd:TIGR03269 379 HRTVLDNL---TEAIGLelpdeLARMKAVITLkmvgfdEEKAEEILDKYP---------DELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1772 PTVLMDEPTSDMDPVTRDMVYATIeqlLLARRAV----VLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSI---LKAREEMeqtfIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
835-1050 |
3.55e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 835 LDGKLGASLVNVSKLYGSkcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI- 913
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 --------------LIPTLTAREHLQLYAQIKIP-PGGSGGVEEIRSEVAQTLQSLNFgkheSYPSWQ-----LSGGYRR 973
Cdd:PRK10762 327 ngivyisedrkrdgLVLGMSVKENMSLTALRYFSrAGGSLKHADEQQAVSDFIRLFNI----KTPSMEqaiglLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 974 RLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1050
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1650-1831 |
3.70e-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: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP--DVGQIYFE---------QPGISYCPQSNPLDPLLTTTECIR 1718
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgrpldkrsfRKIIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 FYGRLRGIrdldqfldrvldtyelrpykdvqvrnlSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQL 1798
Cdd:cd03213 105 FAAKLRGL---------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|....
gi 221500365 1799 LLARRAVVLTSHSVS-EIEHLCQRVAVLRAGQVI 1831
Cdd:cd03213 158 ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1638-1836 |
4.01e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1638 NLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ-------------S 1704
Cdd:PRK13638 6 DLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllalrqqvatvfQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NPLDPLLTT--TECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1780
Cdd:PRK13638 85 DPEQQIFYTdiDSDIAFSLRNLGVpeAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1781 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1836
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
842-1046 |
6.14e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQDN 912
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREH----LQLYAQIKippggsggvEEIRSEVAQTLQSLNFGkH--ESYPSwQLSGGYRRRLCVAIAFIASPS 986
Cdd:PRK11000 85 ALYPHLSVAENmsfgLKLAGAKK---------EEINQRVNQVAEVLQLA-HllDRKPK-ALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRiIAQ 1046
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGR-VAQ 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1643-1833 |
7.46e-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: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1643 YRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQ---IYFEQPG----------ISYCpqSNPLDP 1709
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFGERRGgedvwelrkrIGLV--SPALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIR------FY---GRLRGIRDLDQFL-DRVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTVL- 1775
Cdd:COG1119 90 RFPRDETVLdvvlsgFFdsiGLYREPTDEQRERaRELLELLGLAHLADRPFGTLSQGEQRRVLIAralVK----DPELLi 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1776 MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
845-1052 |
9.13e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-------HQ-----VGVCWQDN 912
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplHArarrgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHLQLYAQIKippggSGGVEEIRSEVAQTL-QSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIR-----DDLSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 992 EPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1637-1830 |
1.45e-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: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI----------------YFEQP-GIS 1699
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgraipYLRRKiGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1700 YcpQSNPLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1777
Cdd:cd03292 84 F--QDFRLLPDRNVYENVAFALEVTGVppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1778 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1635-1830 |
1.61e-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: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP----------DVGQIYFEQPG--ISYC 1701
Cdd:cd03246 2 EVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtsgrvrldgaDISQWDPNELGdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQSnplDPLLTTTecirfygrlrgIRDldqfldrvldtyelrpykdvqvrN-LSGGNRRKLTVAVTCCGCTPTVLMDEPT 1780
Cdd:cd03246 82 PQD---DELFSGS-----------IAE-----------------------NiLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1781 SDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEhLCQRVAVLRAGQV 1830
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1634-1829 |
1.72e-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: 75.18 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYCPQsnpldpllt 1712
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 ttecirfygrlrgirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGcTPTVLM-DEPTSDMDPVTRDMV 1791
Cdd:cd03221 71 ----------------------------------------LSGGEKMRLALAKLLLE-NPNLLLlDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 221500365 1792 yatIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:cd03221 110 ---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1650-1915 |
1.73e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS------------YCPQSNPLDPLLTTTECI 1717
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrrvaSVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1718 RF-----YGRLRGIRDLDQ-FLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtrdmV 1791
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD------I 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1792 YATIEQLLLAR------RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ------RLKSEHGGYYAVTcfCGPAQQA 1859
Cdd:PRK09536 173 NHQVRTLELVRrlvddgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAdvltadTLRAAFDARTAVG--TDPATGA 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1860 ILSRSLNQRLPGARDLQHYAHSLrflvrvrspGSlGD--APLLSELFAILCDVCVNVA 1915
Cdd:PRK09536 251 PTVTPLPDPDRTEAAADTRVHVV---------GG-GQpaARAVSRLVAAGASVSVGPV 298
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
843-1052 |
1.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCW 909
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgiRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QD-NILIPTLTAREHLQLYAQ-IKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRrlCVAIAFI--ASP 985
Cdd:PRK13644 84 QNpETQFVGRTVEEDLAFGPEnLCLPP------IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ--CVALAGIltMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 986 SVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAkYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
851-1052 |
1.85e-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: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIpTLT 919
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLqLYAQIKIPPggsggvEEIRsEVAQTLQSLNF---------------GKhesypswQLSGGYRRRLCVAIAFIAS 984
Cdd:COG1132 430 IRENI-RYGRPDATD------EEVE-EAAKAAQAHEFiealpdgydtvvgerGV-------NLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHfmdeakYLS-----DSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVEQGTHEEL 561
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1648-1839 |
1.87e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1648 YAVRNVNFSVQ-------------RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQP-----------GISYCP 1702
Cdd:PRK10575 12 FALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPLLTTTECI---RF-----YGRLrGIRDLDQfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1774
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigRYpwhgaLGRF-GAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1775 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTS-HSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
851-1023 |
2.20e-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: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTlT 919
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPvssldqdevrrRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLYAqikipPGGSGgvEEI-----RSEVAQTLQSLNFGKHESYPS--WQLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:TIGR02868 425 VRENLRLAR-----PDATD--EELwaaleRVGLADWLRALPDGLDTVLGEggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 993 PCNGVDAKARKDIWQLIERLRQGRAVIFATH 1023
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
810-1052 |
2.38e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 810 YAVIGLAYQRYKKnnYSFVKVSRSQLDGKLGASLvnvsklygskcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQ 889
Cdd:PRK10070 11 YKIFGEHPQRAFK--YIEQGLSKEQILEKTGLSL-----------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 890 IRQSSGKVLLAG---------------EHQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGgsggvEEIRSEVAQTLQSL 954
Cdd:PRK10070 78 IEPTRGQVLIDGvdiakisdaelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINA-----EERREKALDALRQV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 955 NFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYL 1031
Cdd:PRK10070 153 GLENYaHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRI 231
|
250 260
....*....|....*....|.
gi 221500365 1032 SDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK10070 232 GDRIAIMQNGEVVQVGTPDEI 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1646-1843 |
2.64e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1715
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPpyqrpinmmfQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFyGRLRGIRDLDQFLDRVLDTYELRPYKDVQVR---NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD-MV 1791
Cdd:PRK11607 111 NIAF-GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrMQ 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1792 YATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLkSEH 1843
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI-YEH 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
855-1044 |
2.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL---------AGEHQVGVCWQDNI--------LIPT 917
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKKIknfkelrrRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLQLYA-----QIKIPPGGSG-GVEEIRSEVAQTLQSLnfGKHESY---PSWQLSGGYRRRlcVAIAFIAS--PS 986
Cdd:PRK13631 121 VFQFPEYQLFKdtiekDIMFGPVALGvKKSEAKKLAKFYLNKM--GLDDSYlerSPFGLSGGQKRR--VAIAGILAiqPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLI-ERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
845-1043 |
2.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.25 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCA--VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 910
Cdd:PRK13648 12 NVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklrKHIGIVFQn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 -DNILIPTLTA-------REHLQLYaqikippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI 982
Cdd:PRK13648 92 pDNQFVGSIVKydvafglENHAVPY-------------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 983 ASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAV--IFATHFMDEAKYlSDSLVIMRNGRI 1043
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1649-1832 |
2.93e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-------------EQPGISYCPQSNPLDPLLTTTE 1715
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpkssQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIrFYGR-----LRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:PRK10762 99 NI-FLGRefvnrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1635-1843 |
2.93e-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: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------ 1702
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrqlrrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 ---QSNPLDPLLTTTECIRFyGRL------RGIRDLDQFLDRV-----LDTYELRPYKDVQVRNLSGGNRRKLTVAVTCC 1768
Cdd:cd03256 82 mifQQFNLIERLSVLENVLS-GRLgrrstwRSLFGLFPKEEKQralaaLERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1769 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEgITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
845-1046 |
3.01e-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: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNI 913
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelaRRRAVLPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTARE--HLQLYAQikipPGGSGGVEEIRSEVAQTLQSLNFGkHESYPswQLSGGYRRR------LC-VAIAFIAS 984
Cdd:COG4559 86 LAFPFTVEEvvALGRAPH----GSSAAQDRQIVREALALVGLAHLA-GRSYQ--TLSGGEQQRvqlarvLAqLWEPVDGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHfmD---EAKYlSDSLVIMRNGRIIAQ 1046
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLH--DlnlAAQY-ADRILLLHQGRLVAQ 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1648-1832 |
3.13e-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: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1648 YAVRNVNFSVQ--RGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1715
Cdd:cd03298 10 YGEQPMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrpvsmlfQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFyGRLRGIR-------DLDQFLDRV-LDTYELRpykdvQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1787
Cdd:cd03298 90 NVGL-GLSPGLKltaedrqAIEVALARVgLAGLEKR-----LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 1788 RDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLmVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
845-1033 |
3.45e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIK-------LLTGQirQSSGKVLLAGEH-------------Q 904
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNlyapdvdpvevrrR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQDNILIPTltarehlQLYAQIKIPP---GGSGGVEEI--RS--------EVAQTLQslnfgkhESYPSwqLSGGY 971
Cdd:PRK14243 93 IGMVFQKPNPFPK-------SIYDNIAYGArinGYKGDMDELveRSlrqaalwdEVKDKLK-------QSGLS--LSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 972 RRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSD 1033
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1629-1837 |
3.68e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAVRAENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPGISYCPQS--- 1704
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--TVGGMVLSEETvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ----------NPLDPLLTTT--ECIRFYGRLRGI-RD-----LDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVT 1766
Cdd:PRK13635 79 vrrqvgmvfqNPDNQFVGATvqDDVAFGLENIGVpREemverVDQALRQV----GMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1767 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQ 1837
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1646-1829 |
4.17e-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: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGISYCPQSnpldP-LLTTT--ECIRFyGr 1722
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PGSIAYVSQE----PwIQNGTirENILF-G- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1723 lrgiRDLD-QFLDRVLDTYELRPykDVQV-------------RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:cd03250 90 ----KPFDeERYEKVIKACALEP--DLEIlpdgdlteigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1789 DMVYAT-IEQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQ 1829
Cdd:cd03250 164 RHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1644-1831 |
4.39e-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: 75.76 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1644 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYFE-----------QPGISYCPQSNPLDP 1709
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNgipykefaekyPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIRFYGRLRGirdlDQFldrvldtyelrpykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1789
Cdd:cd03233 97 TLTVRETLDFALRCKG----NEF-----------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1790 MVYATIEQLLLARRAVVLTSHSVS--EIEHLCQRVAVLRAGQVI 1831
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
839-1044 |
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 221500365 839 LGASLVNVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------ 901
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 902 ---EHQVGVCWQdnilIPtltareHLQLYAQIKIPPGGSG----GVEEIRSEvAQTLQSLNF-GKHESYPS---WQLSGG 970
Cdd:PRK13649 81 kqiRKKVGLVFQ----FP------ESQLFEETVLKDVAFGpqnfGVSQEEAE-ALAREKLALvGISESLFEknpFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 971 YRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
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 ... |
856-1043 |
5.21e-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: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPtltarehl 924
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 qlyaqikippgGSggveeirseVAQTLqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKD 1004
Cdd:cd03246 90 -----------GS---------IAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 221500365 1005 IWQLIERLR-QGRAVIFATHFMdEAKYLSDSLVIMRNGRI 1043
Cdd:cd03246 135 LNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
855-1052 |
5.46e-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: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVGVCWQD---NILIPTLT 919
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLYAQIKIppgGSGGV---EEIRSEVAQTLQSLNFgkheSYPSW-----QLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG1129 347 IRENITLASLDRL---SRGGLldrRRERALAEEYIKRLRI----KTPSPeqpvgNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 992 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1641-1810 |
6.01e-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: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-----------GISYCPQSNPLD 1708
Cdd:cd03231 6 LTCERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiarGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1709 PLLTTTECIRFYGRLRGIRDLDQFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:cd03231 86 TTLSVLENLRFWHADHSDEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|..
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSH 1810
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTH 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
871-1023 |
6.09e-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: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAGE-------HQV-GVCWQDNILIPTLTAREHLQLYAQIKIPPGGSGg 939
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMpidakemRAIsAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTK- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 940 vEEIRSEVAQTLQSLNF-----------GKHESypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1008
Cdd:TIGR00955 135 -KEKRERVDEVLQALGLrkcantrigvpGRVKG-----LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....*.
gi 221500365 1009 IERLRQ-GRAVIFATH 1023
Cdd:TIGR00955 209 LKGLAQkGKTIICTIH 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1636-1810 |
7.60e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLwlAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-----------YCPQ 1703
Cdd:PRK13538 4 ARNL--ACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyhqdllYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPLLTTTECIRFYGRLRGIRDLDQFLDrVLDTYELRPYKDVQVRNLSGGNRRKLTVA---VTCCgctPTVLMDEP- 1779
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArlwLTRA---PLWILDEPf 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 221500365 1780 TS-DMDPVtrdmvyATIEQLLLARRA----VVLTSH 1810
Cdd:PRK13538 158 TAiDKQGV------ARLEALLAQHAEqggmVILTTH 187
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
845-1033 |
7.93e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLT------GQIRqSSGKVLLAGEH-------------QV 905
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVR-VEGRVEFFNQNiyerrvnlnrlrrQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 906 GVCWQDNILIPtltarehLQLYAQI----KI----PPGGSGGVEEIRSEVAQTLQSLNFGKHESypSWQLSGGYRRRLCV 977
Cdd:PRK14258 91 SMVHPKPNLFP-------MSVYDNVaygvKIvgwrPKLEIDDIVESALKDADLWDEIKHKIHKS--ALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 978 AIAFIASPSVVILDEPCNGVDAKARKDIWQLIE--RLRQGRAVIFATHFMDEAKYLSD 1033
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1644-1831 |
7.98e-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: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1644 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY------FEQPGISYCPQS----------NPL 1707
Cdd:cd03258 15 GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdlTLLSGKELRKARrrigmifqhfNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DPlLTTTECIRFYGRLRGIRDLDQfLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDM 1783
Cdd:cd03258 95 SS-RTVFENVALPLEIAGVPKAEI-EERVLELLElvgLEDKADAYPAQLSGGQKQRVGIA-RALANNPKVLLcDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1784 DPVTRDmvyaTIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:cd03258 172 DPETTQ----SILALLrdINRElglTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1649-1836 |
8.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD--------VGQIYF---------EQPGISYcpqSNPLDPLL 1711
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitVDGITLtaktvwdirEKVGIVF---QNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 --TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1787
Cdd:PRK13640 99 gaTVGDDVAFGLENRAVprPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1788 RDMVYATIEQLLLARRAVVLT-SHSVSEIEHLCQrVAVLRAGQVIASDSP 1836
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISiTHDIDEANMADQ-VLVLDDGKLLAQGSP 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1628-1832 |
8.68e-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: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAV-RAENLWlayRRGHyaVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP--------- 1696
Cdd:COG1129 250 AAPGEVVlEVEGLS---VGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgKPvrirsprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 ---GISYCP---QSNPLDPLLTTTE-----CIRFYGRLRGIRD--LDQFLDRVLDTYELR-PYKDVQVRNLSGGNRRKLT 1762
Cdd:COG1129 325 iraGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRrrERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1763 VA---VTCcgctPTVL-MDEPTSDMDPVTRDMVYATIEQLllARR--AVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:COG1129 405 LAkwlATD----PKVLiLDEPTRGIDVGAKAEIYRLIREL--AAEgkAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
845-1046 |
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 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGeHQV------------GVCWQDN 912
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLadwspaelarrrAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTARE--HLQLYaqikipPGGSGGVEEiRSEVAQTLQSLNFG--KHESYPswQLSGGYRRRlcVAIAFI------ 982
Cdd:PRK13548 86 SLSFPFTVEEvvAMGRA------PHGLSRAED-DALVAAALAQVDLAhlAGRDYP--QLSGGEQQR--VQLARVlaqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 983 --ASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
850-1044 |
1.39e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.72 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-----QSSGKVLLAGehqvgvcwQDNILIPTLTAREHL 924
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDG--------QDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYAQIKIP-PGGS---------------GGVEEIRSEVAQTLQSLNFGKHE----SYPSWQLSGGYRRRLCVAIAFIAS 984
Cdd:PRK14247 85 QMVFQIPNPiPNLSifenvalglklnrlvKSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1641-1843 |
1.41e-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: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------QPGISYCPQS 1704
Cdd:TIGR02769 17 LFGAKQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlyqldrkqrrafRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NP--LDPLLTTTECI----RFYGRLRGIRDLDQFLDrVLDTYELRP-YKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMD 1777
Cdd:TIGR02769 97 SPsaVNPRMTVRQIIgeplRHLTSLDESEQKARIAE-LLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1778 EPTSDMDPVTRdmvyATIEQLLLARR-----AVVLTSHSVSEIEHLCQRVAVLRAGQVIAS-DSPQRLKSEH 1843
Cdd:TIGR02769 176 EAVSNLDMVLQ----AVILELLRKLQqafgtAYLFITHDLRLVQSFCQRVAVMDKGQIVEEcDVAQLLSFKH 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
853-1071 |
1.48e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 853 KCAVSNLSLDFARNQVSCLLGRNGAGKS----TLIKLL--------TGQIRQSSGKVLLAGE--------HQVGVCWQDN 912
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEqtlrgvrgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 I--LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNF----GKHESYPSwQLSGGYRRRLCVAIAFIASPS 986
Cdd:PRK15134 102 MvsLNPLHTLEK--QLYEVLSLHRGMRR--EAARGEILNCLDRVGIrqaaKRLTDYPH-QLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQRLCTSNYSIRL 1064
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKL 256
|
....*..
gi 221500365 1065 RCADATG 1071
Cdd:PRK15134 257 LNSEPSG 263
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
941-1053 |
1.54e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.47 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 941 EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVI 1019
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVL 198
|
90 100 110
....*....|....*....|....*....|....
gi 221500365 1020 FATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1053
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1632-1842 |
1.76e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1632 EAVRAENLWLAYRRG-----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS-- 1704
Cdd:PRK13633 3 EMIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTSDEEnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ------------NPLDPLLTTT--ECIRFYGRLRGI------RDLDQFLDRVlDTYElrpYKDVQVRNLSGGNRRKLTVA 1764
Cdd:PRK13633 81 wdirnkagmvfqNPDNQIVATIveEDVAFGPENLGIppeeirERVDESLKKV-GMYE---YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1765 VTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQllLARR---AVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKKygiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 221500365 1842 E 1842
Cdd:PRK13633 234 E 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
845-1046 |
1.78e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQV------------------- 905
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseaerrrllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 906 -GVCWQDniliptltAREHLQLyaqiKIPPGGSGG----------VEEIRSEVAQTLQ--SLNFGKHESYPSwQLSGGYR 972
Cdd:PRK11701 91 wGFVHQH--------PRDGLRM----QVSAGGNIGerlmavgarhYGDIRATAGDWLErvEIDAARIDDLPT-TFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 973 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1634-1843 |
1.82e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAY--RRghyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-----------GIS 1699
Cdd:PRK11231 3 LRTENLTVGYgtKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPismlssrqlarRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1700 YCPQSNPLDPLLTTTECI--------RFYGRLRGirDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCT 1771
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVaygrspwlSLWGRLSA--EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1772 PTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1634-1842 |
2.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ---------- 1703
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmklresvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 ---SNPLDPLLTTT--ECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLM 1776
Cdd:PRK13636 86 mvfQDPDNQLFSASvyQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1777 DEPTSDMDPV-TRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK13636 166 DEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
850-1046 |
2.39e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 850 YGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTL 918
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 TAREhlqLYAQIKIP--PGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:PRK10253 97 TVQE---LVARGRYPhqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 997 VDAKARKDIWQLIERLRQGRAVIFAT--HFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAvlHDLNQACRYASHLIALREGKIVAQ 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1635-1837 |
2.72e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1635 RAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------ 1702
Cdd:PRK11701 8 SVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 --------QSNPLD--------------PLLTTTEciRFYGRLRgiRDLDQFLDRVldtyELRPYK-DVQVRNLSGGNRR 1759
Cdd:PRK11701 87 lrtewgfvHQHPRDglrmqvsaggnigeRLMAVGA--RHYGDIR--ATAGDWLERV----EIDAARiDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1760 KLTVA---VTccgcTPT-VLMDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK11701 159 RLQIArnlVT----HPRlVFMDEPTGGLD-VS---VQARLLDLLrgLVRElglAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....
gi 221500365 1831 IAS-------DSPQ 1837
Cdd:PRK11701 231 VESgltdqvlDDPQ 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
842-1044 |
3.08e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGS-----KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG-------EHQ----V 905
Cdd:COG1101 3 ELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpEYKrakyI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 906 GVCWQDNIL--IPTLTAREHLQL-YAQIKIPPGGSGGVEEIRSEVAQTLQSLNFG--KHESYPSWQLSGGYRRRLCVAIA 980
Cdd:COG1101 83 GRVFQDPMMgtAPSMTIEENLALaYRRGKRRGLRRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1646-1841 |
3.59e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP-QSNPLDPLLTTTECIRFYGRLR 1724
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1725 GIRDL--------------------------DQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVAVtcCGCT-PTV 1774
Cdd:PRK11300 97 VIENLlvaqhqqlktglfsgllktpafrraeSEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIAR--CMVTqPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1775 LM-DEPTSDMDPVTRDMVYATIEQLllaRR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:PRK11300 175 LMlDEPAAGLNPKETKELDELIAEL---RNehnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
855-1048 |
6.93e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDniliPT--LTAR 921
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysyrsqRIRMIFQD----PStsLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 EHLQLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAK 1000
Cdd:PRK15112 104 QRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1001 ARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1048
Cdd:PRK15112 184 MRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
845-1046 |
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 221500365 845 NVSKLYG--SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgVCWQDnILIPTLtaRE 922
Cdd:TIGR02203 335 NVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-----HDLAD-YTLASL--RR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 HLQLYAQ------------IKIPPGGSGGVEEIRSEVAQT-LQSL----------NFGKHESypswQLSGGYRRRLCVAI 979
Cdd:TIGR02203 407 QVALVSQdvvlfndtiannIAYGRTEQADRAEIERALAAAyAQDFvdklplgldtPIGENGV----LLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQ 1046
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 ... |
1630-1836 |
9.28e-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: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1630 TGEaVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN--- 1705
Cdd:cd03369 4 HGE-IEVENLSVRYAPDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 -----PLDPLLtttecirFYGRLRGirDLDQFlDRvldtyelrpYKDVQVR----------NLSGGNRRKLTVAVTCCGC 1770
Cdd:cd03369 83 sltiiPQDPTL-------FSGTIRS--NLDPF-DE---------YSDEEIYgalrvsegglNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1771 TPTVLMDEPTSDMDPVTRDMVYATIEQLLlaRRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSP 1836
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTiAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1644-1914 |
1.13e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.34 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1644 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycpqsnPLDPlltttecirfyGRL 1723
Cdd:COG1135 15 GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT------ALSE-----------REL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1724 RGIR-------------------------------DLDQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVA---VT 1766
Cdd:COG1135 78 RAARrkigmifqhfnllssrtvaenvalpleiagvPKAEIRKRVaelLELVGLSDKADAYPSQLSGGQKQRVGIAralAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1767 ccgcTPTVLM-DEPTSDMDPVTRDmvyaTIEQLLL-ARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVIasdspqrlk 1840
Cdd:COG1135 158 ----NPKVLLcDEATSALDPETTR----SILDLLKdINRelglTIVLITHEMDVVRRICDRVAVLENGRIV--------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1841 sEHGGYYAVtcFCGPAQ---QAILSRSLNQRLPG--ARDLQHYAHSLRfLVRVRSPGSLGDAPLLSELFAILcDVCVNV 1914
Cdd:COG1135 221 -EQGPVLDV--FANPQSeltRRFLPTVLNDELPEelLARLREAAGGGR-LVRLTFVGESADEPLLSELARRF-GVDVNI 294
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
842-1052 |
1.23e-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: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGvcWQDNILIPTLTA- 920
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD--WQTAKIMREAVAi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 921 -REHLQLYAQIKIPPG-GSGGVEEIRSEVAQTLQSLnfgkHESYPSWQ---------LSGGYRRRLCVAIAFIASPSVVI 989
Cdd:PRK11614 85 vPEGRRVFSRMTVEENlAMGGFFAERDQFQERIKWV----YELFPRLHerriqragtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1647-1839 |
1.27e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1647 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE--------------QPGISYcpqSNPLDPLL- 1711
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteenvwdirhKIGMVF---QNPDNQFVg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 -TTTECIRFYGRLRGIrDLDQFLDRVLDTYEL---RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1787
Cdd:PRK13650 97 aTVEDDVAFGLENKGI-PHEEMKERVNEALELvgmQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1788 RDMVYATIEQLLLARRAVVLT-SHSVSEIEhLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISiTHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
845-1045 |
1.35e-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: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEHQVG------------VCWQ 910
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKAsnirdteragivIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTAREHLQLYAQIKIpPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITL-PGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1650-1837 |
1.48e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------QSNPLDPLLTTTECI 1717
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelakrlailrQENHINSRLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1718 RF----Y--GRLRGiRDlDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMdpvtrDMV 1791
Cdd:COG4604 97 AFgrfpYskGRLTA-ED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNL-----DMK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1792 YAT-IEQLL--LAR---RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:COG4604 170 HSVqMMKLLrrLADelgKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1651-1833 |
1.92e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1651 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTECI 1717
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltpakahQLGIYLVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1718 RF-----YGRLRGIRDLDQFLDRVLD------TYELrpyKDVQVRNLSGGNRRKLTVavtccgctptVLMDEPTSDMDPV 1786
Cdd:PRK15439 108 LFglpkrQASMQKMKQLLAALGCQLDldssagSLEV---ADRQIVEILRGLMRDSRI----------LILDEPTASLTPA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1787 TRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
845-1055 |
2.16e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-------------QVGVCWQD 911
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpkvderlirqEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLqLYAQIKIPPGGSGGVEEIRSEVaqtLQSLNFGKHES-YPSwQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK09493 86 FYLFPHLTALENV-MFGPLRVRGASKEEAEKQAREL---LAKVGLAERAHhYPS-ELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 991 DEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL------QRL 1055
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLiknppsQRL 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1641-1810 |
2.38e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAVRN-VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QPG--------ISYCPQSNPLDPL 1710
Cdd:PRK13543 17 LAFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTAtrgdrsrfMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1711 LTTTECIRFYGRLRGiRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDM 1790
Cdd:PRK13543 97 LSTLENLHFLCGLHG-RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 221500365 1791 VYATIEQLLLARRAVVLTSH 1810
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1651-1830 |
2.64e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1651 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ-------------PGISYCPQSNP-----LDPLLT 1712
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalstaqrlaRGLVYLPEDRQssglyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIRFYGR----LRGIRDldqflDRVLDTYELR-----PYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSD 1782
Cdd:PRK15439 360 WNVCALTHNRrgfwIKPARE-----NAVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIA-KCLEASPQLLIvDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1649-1871 |
3.60e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.53 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------------QPGISYCPQSNPLDPLLT 1712
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevrRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIRFYGRLRGIRDLDQfLDRVLDTYE---LRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1789
Cdd:PRK10070 123 VLDNTAFGMELAGINAEER-REKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1790 MVYATIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYYAVTCFCGP------AQQAILS 1862
Cdd:PRK10070 202 EMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVdisqvfSAKDIAR 281
|
250
....*....|..
gi 221500365 1863 RSLN---QRLPG 1871
Cdd:PRK10070 282 RTPNgliRKTPG 293
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
851-1046 |
3.92e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKST----LIKLLTGQ---------IRQSSGKVLLAGEHQVGVCWQD--NILI 915
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgqpLHNLNRRQLLPVRHRIQVVFQDpnSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTArehLQLYA---QIKIPPGGSGGVEEirsEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK15134 377 PRLNV---LQIIEeglRVHQPTLSAAQREQ---QVIAVMEEvgLDPETRHRYPA-EFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1637-1836 |
4.71e-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: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRG-HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpG--------------ISYC 1701
Cdd:cd03244 6 KNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID--GvdiskiglhdlrsrISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1702 PQsnplDPLLtttecirFYGRLRgiRDLDQF-------LDRVLDTYELRPY-------KDVQV----RNLSGGNRRKLTV 1763
Cdd:cd03244 84 PQ----DPVL-------FSGTIR--SNLDPFgeysdeeLWQALERVGLKEFveslpggLDTVVeeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1764 AVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSP 1836
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1634-1839 |
4.76e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP-------------GIS 1699
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgEPitkenirevrkfvGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1700 YcpqSNPLDPLLTTT--ECIRFYGRLRGIRD--LDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVL 1775
Cdd:PRK13652 84 F---QNPDDQIFSPTveQDIAFGPINLGLDEetVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIA-GVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1776 -MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13652 160 vLDEPTAGLDPQGVKELIDFLNDLPETYgMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
831-1052 |
5.59e-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: 74.39 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 831 SRSQLDGKLGASLVNVSKLYGSKcAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQvgvcwq 910
Cdd:TIGR01193 466 ELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL------ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLtaREHLQLYAQIKIPPGGS----------GGVE-----------EIRSEVAQTlqSLNFGKHESYPSWQLSG 969
Cdd:TIGR01193 539 KDIDRHTL--RQFINYLPQEPYIFSGSilenlllgakENVSqdeiwaaceiaEIKDDIENM--PLGYQTELSEEGSSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 970 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIwqlIERLR--QGRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQH 1047
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLLnlQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
....*
gi 221500365 1048 SRDSL 1052
Cdd:TIGR01193 691 SHDEL 695
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
866-1023 |
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 221500365 866 NQVSCLLGRNGAGKSTLIKLLTGQIRQS--SGKVLLAG-------EHQVGVCWQDNILIPTLTAREHLQLYAQIKippgg 936
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGrpldknfQRSTGYVEQQDVHSPNLTVREALRFSALLR----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 937 sggveeirsevaqtlqslnfgkhesypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQG 1015
Cdd:cd03232 108 -----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSG 158
|
....*...
gi 221500365 1016 RAVIFATH 1023
Cdd:cd03232 159 QAILCTIH 166
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
959-1043 |
7.23e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 959 HESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVI 1037
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLV 475
|
....*.
gi 221500365 1038 MRNGRI 1043
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) ... |
1660-1825 |
7.80e-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: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1660 GECFGLLGKNGAGKSTIFKLLTGQLQPDVG--------------------QIYFEQ-------PGISycPQSNPLDPLlt 1712
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselQNYFTKllegdvkVIVK--PQYVDLIPK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 tteciRFYGRLRGI---RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1789
Cdd:cd03236 102 -----AVKGKVGELlkkKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 221500365 1790 MVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVL 1825
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
844-1044 |
8.50e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 844 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIK-----LLTGQIRQSSGKVLLAGEH-------------QV 905
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNiyspdvdpievrrEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 906 GVCWQDNILIPTLTAREHLQLYAQIKippGGSGGVEEIRSEVAQTLQSLNF-----GKHESYPSwQLSGGYRRRLCVAIA 980
Cdd:PRK14267 88 GMVFQYPNPFPHLTIYDNVAIGVKLN---GLVKSKKELDERVEWALKKAALwdevkDRLNDYPS-NLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
845-1044 |
8.92e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLY---------GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehqvgvCWQDNILI 915
Cdd:PRK10419 8 GLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV----------SWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTA-----REHLQLYAQIkiPPGGSG---GVEEIRSEVAQTLQSLNFGKHES------------------YPSwQLSG 969
Cdd:PRK10419 78 KLNRAqrkafRRDIQMVFQD--SISAVNprkTVREIIREPLRHLLSLDKAERLArasemlravdlddsvldkRPP-QLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 970 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
856-1052 |
9.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQ--DNILIPTlTARE 922
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrrKIGMVFQnpDNQFVGA-TVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 HLQLYAQIKIPPGgsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:PRK13642 102 DVAFGMENQGIPR-----EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1003 KDIWQLIERLRQGR--AVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK13642 177 QEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1633-1831 |
9.33e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHyAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGIsYCPQSNPL 1707
Cdd:PRK14267 4 AIETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNI-YSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 D---------------PLLTTTECI----RFYGRLRGIRDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLT 1762
Cdd:PRK14267 82 EvrrevgmvfqypnpfPHLTIYDNVaigvKLNGLVKSKKELDERVEWALKKAAL--WDEVKDRlndypsNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1763 VAVTCCGCTPTVLMDEPTSDMDPVTRdmvyATIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGT----AKIEELLFELKkeyTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1649-1829 |
1.03e-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: 69.77 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGisycpqsNPLDpLLTTTECIRFYGRLRGIRD 1728
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-------GWVD-LAQASPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1729 LDQFLD---RV--LDT-----YEL---RPYKDVQVRNL------------------SGGNRRKLTVAVTCCGCTPTVLMD 1777
Cdd:COG4778 98 VSQFLRvipRVsaLDVvaeplLERgvdREEARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1778 EPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1647-1835 |
1.17e-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: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1647 HY----AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPL-DPLLTTTECIRFYG 1721
Cdd:PRK11614 14 HYgkiqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1722 RLRGIRDL---------DQFLDRVLDTYELRP----YKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:PRK11614 94 RMTVEENLamggffaerDQFQERIKWVYELFPrlheRRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1835
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
855-1046 |
1.20e-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: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRqSSGKVLLAGEHqvgvcwqdnilIPTLTAREHLQLYAQIKI-- 932
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQD-----------LDGLSRRALRPLRRRMQVvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 933 ------------------------PPGGSGgvEEIRSEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPS 986
Cdd:COG4172 369 qdpfgslsprmtvgqiiaeglrvhGPGLSA--AERRARVAEALEEvgLDPAARHRYPH-EFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 987 VVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLqrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
856-1046 |
1.24e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKS----TLIKLLTGQIRQSSGKVLLAGEHQVGvCWQDNILIPTLtarehlqlyaqIK 931
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP-CALRGRKIATI-----------MQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 IPPGGSGGVEEIRSEVAQTLQSLnfGKH----------------------ESYPsWQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:PRK10418 87 NPRSAFNPLHTMHTHARETCLAL--GKPaddatltaaleavglenaarvlKLYP-FEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
858-1052 |
1.28e-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: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEH-----------QVGVCWQDNILIPTlTAREHLQL 926
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsQIGLVSQEPVLFDG-TIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 yaqikippGGSGGVEEIRSEVAQTLQSLNF------------GKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:cd03249 100 --------GKPDATDEEVEEAAKKANIHDFimslpdgydtlvGERGS----QLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 995 NGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
842-1045 |
1.32e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ 910
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTARE--------HLQLYAQIKipPGGSGGVEEI--RSEVAQtlqslnFGKHesyPSWQLSGGYRRRLCVAIA 980
Cdd:PRK09536 85 DTSLSFEFDVRQvvemgrtpHRSRFDTWT--ETDRAAVERAmeRTGVAQ------FADR---PVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 981 FIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1630-1832 |
1.59e-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: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1630 TGEAV-RAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-------------Q 1695
Cdd:COG3845 253 PGEVVlEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeditglsprerrR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1696 PGISYCPQsnplDPL-------LTTTECI--RFYGRL----RGIRD---LDQFLDRVLDTYELR-PYKDVQVRNLSGGNR 1758
Cdd:COG3845 333 LGVAYIPE----DRLgrglvpdMSVAENLilGRYRRPpfsrGGFLDrkaIRAFAEELIEEFDVRtPGPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1759 RKLTVA--VTccgCTPTVL-MDEPTSDMDPVTRDMVYatieQLLLARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:COG3845 409 QKVILAreLS---RDPKLLiAAQPTRGLDVGAIEFIH----QRLLELRdagaAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
.
gi 221500365 1832 A 1832
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 ... |
1634-1836 |
1.71e-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: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDVGQIYFEqpgISYCPQSNPLD-PL 1710
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH---VALCEKCGYVErPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1711 LTTTEC-----------IRFYG------------------RLRGIRDLDQFLDRVLDTYELRPYK-------------DV 1748
Cdd:TIGR03269 77 KVGEPCpvcggtlepeeVDFWNlsdklrrrirkriaimlqRTFALYGDDTVLDNVLEALEEIGYEgkeavgravdlieMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1749 QV--------RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLC 1819
Cdd:TIGR03269 157 QLshrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEDLS 236
|
250
....*....|....*..
gi 221500365 1820 QRVAVLRAGQVIASDSP 1836
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTP 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1652-1784 |
1.81e-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: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPGISYCPQS-NPLDPLLTTTECIRfygrlrgiRDL 1729
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQSrDALDPNKTVWEEIS--------GGL 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1730 DQFldrVLDTYEL--RPY--------KDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1784
Cdd:TIGR03719 412 DII---KLGKREIpsRAYvgrfnfkgSDQQkkVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1633-1842 |
2.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQ--------- 1703
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrskvgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 --SNPLDPLLTTT--ECIRFYGRLRGIRDlDQFLDRV---LDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLM 1776
Cdd:PRK13647 84 vfQDPDDQVFSSTvwDDVAFGPVNMGLDK-DEVERRVeeaLKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1777 DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
845-1045 |
2.18e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEHQ------------VGVCWQ 910
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqasnirdteragIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTAREHLQLYAQIKipPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEIT--PGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 991 DEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1649-1834 |
2.28e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPD---VGQIYF-------------EQPGISYCPQSNPLDPLLT 1712
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFegeelqasnirdtERAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIrFYGR---LRGIRDLDQFL---DRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSdmdPV 1786
Cdd:PRK13549 99 VLENI-FLGNeitPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA---SL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1787 TRdmvyATIEQLL-----LARRAV--VLTSHSVSEIEHLCQRVAVLRAGQVIASD 1834
Cdd:PRK13549 175 TE----SETAVLLdiirdLKAHGIacIYISHKLNEVKAISDTICVIRDGRHIGTR 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1653-1830 |
2.43e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1653 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY-------FEQP------GISYCPQSNPLD---PLLTTTE- 1715
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidIRSPrdairaGIMLCPEDRKAEgiiPVHSVADn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 ----CIRFYGRLRGIRD-------LDQFLDRvldtyeLR---PYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:PRK11288 352 inisARRHHLRAGCLINnrweaenADRFIRS------LNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
853-1048 |
3.44e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 853 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTG-------------------------QIRQSSGKVLLAGEHQ-VG 906
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnskitvdgitltaktvwDIREKVGIVFQNPDNQfVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQDNI---LIPTLTAREHLqlyaqIKIppggsggVEEIRSEVAQtlqsLNFGKHEsyPSWqLSGGYRRRlcVAIAFIA 983
Cdd:PRK13640 100 ATVGDDVafgLENRAVPRPEM-----IKI-------VRDVLADVGM----LDYIDSE--PAN-LSGGQKQR--VAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 984 S--PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKyLSDSLVIMRNGRIIAQHS 1048
Cdd:PRK13640 159 AvePKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
871-1042 |
3.55e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGE-------HQVGVCWQDNILIPTLTAREHLQLYAQIKIPPGGSggvE 941
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqilKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKSLT---K 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 942 EIRSEVAQTLQS-LNFGKHESYPSWQ-----LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ- 1014
Cdd:PLN03211 176 QEKILVAESVISeLGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQk 255
|
170 180
....*....|....*....|....*....
gi 221500365 1015 GRAVIFATHFMDEAKY-LSDSLVIMRNGR 1042
Cdd:PLN03211 256 GKTIVTSMHQPSSRVYqMFDSVLVLSEGR 284
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1649-1855 |
4.34e-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: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------QPGISYCPQSNPLDPLLTTTECIR 1718
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvqERNVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 FYGRLRGIR------DLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDMDPVTRdmv 1791
Cdd:cd03296 97 FGLRVKPRSerppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA-RALAVEPKVLLlDEPFGALDAKVR--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1792 yatiEQLllaRR-----------AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLkSEHGGYYAVTCFCGP 1855
Cdd:cd03296 173 ----KEL---RRwlrrlhdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV-YDHPASPFVYSFLGE 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1642-1903 |
4.37e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.83 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1642 AYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycpqsnPLDP------------ 1709
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT------ALSEkelrkarrqigm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 ------LL---TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCcGCTPTVLM-D 1777
Cdd:PRK11153 87 ifqhfnLLssrTVFDNVALPLELAGTpkAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL-ASNPKVLLcD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1778 EPTSDMDPVTRDmvyaTIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVIasdspqrlksEHGGYYAVtcF 1852
Cdd:PRK11153 166 EATSALDPATTR----SILELLkdINRElglTIVLITHEMDVVKRICDRVAVIDAGRLV----------EQGTVSEV--F 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1853 CGPAQ---QAILSRSLNQRLPG---ARDLQHYAHSLRFLVRVRSPGSLGDAPLLSEL 1903
Cdd:PRK11153 230 SHPKHpltREFIQSTLHLDLPEdylARLQAEPTTGSGPLLRLEFTGESVDAPLLSET 286
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1633-1837 |
5.43e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.48 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGH-YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQS------- 1704
Cdd:PRK13632 7 MIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID--GITISKENlkeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ------NPLDPLL--TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV 1774
Cdd:PRK13632 85 igiifqNPDNQFIgaTVEDDIAFGLENKKVppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1775 LMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEhLCQRVAVLRAGQVIASDSPQ 1837
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
855-1053 |
6.69e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------------EHQVGVCWQDNILIPTLTARE 922
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtfngpkssqEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 HLQLYAQIKIPPGGSGGvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:PRK10762 99 NIFLGREFVNRFGRIDW-KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1003 KDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1053
Cdd:PRK10762 178 ESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1634-1842 |
8.40e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPD--------------------VGQIYF 1693
Cdd:PRK09984 5 IRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1694 EQPGISYCPQSNPLDPLLTTTE---------------CIRFYGRLRGIRDLdQFLDRVldtyELRPYKDVQVRNLSGGNR 1758
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLEnvligalgstpfwrtCFSWFTREQKQRAL-QALTRV----GMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1759 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*
gi 221500365 1838 RLKSE 1842
Cdd:PRK09984 239 QFDNE 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1637-1831 |
9.00e-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: 70.10 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRGHY---AVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQLQPDVGQIYFE--------------- 1694
Cdd:COG4172 10 EDLSVAFGQGGGtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgqdllglserelrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1695 ----------QPGISycpqsnpLDPLLTT----TECIRFYGRLRG------IRDLdqfLDRV--------LDTYelrPYK 1746
Cdd:COG4172 90 rgnriamifqEPMTS-------LNPLHTIgkqiAEVLRLHRGLSGaaararALEL---LERVgipdperrLDAY---PHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1747 dvqvrnLSGGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQ 1820
Cdd:COG4172 157 ------LSGGQRQRVMIAMALA-NEPDLLIaDEPTTALD-VT---VQAQILDLLkdLQRElgmALLLITHDLGVVRRFAD 225
|
250
....*....|.
gi 221500365 1821 RVAVLRAGQVI 1831
Cdd:COG4172 226 RVAVMRQGEIV 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1652-1810 |
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 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQP-GISYCPQSNPLDPLLTTTecIRFYGRLR-GIRDL 1729
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLDTTLPLT--VNRFLRLRpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1730 DQF--LDRVLDTYELrpykDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLllaRR---- 1803
Cdd:PRK09544 100 DILpaLKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL---RReldc 172
|
....*..
gi 221500365 1804 AVVLTSH 1810
Cdd:PRK09544 173 AVLMVSH 179
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1643-1839 |
1.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1643 YRRG----HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLLT------ 1712
Cdd:PRK13646 12 YQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKrigmvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 ----------TTECIRFYGRLRGIRDLDQFLDRVL----------DTYELRPYKdvqvrnLSGGNRRKLTVaVTCCGCTP 1772
Cdd:PRK13646 92 qfpesqlfedTVEREIIFGPKNFKMNLDEVKNYAHrllmdlgfsrDVMSQSPFQ------MSGGQMRKIAI-VSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1773 TVL-MDEPTSDMDPVTRDMVYATIEQLLLAR-RAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13646 165 DIIvLDEPTAGLDPQSKRQVMRLLKSLQTDEnKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1649-1863 |
1.24e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAG--KSTIFKLLTGqlqPDVGQiyfeQPG--ISYCPQSNPLDPLLTTTECIR------ 1718
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR----RPWrf*TWCANRRALRRTIG*HRPVR*grres 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 FYGRLR----------GIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:NF000106 101 FSGRENlymigr*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHGGYyavTCFCGPAQQAILSR 1863
Cdd:NF000106 181 NEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR---TLQIRPAHAAELDR 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1641-1831 |
1.38e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------------QPGISYCPQS 1704
Cdd:PRK10419 18 LSGKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklnraqrkafRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NP--LDPLLTTTECIRfyGRLRGIRDLDQF-----LDRVLDTYELRPyKDVQVR--NLSGGNRRKLTVAvTCCGCTPT-V 1774
Cdd:PRK10419 98 SIsaVNPRKTVREIIR--EPLRHLLSLDKAerlarASEMLRAVDLDD-SVLDKRppQLSGGQLQRVCLA-RALAVEPKlL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1775 LMDEPTSDMDPVTRdmvyATIEQLLLARR-----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK10419 174 ILDEAVSNLDLVLQ----AGVIRLLKKLQqqfgtACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
860-1053 |
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 221500365 860 SLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-HQ--------VGVCWQDNILIPTLTAREH--LQLYA 928
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTttppsrrpVSMLFQENNLFSHLTVAQNigLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 929 QIKIPPGGSGGVEEIRSEVAqtLQSLnfgkHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1008
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMG--IEDL----LARLPG-QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1009 IERLRQGRAV--IFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSLQ 1053
Cdd:PRK10771 172 VSQVCQERQLtlLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
855-1046 |
1.63e-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: 69.33 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKS----TLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNI-- 913
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllglserelrrirgNRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTL---------QSLNfgkheSYPSwQLSGGYRRRLCVAIAFIAS 984
Cdd:COG4172 105 LNPLHTIGK--QIAEVLRLHRGLSG--AAARARALELLervgipdpeRRLD-----AYPH-QLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 985 PSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1633-1784 |
1.71e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYaVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI-YFEQPGISYCPQ--SNPLDP 1709
Cdd:PRK15064 319 ALEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQdhAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIRFYgrlRGIRDLDQ----FLDRVLDTYElrpykDV--QVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1783
Cdd:PRK15064 398 DLTLFDWMSQW---RQEGDDEQavrgTLGRLLFSQD-----DIkkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHM 469
|
.
gi 221500365 1784 D 1784
Cdd:PRK15064 470 D 470
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
844-1052 |
1.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 844 VNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSG-----KVLLAGE------------HQVG 906
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRsifnyrdvlefrRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQ----------DNILIPT----LTAREHLQLYAQIKIPPGGsggveeIRSEVAQTLQSLNFgkhesypswQLSGGYR 972
Cdd:PRK14271 105 MLFQrpnpfpmsimDNVLAGVrahkLVPRKEFRGVAQARLTEVG------LWDAVKDRLSDSPF---------RLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 973 RRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
844-1046 |
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 221500365 844 VNVSKLYGSKCAVSNLSLdfARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----EHQVGVC----------- 908
Cdd:PRK11144 4 LNFKQQLGDLCLTVNLTL--PAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGIClppekrrigyv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 909 WQDNILIPTLTAREHLQlYaqikippggsGGVEEIRSEVAQTLQSLNFGKH-ESYPsWQLSGGYRRRlcVAI--AFIASP 985
Cdd:PRK11144 82 FQDARLFPHYKVRGNLR-Y----------GMAKSMVAQFDKIVALLGIEPLlDRYP-GSLSGGEKQR--VAIgrALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 986 SVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAReiNIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1641-1843 |
1.97e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAVRnVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------QPGISYCPQSNPLDPL 1710
Cdd:PRK10771 7 ITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttppsRRPVSMLFQENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1711 LTTTECIRFyGRLRGIR-------DLDQFLDRV-LDTYELR-PYKdvqvrnLSGGNRRKltVAVTCCGC--TPTVLMDEP 1779
Cdd:PRK10771 86 LTVAQNIGL-GLNPGLKlnaaqreKLHAIARQMgIEDLLARlPGQ------LSGGQRQR--VALARCLVreQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1780 TSDMDPVTRDMVYATIEQLLLARRAVVL-TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
855-1044 |
2.26e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKS----TLIKLLT---GQI-------RQSSGKVLLAGEHQ-----------VGVCW 909
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagGLVqcdkmllRRRSRQVIELSEQSaaqmrhvrgadMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 910 QDNI--LIPTLTAREhlQLYAQIKIPPGGSGgvEEIRSEVAQTLQSLNFGKHES----YPSwQLSGGYRRRLCVAIAFIA 983
Cdd:PRK10261 111 QEPMtsLNPVFTVGE--QIAESIRLHQGASR--EEAMVEAKRMLDQVRIPEAQTilsrYPH-QLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 984 SPSVVILDEPCNGVDAKARKDIWQLIERLRQGRA--VIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
839-1050 |
2.32e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 839 LGASLVNVSKLYGSKCAvSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE------------HQVG 906
Cdd:PRK11288 253 LGEVRLRLDGLKGPGLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQDNI---LIPTLTAREHLQLYAQIKIPPGG---SGGVEEirsEVAQT-LQSLNFgkheSYPSWQ-----LSGGYRRR 974
Cdd:PRK11288 332 LCPEDRKaegIIPVHSVADNINISARRHHLRAGcliNNRWEA---ENADRfIRSLNI----KTPSREqlimnLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 975 lcvAI--AFIASP-SVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1050
Cdd:PRK11288 405 ---AIlgRWLSEDmKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELARE 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
855-1045 |
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 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------------------HQVGvcwqdn 912
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgvayipedrLGRG------ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 iLIPTLTAREHLQLYAQIKiPPGGSGGV---EEIRsEVAQTL--------QSLNfgkhesYPSWQLSGGYRRRLCVAIAF 981
Cdd:COG3845 347 -LVPDMSVAENLILGRYRR-PPFSRGGFldrKAIR-AFAEELieefdvrtPGPD------TPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQ-LIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
843-1045 |
2.56e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLY----GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG----------------E 902
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadalaqlrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 903 HqVGVCWQDNILIPTLTAREHlqlyaqIKIPPGGSGGVEEIRSEVAQTL-QSLNFGKHESYPSWQLSGGYRRRLCVAIAF 981
Cdd:PRK10535 87 H-FGFIFQRYHLLSHLTAAQN------VEVPAVYAGLERKQRLLRAQELlQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYlSDSLVIMRNGRIIA 1045
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVR 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
845-1044 |
2.61e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL------------TGQIR--------QSSGKVLLAGEhq 904
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVynghniysPRTDTVDLRKE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQDNILIPtLTAREH----LQLyAQIKIPPGGSGGVEE------IRSEVAQTLqslnfgkHESypSWQLSGGYRRR 974
Cdd:PRK14239 88 IGMVFQQPNPFP-MSIYENvvygLRL-KGIKDKQVLDEAVEKslkgasIWDEVKDRL-------HDS--ALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 975 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1634-1848 |
2.72e-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: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAY--RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF--------------EQpg 1697
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdlnlrwlrSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1698 ISYCPQsnplDPLL---TTTECIRfYGRLRGIRDLDQ----------FLDRVLDTYelrpykDVQVRN----LSGGNRRK 1760
Cdd:cd03249 79 IGLVSQ----EPVLfdgTIAENIR-YGKPDATDEEVEeaakkanihdFIMSLPDGY------DTLVGErgsqLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1761 LTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLK 1840
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVI-AHRLSTIRN-ADLIAVLQNGQVVEQGTHDELM 225
|
....*...
gi 221500365 1841 SEHGGYYA 1848
Cdd:cd03249 226 AQKGVYAK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1633-1848 |
2.81e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAY-RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpldplL 1711
Cdd:PRK11160 338 SLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA-----L 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 TTTECI---R---FYGRLRGIRDL------DQFLDRVLDTYELRpyKDVQV------------RNLSGGNRRKLTVAVTC 1767
Cdd:PRK11160 413 RQAISVvsqRvhlFSATLRDNLLLaapnasDEALIEVLQQVGLE--KLLEDdkglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1768 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLcQRVAVLRAGQVIASDSPQRLKSEHGGYY 1847
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
.
gi 221500365 1848 A 1848
Cdd:PRK11160 569 Q 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
858-1046 |
2.93e-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: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREHLQl 926
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrRAIGVVPQDTVLFND-TIGYNIR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 YAQIkippggSGGVEEIR--SEVAQ---TLQSLNFGkhesYPS------WQLSGGYRRRLCVAIAFIASPSVVILDEPCN 995
Cdd:cd03253 97 YGRP------DATDEEVIeaAKAAQihdKIMRFPDG----YDTivgergLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 996 GVDAKARKDIWQLIERLRQGRAVIFATH----FMDeakylSDSLVIMRNGRIIAQ 1046
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHrlstIVN-----ADKIIVLKDGRIVER 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1641-1841 |
3.50e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1641 LAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI---------------SYCPQS 1704
Cdd:PRK11831 13 VSFTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlytvrkrmSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 NPLDPLLTTTECIRFygRLRGIRDLDQFLDRV-----LDTYELRPYKDVQVRNLSGGNRRKLTVAvTCCGCTPTVLM-DE 1778
Cdd:PRK11831 93 GALFTDMNVFDNVAY--PLREHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALA-RAIALEPDLIMfDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1779 PTSDMDPVTRDMVYATIEQL--LLARRAVVLtSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELnsALGVTCVVV-SHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1649-1870 |
4.01e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLLTTTEcirfygrlrgiRD 1728
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVH-----------QE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1729 LDQFLDR-VLDTYEL-------------RPYKD---------------VQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1779
Cdd:PRK10982 82 LNLVLQRsVMDNMWLgryptkgmfvdqdKMYRDtkaifdeldididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1780 TSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSEHggyyAVTCFCGpaqqa 1859
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDK----IIAMMVG----- 232
|
250
....*....|.
gi 221500365 1860 ilsRSLNQRLP 1870
Cdd:PRK10982 233 ---RSLTQRFP 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
856-1050 |
4.18e-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: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTLTAREHL 924
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRplsdwsaaelaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYAQikippgGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFI-------ASPSVVILDEPCNGV 997
Cdd:COG4138 91 ALHQP------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 998 DAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRD 1050
Cdd:COG4138 165 DVAQQAALDRLLRELcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
858-1043 |
4.26e-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: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------EH-----QVGVCWQDniliPTLTAREhlql 926
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyEHkylhsKVSLVGQE----PVLFARS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 yAQIKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESYPSW--------QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 998
Cdd:cd03248 104 -LQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 999 AKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRI 1043
Cdd:cd03248 183 AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
845-1052 |
4.27e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.06 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLY-GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL-------TGQIR---QSSGKVLLAG-EHQVGVCWQDN 912
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILidgTDIRTVTRASlRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIpTLTAREHLQLYAqikipPGGSGgvEEIR--SEVAQTL-----QSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 985
Cdd:PRK13657 419 GLF-NRSIEDNIRVGR-----PDATD--EEMRaaAERAQAHdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221500365 986 SVVILDEPCNGVDAKARKDIWQLIERLRQGRavifaTHFMDeAKYLS-----DSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLStvrnaDRILVFDNGRVVESGSFDEL 556
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
855-1045 |
5.46e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE---------------HQVGVCWQDNILIPTLT 919
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvayvpQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHLQLYAQIKIPPggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 999
Cdd:PRK15056 102 MMGRYGHMGWLRRAK------KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1000 KARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLViMRNGRIIA 1045
Cdd:PRK15056 176 KTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLA 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
846-1003 |
5.54e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.89 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 846 VSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI--LIPTLTAREH 923
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLefLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 924 LqlyaqIKIPPggsggvEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:PRK10636 398 L-----ARLAP------QELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
.
gi 221500365 1003 K 1003
Cdd:PRK10636 467 Q 467
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1637-1847 |
5.79e-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: 64.81 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYR-RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQ 1703
Cdd:cd03252 4 EHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladpawlRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPL------------DPLLTTTECI---RFYGRLRGIRDLDQFLDRVLDTyelrpykdvQVRNLSGGNRRKLTVAVTCC 1768
Cdd:cd03252 84 ENVLfnrsirdnialaDPGMSMERVIeaaKLAGAHDFISELPEGYDTIVGE---------QGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1769 GCTPTVLMDEPTSDMD-----PVTRDMvyatieQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:cd03252 155 HNPRILIFDEATSALDyesehAIMRNM------HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
....
gi 221500365 1844 GGYY 1847
Cdd:cd03252 228 GLYA 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1652-1839 |
5.97e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV---GQIYF--------EQPGIS-YCPQSNPLDPLLTTTECIRF 1719
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLngmpidakEMRAISaYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1720 YGRLRGIRDLD-----QFLDRVLDTYELRPYKDV------QVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:TIGR00955 123 QAHLRMPRRVTkkekrERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSHS-VSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
845-998 |
6.55e-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: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEhQVGVCWQDNiliptltAREHL 924
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE-TVKLAYVDQ-------SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 Q----LYAQIkippggSGGVEEIR---SEVA--QTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:TIGR03719 398 DpnktVWEEI------SGGLDIIKlgkREIPsrAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....
gi 221500365 995 NGVD 998
Cdd:TIGR03719 472 NDLD 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1633-1844 |
6.99e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQpdVGQIyfE---------------Q 1695
Cdd:NF033858 1 VARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQ--QGRV--EvlggdmadarhrravC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1696 PGISYCPQ---SNpLDPLLTTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVavtCCGC 1770
Cdd:NF033858 76 PRIAYMPQglgKN-LYPTLSVFENLDFFGRLFGQdaAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL---CCAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1771 --TPTVL-MDEPTSDMDPVTRDMVYATIEQLLlARRA----VVLTSHsVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEH 1843
Cdd:NF033858 152 ihDPDLLiLDEPTTGVDPLSRRQFWELIDRIR-AERPgmsvLVATAY-MEEAER-FDWLVAMDAGRVLATGTPAELLART 228
|
.
gi 221500365 1844 G 1844
Cdd:NF033858 229 G 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1634-1835 |
8.34e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRghYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV----GQIYFEqpGISYCPQS----- 1704
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLLD--GKPVAPCAlrgrk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 ------NP---LDPLLTTTECIRFYGRLRGIRDLDQFL------------DRVLDTYelrPYKdvqvrnLSGGNRRKLTV 1763
Cdd:PRK10418 81 iatimqNPrsaFNPLHTMHTHARETCLALGKPADDATLtaaleavglenaARVLKLY---PFE------MSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1764 AVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRA--VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1835
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLES-IVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
841-1052 |
8.43e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 841 ASLVNVSKLYGskcAVSNL-SLDFA--RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE----------HQVGV 907
Cdd:PRK15439 12 LCARSISKQYS---GVEVLkGIDFTlhAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakaHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 908 CW--QDNILIPTLTAREHLQLyaqikippgGSGGVEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASP 985
Cdd:PRK15439 89 YLvpQEPLLFPNLSVKENILF---------GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 986 SVVILDEPCNGVD-AKARKDIWQLIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRI-----IAQHSRDSL 1052
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIalsgkTADLSTDDI 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
855-1042 |
8.89e-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: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL-----------AGEHQV--------GVCWQDNILI 915
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdggwvdlaqASPREIlalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 916 PTLTAREhlqLYAQikipPGGSGGV--EEIRSEVAQTLQSLNFGKHesypSWQL-----SGGYRRRLCVAIAFIASPSVV 988
Cdd:COG4778 106 PRVSALD---VVAE----PLLERGVdrEEARARARELLARLNLPER----LWDLppatfSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1650-1810 |
9.36e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI---------YFEQPGISYCPQSNPLDPLLTTTECIRFY 1720
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQHRAELDPEKTVMDNLAEGKQEVMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1721 GRLRGIRD-LDQFLdrvldtyeLRPYKDVQ-VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMvyatIEQL 1798
Cdd:PRK11147 415 GRPRHVLGyLQDFL--------FHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL----LEEL 482
|
170
....*....|...
gi 221500365 1799 LLARRA-VVLTSH 1810
Cdd:PRK11147 483 LDSYQGtVLLVSH 495
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1649-1831 |
9.43e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLT--GQLQPDV---GQIYFEQPGIsYCP----------------QSNPL 1707
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYNGHNI-YSPrtdtvdlrkeigmvfqQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DplLTTTECIRFYGRLRGIRD---LDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDE 1778
Cdd:PRK14239 99 P--MSIYENVVYGLRLKGIKDkqvLDEAVEKSLKGASI--WDEVKDRlhdsalGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1779 PTSDMDPVTRDMvyatIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK14239 175 PTSALDPISAGK----IEETLLGLKddyTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
858-1038 |
1.00e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI--RQSSGKVllagEHQVGVCWQDNILIptltarEHlqlyaqikIPPG 935
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----DVPDNQFGREASLI------DA--------IGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 936 GSggveeirseVAQTLQSLNFGKHESYPSW-----QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVD---AKARKDIWQ 1007
Cdd:COG2401 110 GD---------FKDAVELLNAVGLSDAVLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQ 180
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 1008 LIERlRQGRAVIFATHFMDEAKYLSDSLVIM 1038
Cdd:COG2401 181 KLAR-RAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1650-1810 |
1.14e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-----------QPGISYCPQSNPLDPLLTTTE-C- 1716
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsikkdlctyQKQLCFVGHRSGINPYLTLREnCl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 --IRFYGRLRGIrdldqflDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1794
Cdd:PRK13540 97 ydIHFSPGAVGI-------TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*.
gi 221500365 1795 IEQLLLARRAVVLTSH 1810
Cdd:PRK13540 170 IQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1634-1839 |
1.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGH--YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE--------------QPG 1697
Cdd:PRK13642 5 LEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgelltaenvwnlrrKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1698 ISYcpqSNPLDPLL--TTTECIRFYGRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPT 1773
Cdd:PRK13642 85 MVF---QNPDNQFVgaTVEDDVAFGMENQGIprEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1774 VLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1650-1833 |
1.22e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQ-----LQPDV-------GQIYFEQpgIS-YCPQSNPLDPLLTTTEC 1716
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggyIEGDIrisgfpkKQETFAR--ISgYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 IRFYGRLRGIRDLDQ-----FLDRVLDTYELRPYKDVQV-----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPV 1786
Cdd:PLN03140 974 LIYSAFLRLPKEVSKeekmmFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1787 TRDMVYATIEQLLLARRAVVLTSH--SVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:PLN03140 1054 AAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYS 1102
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
842-1043 |
1.27e-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: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKC-AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG---------EHQVGVCWQD 911
Cdd:PRK11650 5 KLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepaDRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAREHLQlYAqIKIppggsGGV--EEIRSEVAQTLQSLNFGKH-ESYPSwQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:PRK11650 85 YALYPHMSVRENMA-YG-LKI-----RGMpkAEIEERVAEAARILELEPLlDRKPR-ELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 989 ILDEPCNGVDAKARK----DIWQLIERLRQgrAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK11650 157 LFDEPLSNLDAKLRVqmrlEIQRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
843-1045 |
1.34e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTARE 922
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-----------IDFKSSKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 923 HLQlyaqikippggsGGVEEIRSEVAQTLQ-----SLNFGKhesYPS-------------------------------WQ 966
Cdd:PRK10982 70 ALE------------NGISMVHQELNLVLQrsvmdNMWLGR---YPTkgmfvdqdkmyrdtkaifdeldididprakvAT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 967 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1649-1833 |
1.52e-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: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPD---VGQIYF-------------EQPGISYCPQSNPLDPLLT 1712
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWsgsplkasnirdtERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIrFYGR---LRGIR-DLDQFLDR---VLDTYELRPYKDVQ-VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1784
Cdd:TIGR02633 95 VAENI-FLGNeitLPGGRmAYNAMYLRaknLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221500365 1785 PVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1646-1842 |
1.73e-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: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDvGQIYFEqpGISYcpQSNPLDPL-----LTTTECIRFY 1720
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQID--GVSW--NSVPLQKWrkafgVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1721 GRLRGIRD-----LDQFLDRVLDTYELR------PYK-DVQVRN----LSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1784
Cdd:cd03289 91 GTFRKNLDpygkwSDEEIWKVAEEVGLKsvieqfPGQlDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1785 PVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1842
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 ... |
1652-1831 |
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 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLL---------TGQLQPDvGQ---IYFeQPGISYCPQSNPLDPLLTTTECIRF 1719
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLagrktagviTGEILIN-GRpldKNF-QRSTGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1720 YGRLRGirdldqfldrvldtyelrpykdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL 1799
Cdd:cd03232 103 SALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170 180 190
....*....|....*....|....*....|....
gi 221500365 1800 LARRAVVLTSHSVSE-IEHLCQRVAVL-RAGQVI 1831
Cdd:cd03232 156 DSGQAILCTIHQPSAsIFEKFDRLLLLkRGGKTV 189
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1652-1817 |
1.88e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGEcFGLL-GKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI------------SYCPQSnpldPLL---TTTE 1715
Cdd:PRK10247 25 NISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeiyrqqvSYCAQT----PTLfgdTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFYGRLRGIR-DLDQFLDRvLDTYELrPYKDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVY 1792
Cdd:PRK10247 100 NLIFPWQIRNQQpDPAIFLDD-LERFAL-PDTILTknIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180
....*....|....*....|....*.
gi 221500365 1793 ATIEQLLLARR-AVVLTSHSVSEIEH 1817
Cdd:PRK10247 178 EIIHRYVREQNiAVLWVTHDKDEINH 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1647-1830 |
1.90e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1647 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGiSYCPQSNPLDPLLTTTECIRFYGRLRGI 1726
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-ALIAISSGLNGQLTGIENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1727 --RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTcCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARR 1803
Cdd:PRK13545 116 tkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAIS-VHINPDILvIDEALSVGDQTFTKKCLDKMNEFKEQGK 194
|
170 180
....*....|....*....|....*..
gi 221500365 1804 AVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK13545 195 TIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1648-1830 |
1.92e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1648 YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPLLTTTECIRFYGRLRGI 1726
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--DRNGeVSVIAISAGLSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1727 --RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRA 1804
Cdd:PRK13546 116 krKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKT 195
|
170 180
....*....|....*....|....*.
gi 221500365 1805 VVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK13546 196 IFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1657-1824 |
2.01e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1657 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqPGISYCPQSNPLDPLLTTTECirfygrLRGIRdlDQFLDRV 1736
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIKPDYDGTVEDL------LRSIT--DDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1737 LDTYELRPYK-----DVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLT-SH 1810
Cdd:PRK13409 433 YKSEIIKPLQlerllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVvDH 512
|
170
....*....|....
gi 221500365 1811 SVSEIEHLCQRVAV 1824
Cdd:PRK13409 513 DIYMIDYISDRLMV 526
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1634-1830 |
2.16e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------- 1704
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrrqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 -----------------NPLDPLL---TTTECIRfygrlrgiRDLDQFLDRV--LDTYELRPYKdvqvrnLSGGNRRKLT 1762
Cdd:PRK10908 82 gmifqdhhllmdrtvydNVAIPLIiagASGDDIR--------RRVSAALDKVglLDKAKNFPIQ------LSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1763 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
867-1041 |
2.38e-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: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 867 QVSCLLGRNGAGKSTLIKLL---------TGQIRQSSGKVLLAG-EHQVGVCWQDNILIPTLTAREHLQLYAQIKIPpgG 936
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaervttgviTGGDRLVNGRPLDSSfQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQP--K 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 937 SGGVEEIRSEVAQTLQSLNFgkhESY-------PSWQLSGGYRRRLCVAIAFIASP-SVVILDEPCNGVDAKARKDIWQL 1008
Cdd:TIGR00956 868 SVSKSEKMEYVEEVIKLLEM---ESYadavvgvPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKL 944
|
170 180 190
....*....|....*....|....*....|....*....
gi 221500365 1009 IERL-RQGRAVIFATH-----FMDEAkylsDSLVIMRNG 1041
Cdd:TIGR00956 945 MRKLaDHGQAILCTIHqpsaiLFEEF----DRLLLLQKG 979
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1650-1839 |
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 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLT-------GQLQPDVGQIYF-------------EQPGISYcPQSNPLdP 1709
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFgkdifqidaiklrKEVGMVF-QQPNPF-P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIRFYGRLRGI---RDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDEPT 1780
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIkekREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1781 SDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK14246 182 SMIDIVNSQAIEKLITE-LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
845-1046 |
2.98e-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: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLL-------TGQIR-------------QSSGKVLlAGEHQ 904
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRvgditidtarslsQQKGLIR-QLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 905 VGVCWQDNILIPTLTAREH-LQLYAQIKIPPGGSGgVEEIRSEVAQTLQSlnfGKHESYPSwQLSGGYRRRLCVAIAFIA 983
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEA-TARARELLAKVGLA---GKETSYPR-RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 984 SPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
842-1055 |
3.07e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYG-SKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQD-NILIPTLT 919
Cdd:PRK10522 324 ELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 920 AREHL--QLYaqikippgGSGGVEEIRSEVAQTLQSLNFG-----KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:PRK10522 404 TDFHLfdQLL--------GPEGKPANPALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 993 PCNGVDAKARKDIWQ-LIERLRQGRAVIFAT----HFMDEAkylsDSLVIMRNGRI-------IAQHSRDSLQRL 1055
Cdd:PRK10522 476 WAADQDPHFRREFYQvLLPLLQEMGKTIFAIshddHYFIHA----DRLLEMRNGQLseltgeeRDAASRDAVART 546
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
871-1044 |
3.17e-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: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIR---QSSGKVLLAG----------EHQVGVCWQDNILIPTLTAREHLQLYAQIKippggs 937
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGipykefaekyPGEIIYVSEEDVHFPTLTVRETLDFALRCK------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 938 gGVEEIRSevaqtlqslnfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGR 1016
Cdd:cd03233 112 -GNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDVLK 169
|
170 180 190
....*....|....*....|....*....|
gi 221500365 1017 AVIFATHFM--DEAKYLSDSLVIMRNGRII 1044
Cdd:cd03233 170 TTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
859-1051 |
3.76e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 859 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGqIRQSSGKVLLAGE------------HQVGVCWQDN--ILIPTLtarEHL 924
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQpleawsaaelarHRAYLSQQQTppFAMPVF---QYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 QLYaqikIPPGGSggVEEIRSEVAQTLQSLNFGKHESYPSWQLSGG--YRRRL---CVAIAFIASPS--VVILDEPCNGV 997
Cdd:PRK03695 91 TLH----QPDKTR--TEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLaavVLQVWPDINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 998 DAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDS 1051
Cdd:PRK03695 165 DVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1653-1837 |
3.97e-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: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1653 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPDVGQIYFEQPGIS------------YCPQSNPLDPLLTTTECIRFY 1720
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSdwsaaelarhraYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1721 GRLRGIRD-LDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTV-------LMDEPTSDMDPVTRDMVY 1792
Cdd:COG4138 94 QPAGASSEaVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegqllLLDEPMNSLDVAQQAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 1793 ATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQ 1837
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
856-1055 |
4.65e-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: 64.38 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLL------------AGEHqVGVCWQD----------NI 913
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreeLGRH-IGYLPQDvelfdgtiaeNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 914 liptltAR------EHLQLYAQI--------KIPPG-----GSGGVeeirsevaqtlqslnfgkhesypswQLSGGYRRR 974
Cdd:COG4618 427 ------ARfgdadpEKVVAAAKLagvhemilRLPDGydtriGEGGA-------------------------RLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 975 LCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ-GRAVIFATH---FMDEAkylsDSLVIMRNGRIIAQHSRD 1050
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHrpsLLAAV----DKLLVLRDGRVQAFGPRD 551
|
....*.
gi 221500365 1051 S-LQRL 1055
Cdd:COG4618 552 EvLARL 557
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1628-1811 |
5.41e-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: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------Q 1695
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdevR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1696 PGISYCPQsnplDP-LLTTT--ECIRFyGR-----------LRGIRdLDQFLDRVLDTYELRPYKDvqVRNLSGGNRRKL 1761
Cdd:TIGR02868 409 RRVSVCAQ----DAhLFDTTvrENLRL-ARpdatdeelwaaLERVG-LADWLRALPDGLDTVLGEG--GARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1762 TVAVTCCGCTPTVLMDEPTSDMDPVTRDmvyATIEQLL--LARRAVVLTSHS 1811
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETAD---ELLEDLLaaLSGRTVVLITHH 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1652-1784 |
6.55e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF-EQPGISYCPQS-NPLDPLLTTTECIRfyGRLRGIRdl 1729
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQSrDALDPNKTVWEEIS--GGLDIIK-- 417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1730 dqfldrvLDTYEL--RPY--------KDVQ--VRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMD 1784
Cdd:PRK11819 418 -------VGNREIpsRAYvgrfnfkgGDQQkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
855-1052 |
6.72e-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: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwQDnilIPTLTAREHLQLYAQIKI-- 932
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG--------QD---ITGLSGRELRPLRRRMQMvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 933 --PPG-------------------GSGGVEEIRSEVAQTLQS--LNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:COG4608 102 qdPYAslnprmtvgdiiaeplrihGLASKAERRERVAELLELvgLRPEHADRYPH-EFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1628-1839 |
8.45e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAVRAENLWLAY--RRG--------HYAVRNVNFSVQRGECFGLLGKNGAGKST----IFKLLTGQ------LQPD 1687
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpiRKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1688 VG-------------QIYFEQPGISYCPQsnpLDPLLTTTECIRFYGRLRGIRDLDQFLDRVLDTYELRPykDVQVR--- 1751
Cdd:PRK15134 350 HNlnrrqllpvrhriQVVFQDPNSSLNPR---LNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP--ETRHRypa 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1752 NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARR-AVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
....*....
gi 221500365 1831 IASDSPQRL 1839
Cdd:PRK15134 505 VEQGDCERV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1644-1830 |
9.06e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1644 RRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSnPLDPLLT----TTECIR- 1718
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN--GKDISPRS-PLDAVKKgmayITESRRd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 --FY-----------------GRLRGIRDLdqFLDRVLDTYELRPYKDVQVR---------NLSGGNRRKLTVAVTCCgC 1770
Cdd:PRK09700 350 ngFFpnfsiaqnmaisrslkdGGYKGAMGL--FHEVDEQRTAENQRELLALKchsvnqnitELSGGNQQKVLISKWLC-C 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1771 TPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK09700 427 CPEVIIfDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
842-1052 |
9.71e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.52 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNIL------- 914
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAR-----EHLQLYAQIKIppggsggveeIRSEVAQTLQSLNFGKHES--------------------YPSwQLSG 969
Cdd:PRK10619 87 LRLLRTRltmvfQHFNLWSHMTV----------LENVMEAPIQVLGLSKQEAreravkylakvgideraqgkYPV-HLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 970 GYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS 1048
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....
gi 221500365 1049 RDSL 1052
Cdd:PRK10619 236 PEQL 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1609-1692 |
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 221500365 1609 LDKLGQLKLVNIQSIFK--SCVDTGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQP 1686
Cdd:PRK10522 296 FNKLNKLALAPYKAEFPrpQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
....*.
gi 221500365 1687 DVGQIY 1692
Cdd:PRK10522 376 QSGEIL 381
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
843-1023 |
1.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE--------HQVGVCW--QDN 912
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctYQKQLCFvgHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 913 ILIPTLTAREHlqLYAQIKIPPGGSGGVEEIRsevaqtlqSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDE 992
Cdd:PRK13540 84 GINPYLTLREN--CLYDIHFSPGAVGITELCR--------LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 221500365 993 PCNGVDAKARKDIWQLIERLR-QGRAVIFATH 1023
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRaKGGAVLLTSH 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1648-1837 |
1.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1648 YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISycPQS-------------NPLDPLLTTT 1714
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT--DDNfeklrkhigivfqNPDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 ecIRF---YG---RLRGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:PRK13648 101 --VKYdvaFGlenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1789 DMVYATIEQLLLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQ 1837
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTPT 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1656-1817 |
1.37e-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: 63.26 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1656 SVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPgISYCPQSNPLDPLLTTTECIR-----------FYGRLr 1724
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISYKPQYISPDYDGTVEEFLRsantddfgssyYKTEI- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1725 gIRDLDqfLDRVLDTYelrpykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRA 1804
Cdd:COG1245 440 -IKPLG--LEKLLDKN---------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
170
....*....|...
gi 221500365 1805 VVLTshsvseIEH 1817
Cdd:COG1245 508 TAMV------VDH 514
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
845-1044 |
2.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKC-----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQ--------VGVCWQD 911
Cdd:PRK13651 7 NIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkeKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 912 NILIPTLTAR------------------EHlQLYAQ-----IKIPPGGSGGVEEIRSEVAQTLQSLnFGKHESY---PSW 965
Cdd:PRK13651 87 LVIQKTRFKKikkikeirrrvgvvfqfaEY-QLFEQtiekdIIFGPVSMGVSKEEAKKRAAKYIEL-VGLDESYlqrSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 966 QLSGGYRRRlcVAIAFIAS--PSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
Cdd:PRK13651 165 ELSGGQKRR--VALAGILAmePDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
..
gi 221500365 1043 II 1044
Cdd:PRK13651 243 II 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1652-1815 |
2.42e-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: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLqpDVGQIYFE-------------QPGISYCPQSNPLDPLLTTTECIR 1718
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGdrlvngrpldssfQRSIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1719 FYGRLR-----GIRDLDQFLDRVLDTYELRPYKDVQV----RNLSGGNRRKLTVAVTCCGcTPTVL--MDEPTSDMDPVT 1787
Cdd:TIGR00956 859 FSAYLRqpksvSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVA-KPKLLlfLDEPTSGLDSQT 937
|
170 180
....*....|....*....|....*...
gi 221500365 1788 RDMVYATIEQLLLARRAVVLTSHSVSEI 1815
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIHQPSAI 965
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
812-1043 |
2.75e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 812 VIGLAYQRYKKNNYSFVKVSRSQLDGKLGASLVNVSKLYGSKcaVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR 891
Cdd:PRK09700 237 IVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 892 QSSGKVLLAGEH----------QVGVCW-----QDNILIPTLTAREHLQLYAQIKIppGGSGG-------VEEIR-SEVA 948
Cdd:PRK09700 315 RAGGEIRLNGKDisprspldavKKGMAYitesrRDNGFFPNFSIAQNMAISRSLKD--GGYKGamglfheVDEQRtAENQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 949 QTLQSLNFGKHESYPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDE 1027
Cdd:PRK09700 393 RELLALKCHSVNQNIT-ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPE 471
|
250
....*....|....*.
gi 221500365 1028 AKYLSDSLVIMRNGRI 1043
Cdd:PRK09700 472 IITVCDRIAVFCEGRL 487
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1660-1810 |
3.06e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1660 GECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI---------YFEQPGISYC-PQSNPLDPLLTTTEcirfygrlrgiRDL 1729
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLrADESPLQHLARLAP-----------QEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1730 DQFLDRVLDTYELRPYKDVQV-RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtRDMVYATIEQLLLARRAVVLT 1808
Cdd:PRK10636 407 EQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD---LDMRQALTEALIDFEGALVVV 483
|
..
gi 221500365 1809 SH 1810
Cdd:PRK10636 484 SH 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1634-1831 |
3.13e-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: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENL--WLAYRRG--------HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFK-LLtgQLQPDVGQIYFEQPGISYCP 1702
Cdd:COG4172 276 LEARDLkvWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLL--RLIPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QS--------------NP---LDPLLTTTECI----RFYGRLRGIRDLDQFLDRVLDTYELRPykdvQVRN-----LSGG 1756
Cdd:COG4172 354 RRalrplrrrmqvvfqDPfgsLSPRMTVGQIIaeglRVHGPGLSAAERRARVAEALEEVGLDP----AARHrypheFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1757 NR------RKLTVAvtccgctPTVLM-DEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAV 1824
Cdd:COG4172 430 QRqriaiaRALILE-------PKLLVlDEPTSALD-VS---VQAQILDLLrdLQREhglAYLFISHDLAVVRALAHRVMV 498
|
....*..
gi 221500365 1825 LRAGQVI 1831
Cdd:COG4172 499 MKDGKVV 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1634-1831 |
3.24e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGI-SYCPQSNP------ 1706
Cdd:PRK11147 4 ISIHGAWLSFSD-APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvARLQQDPPrnvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1707 ---------------------LDPLLTTTECIRFYGRLRGIRD-LD-----QFLDR---VLDTYELRPykDVQVRNLSGG 1756
Cdd:PRK11147 83 vydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQEqLDhhnlwQLENRineVLAQLGLDP--DAALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1757 NRRKLTVA---VtccgCTPTVLM-DEPTSDMDPVTRDMvyatIEQLLLA-RRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
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 ... |
842-999 |
3.77e-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: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAV-SNLSLDF---ARNQVsclLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT 917
Cdd:TIGR03719 6 TMNRVSKVVPPKKEIlKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHL---------------QLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNFGKHESY----------PSW-----QL 967
Cdd:TIGR03719 83 KTVRENVeegvaeikdaldrfnEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQleiamdalrcPPWdadvtKL 162
|
170 180 190
....*....|....*....|....*....|..
gi 221500365 968 SGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 999
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1649-1842 |
3.78e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLL----------------- 1711
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgvvfqfpesqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 TTTECIRFYGRLRGI--RDLDQFLDRVLDTYEL-RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTR 1788
Cdd:PRK13643 101 TVLKDVAFGPQNFGIpkEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1789 DMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1649-1791 |
4.07e-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: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP------------QsnplDPLLTTTEC 1716
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeykrakyigrvfQ----DPMMGTAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 I-----------RfyGRLRGIR------DLDQFLDRvLDTYEL----RPykDVQVRNLSGGNRRKLTVaVTCCGCTPTVL 1775
Cdd:COG1101 97 MtieenlalayrR--GKRRGLRrgltkkRRELFREL-LATLGLglenRL--DTKVGLLSGGQRQALSL-LMATLTKPKLL 170
|
170
....*....|....*..
gi 221500365 1776 M-DEPTSDMDPVTRDMV 1791
Cdd:COG1101 171 LlDEHTAALDPKTAALV 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1629-1830 |
4.92e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAV-RAENL--WLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGK----STIFKLLTGQLQpdvGQIYFE-QP---- 1696
Cdd:PRK13549 254 TIGEVIlEVRNLtaWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRWE---GEIFIDgKPvkir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 --------GISYCPQSNPLD---PLLTTTECI------RFYGRLR-----GIRDLDQFLDRvldtyeLR---PYKDVQVR 1751
Cdd:PRK13549 331 npqqaiaqGIAMVPEDRKRDgivPVMGVGKNItlaaldRFTGGSRiddaaELKTILESIQR------LKvktASPELAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1752 NLSGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK13549 405 RLSGGNQQKAVLA-KCLLLNPKILiLDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1630-1868 |
5.91e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1630 TGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QP 1696
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDdcdvakfgltdlRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 GISYCPQSnpldPLLtttecirFYGRLRgiRDLDQF-----------LDR--VLDTYELRPYK-DVQV----RNLSGGNR 1758
Cdd:PLN03232 1311 VLSIIPQS----PVL-------FSGTVR--FNIDPFsehndadlweaLERahIKDVIDRNPFGlDAEVseggENFSVGQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1759 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQR 1838
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI-AHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
250 260 270
....*....|....*....|....*....|.
gi 221500365 1839 LKSEHG-GYYAVTCFCGPAQQAILSRSLNQR 1868
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) ... |
862-1037 |
7.48e-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: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 862 DFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgVCWQDNILIPTLTAREHLQLYAQIKippgGSGGVE 941
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---VSYKPQYIKADYEGTVRDLLSSITK----DFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 942 EIRSEVAQTLQSLNFGKHESYpswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR----KDIWQLIERLRQGRA 1017
Cdd:cd03237 94 YFKTEIAKPLQIEQILDREVP---ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNEKTAF 170
|
170 180
....*....|....*....|
gi 221500365 1018 VIFATHFMdeAKYLSDSLVI 1037
Cdd:cd03237 171 VVEHDIIM--IDYLADRLIV 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1634-1830 |
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 221500365 1634 VRAENLWLAYRR--GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE----------------- 1694
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpisqyehkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1695 -------------QPGISYCPQSNPLDpllTTTECIRFYGRLRGIRDLdqfldrvldtyELRPYKDVQVRN--LSGGNRR 1759
Cdd:cd03248 92 lvgqepvlfarslQDNIAYGLQSCSFE---CVKEAAQKAHAHSFISEL-----------ASGYDTEVGEKGsqLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1760 KLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVyatiEQLL---LARRAVVLTSHSVSEIEHlCQRVAVLRAGQV 1830
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQV----QQALydwPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
966-1052 |
8.25e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 966 QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
....*...
gi 221500365 1045 AQHSRDSL 1052
Cdd:PRK13549 485 GDLINHNL 492
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1650-1818 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPlLTTTECIRFygrlrGIrD 1728
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGrISFSSQFSWIMP-GTIKENIIF-----GV-S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1729 LDQFLDR-VLDTYELR------PYKDVQVR-----NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIE 1796
Cdd:cd03291 124 YDEYRYKsVVKACQLEeditkfPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV 203
|
170 180
....*....|....*....|..
gi 221500365 1797 QLLLARRAVVLTShsvSEIEHL 1818
Cdd:cd03291 204 CKLMANKTRILVT---SKMEHL 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
855-1044 |
1.09e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHqvgvcwqdnilIPTLTA------REHLQL-- 926
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR-----------IDTLSPgklqalRRDIQFif 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 ---YAQIK---------IPP---GGSGGVEEIRSEVAQTLQSLNFGKHES--YPSwQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:PRK10261 408 qdpYASLDprqtvgdsiMEPlrvHGLLPGKAAAARVAWLLERVGLLPEHAwrYPH-EFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1625-1842 |
1.11e-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: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1625 KSCVDTGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDvGQIYFEqpGISYcpQ 1703
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQID--GVSW--N 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 SNPLDPL-----LTTTECIRFYGRLRGIRD-----LDQFLDRVLDTYELR------PYK-DVQVRN----LSGGNRRKLT 1762
Cdd:TIGR01271 1284 SVTLQTWrkafgVIPQKVFIFSGTFRKNLDpyeqwSDEEIWKVAEEVGLKsvieqfPDKlDFVLVDggyvLSNGHKQLMC 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1763 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
865-1023 |
1.47e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDniliPTLTAR---------------EHLQLYAQ 929
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQD----PPRNVEgtvydfvaegieeqaEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 930 IkippggSGGVEEIRSE------------------------VAQTLQSLNFGKHESYPSwqLSGGYRRRLCVAIAFIASP 985
Cdd:PRK11147 104 I------SHLVETDPSEknlnelaklqeqldhhnlwqlenrINEVLAQLGLDPDAALSS--LSGGWLRKAALGRALVSNP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 986 SVVILDEPCNGVDAKArkdiwqlIERLR------QGrAVIFATH 1023
Cdd:PRK11147 176 DVLLLDEPTNHLDIET-------IEWLEgflktfQG-SIIFISH 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
871-1006 |
1.59e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDN--ILIPTLT-----AREHLQLYAQIKIPPGGSGG---- 939
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpaLPQPALEyvidgDREYRQLEAQLHDANERNDGhaia 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 940 ----------VEEIRSEVAQTLQSLNFGKHE-SYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARkdIW 1006
Cdd:PRK10636 112 tihgkldaidAWTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV--IW 187
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
605-744 |
1.60e-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: 58.56 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 605 DVFKRGLYLAQGVQVAYLLGLVVFVALS------VRERIWMRESRNSMLMRSMGLKAHSELVAWALMSFLeLCVIFALIS 678
Cdd:pfam12698 146 PVESTPLFNPQSGYAYYLVGLILMIIILigaaiiAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLII 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 679 GVLYSGGILGYTNWFFMMFYCLSFGLCLISFCYMCTNFFNSAnIGAVASALLFFISLCPFIIVLMF 744
Cdd:pfam12698 225 LLLLFGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNS-EDAQSIIGIVILLLSGFFGGLFP 289
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1616-1810 |
1.61e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1616 KLVNIQSIFKSCVDTGEAVR--AENLWLAYRRGH-YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY 1692
Cdd:COG2401 9 VLMRVTKVYSSVLDLSERVAivLEAFGVELRVVErYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1693 FEQPgisycpqSNPLDPLLTTTECIrfyGRLRGIRDLDQFLDRV--LDTYE-LRPYKdvqvrNLSGGNRRKLTVAVTCCG 1769
Cdd:COG2401 89 VDVP-------DNQFGREASLIDAI---GRKGDFKDAVELLNAVglSDAVLwLRRFK-----ELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 1770 CTPTVLMDEPTSDMDPVTRDMVYATIeqLLLARRA----VVLTSH 1810
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNL--QKLARRAgitlVVATHH 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1650-1831 |
1.63e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGISYCPQS-------------NPLdPLL 1711
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIelrrrvqmvfqipNPI-PNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 TTTECIRFYGRLRGI----RDLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:PRK14247 98 SIFENVALGLKLNRLvkskKELQERVRWALEKAQL--WDEVKDRldapagKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1782 DMDPVTRdmvyATIEQLLLARR---AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK14247 176 NLDPENT----AKIESLFLELKkdmTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1642-1784 |
1.79e-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: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1642 AYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGIS--YCPQSNPLDPLLTTTECI-- 1717
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIKvgYLPQEPQLDPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1718 ----------RF--------------------YGRLRGI------RDLDQFLDRVLDTyeLR-PYKDVQVRNLSGGNRRK 1760
Cdd:TIGR03719 92 gvaeikdaldRFneisakyaepdadfdklaaeQAELQEIidaadaWDLDSQLEIAMDA--LRcPPWDADVTKLSGGERRR 169
|
170 180 190
....*....|....*....|....*....|
gi 221500365 1761 ltVAVtccgC-----TPTV-LMDEPTSDMD 1784
Cdd:TIGR03719 170 --VAL----CrlllsKPDMlLLDEPTNHLD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1651-1815 |
1.82e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1651 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTECIRFY 1720
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppAERGVGMVFQSYALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1721 GRLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGcTPTV-LMDEPTSDMDPVTR--------- 1788
Cdd:PRK11000 100 LKLAGAkkEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA-EPSVfLLDEPLSNLDAALRvqmrieisr 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 221500365 1789 -------DMVYAT---IEQLLLARRAVVLTSHSVSEI 1815
Cdd:PRK11000 179 lhkrlgrTMIYVThdqVEAMTLADKIVVLDAGRVAQV 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
858-1052 |
1.97e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAG------EH-----QVGVCWQ----------DNILIp 916
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyDHhylhrQVALVGQepvlfsgsvrENIAY- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 917 TLTAREHLQLYAQIKippggSGGVEEIRSEVAQTLQSlNFGKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:TIGR00958 578 GLTDTPDEEIMAAAK-----AANAHDFIMEFPNGYDT-EVGEKGS----QLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 997 VDAKARKDIWQLieRLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:TIGR00958 648 LDAECEQLLQES--RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
845-998 |
2.22e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLaGEhQVGVCWQDNiliptltAREHL 924
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-TVKLAYVDQ-------SRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 925 Q----LYAQIkippggSGGVEEI---------RSEVAqtlqSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVIL 990
Cdd:PRK11819 400 DpnktVWEEI------SGGLDIIkvgnreipsRAYVG----RFNFkGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
....*...
gi 221500365 991 DEPCNGVD 998
Cdd:PRK11819 470 DEPTNDLD 477
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1652-1839 |
2.45e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPGISYCPQSNPLDPLLTTTECIRFYG 1721
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgedvthrsiQQRDICMVFQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1722 RLRGI--RDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCgCTPTVLM-DEPTSDMDPVTRDMVYATIEQL 1798
Cdd:PRK11432 104 KMLGVpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI-LKPKVLLfDEPLSNLDANLRRSMREKIREL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221500365 1799 llaRRAVVLTS----HSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK11432 183 ---QQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1643-1818 |
2.60e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1643 YRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIY---------FEQPGISYCPQSNplDPLLTT 1713
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavFSQHHVDGLDLSS--NPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1714 TECirFYG----RLRGirDLDQFldRVLDTYELRPykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpvtRD 1789
Cdd:PLN03073 596 MRC--FPGvpeqKLRA--HLGSF--GVTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LD 661
|
170 180
....*....|....*....|....*....
gi 221500365 1790 MVYATIEQLLLARRAVVLTSHSvseiEHL 1818
Cdd:PLN03073 662 AVEALIQGLVLFQGGVLMVSHD----EHL 686
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1649-1848 |
2.81e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.82 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNpL---------DPLL---TTTEC 1716
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS-LrrniavvfqDAGLfnrSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 IRFyGR-------LRGIRDLDQ---FLDRVLDTYelrpykDVQV----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:PRK13657 429 IRV-GRpdatdeeMRAAAERAQahdFIERKPDGY------DTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLkSEHGGYYA 1848
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFII-AHRLSTVRN-ADRILVFDNGRVVESGSFDEL-VARGGRFA 564
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1650-1833 |
2.81e-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: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV--GQIYFE-------------QPGISYCPQSNPldpllttt 1714
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKgeditdlppeeraRLGIFLAFQYPP-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 ecirfygRLRGIRDLDqFLdrvldtyelrpyKDVQVrNLSGGNRRK---LTVAVTccgcTPT-VLMDEPTSDMDPVTRDM 1790
Cdd:cd03217 88 -------EIPGVKNAD-FL------------RYVNE-GFSGGEKKRneiLQLLLL----EPDlAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1791 VYATIEQLLLARRAVVLTSHSVSEIEHL-CQRVAVLRAGQVIAS 1833
Cdd:cd03217 143 VAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
831-998 |
2.83e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 831 SRSqldGKLGASLVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehQVG---- 906
Cdd:PRK11147 313 SRS---GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------HCGtkle 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 907 VCWQDN---ILIPTLTAREHLqlyaqikippggSGGVEEI-----RSEVAQTLQSLNFG-KHESYPSWQLSGGYRRRLCV 977
Cdd:PRK11147 384 VAYFDQhraELDPEKTVMDNL------------AEGKQEVmvngrPRHVLGYLQDFLFHpKRAMTPVKALSGGERNRLLL 451
|
170 180
....*....|....*....|.
gi 221500365 978 AIAFIASPSVVILDEPCNGVD 998
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1664-1784 |
3.00e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1664 GLLGKNGAGKSTIFKLLTGQLQPDVGQIYFeQPGIS--YCPQSNPLDPLLTTTECI------------RF---------- 1719
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIKvgYLPQEPQLDPEKTVRENVeegvaevkaaldRFneiyaayaep 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1720 ----------YGRLRGI------RDLDQFLDRVLDTyeLR-PYKDVQVRNLSGGNRRKltVAVtccgC-----TPTV-LM 1776
Cdd:PRK11819 116 dadfdalaaeQGELQEIidaadaWDLDSQLEIAMDA--LRcPPWDAKVTKLSGGERRR--VAL----CrllleKPDMlLL 187
|
....*...
gi 221500365 1777 DEPTSDMD 1784
Cdd:PRK11819 188 DEPTNHLD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1629-1833 |
3.08e-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: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1629 DTGEAV-RAENL--WLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQLQpdvGQIYFEQ------ 1695
Cdd:TIGR02633 252 EIGDVIlEARNLtcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTelvqALFGAYPGKFE---GNVFINGkpvdir 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1696 -------PGISYCPQSNPLD---PLLTTTECI------RFYGRLRgirdLD-----QFLDRVLDTYELRPYK-DVQVRNL 1753
Cdd:TIGR02633 329 npaqairAGIAMVPEDRKRHgivPILGVGKNItlsvlkSFCFKMR----IDaaaelQIIGSAIQRLKVKTASpFLPIGRL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1754 SGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:TIGR02633 405 SGGNQQKAVLA-KMLLTNPRVLiLDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
.
gi 221500365 1833 S 1833
Cdd:TIGR02633 484 D 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1650-1818 |
4.40e-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: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPG-ISYCPQSNPLDPlLTTTECIRFygrlrGIrD 1728
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGrISFSPQTSWIMP-GTIKDNIIF-----GL-S 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1729 LDQFLDR-VLDTYELR------PYKDVQVR-----NLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT-RDMVYATI 1795
Cdd:TIGR01271 513 YDEYRYTsVIKACQLEedialfPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESCL 592
|
170 180
....*....|....*....|...
gi 221500365 1796 EQLLLARRAVVLTshsvSEIEHL 1818
Cdd:TIGR01271 593 CKLMSNKTRILVT----SKLEHL 611
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
856-1052 |
4.42e-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: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-QSSGKVLLAGeHQV-----------GVCW------QDNIlIPT 917
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING-KPVdirnpaqairaGIAMvpedrkRHGI-VPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHLQLYAQIKIPPGGSGGVEEIRSEVAQTLQSLNF-GKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNG 996
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 997 VDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL 490
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
868-1044 |
5.26e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 868 VSCLLGRNGAGKSTLIKLLTGqiRQSSGKVllAGEHQV--------------GVCWQDNILIPTLTAREHLQLYAQIKIP 933
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDIRIsgfpkkqetfarisGYCEQNDIHSPQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 934 PGGSGgvEEIRSEVAQTLQSLNFGKHES----YPSWQ-LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQL 1008
Cdd:PLN03140 984 KEVSK--EEKMMFVDEVMELVELDNLKDaivgLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190
....*....|....*....|....*....|....*....
gi 221500365 1009 IER-LRQGRAVIFATH--FMDEAKYLSDSLVIMRNGRII 1044
Cdd:PLN03140 1062 VRNtVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVI 1100
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1636-1814 |
7.06e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.86 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1636 AENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE---------QPGISYcpQSNP 1706
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegpgaERGVVF--QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1707 LDPLLTTTECIRFYGRLRGIRDLD------QFLDRV-LDTYELRPykdvqVRNLSGGNRRKLTVAVTCCGCTPTVLMDEP 1779
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQrleiahQMLKKVgLEGAEKRY-----IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 221500365 1780 TSDMDPVTRDMvyatIEQLLL-----ARRAVVLTSHSVSE 1814
Cdd:PRK11248 156 FGALDAFTREQ----MQTLLLklwqeTGKQVLLITHDIEE 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1646-1842 |
7.08e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCP----------QSNPLDPLLTTTE 1715
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPaenrhvntvfQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1716 CIRFYGRLRGIRDlDQFLDRVLDTY---ELRPYKDVQVRNLSGGNRRKLTVA---VTccgcTPTV-LMDEPTSDMDPVTR 1788
Cdd:PRK09452 106 NVAFGLRMQKTPA-AEITPRVMEALrmvQLEEFAQRKPHQLSGGQQQRVAIAravVN----KPKVlLLDESLSALDYKLR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1789 DMVYATIEQLllaRRAVVLT----SHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:PRK09452 181 KQMQNELKAL---QRKLGITfvfvTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
853-1039 |
7.27e-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: 53.90 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 853 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKlltgQIrqssgKVLLAGEHqvgvcwqdniliptltarehlqlyaqiki 932
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD----AI-----GLALGGAQ----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 933 PPGGSGGVEEIRSEVAQTLQSLNFGKHesypswQLSGGYRRRLCVAIAF----IASPSVVILDEPCNGVDAKARKDIWQL 1008
Cdd:cd03227 50 SATRRRSGVKAGCIVAAVSAELIFTRL------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|..
gi 221500365 1009 IERLRQGRA-VIFATHFMDEAKyLSDSLVIMR 1039
Cdd:cd03227 124 ILEHLVKGAqVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
842-999 |
8.59e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKLYGSKCAV-SNLSLDF---ARNQVsclLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPT 917
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 918 LTAREHlqlyaqikippggsggVEEIRSEVAQTLQSLN-----FGKHESY------------------------------ 962
Cdd:PRK11819 85 KTVREN----------------VEEGVAEVKAALDRFNeiyaaYAEPDADfdalaaeqgelqeiidaadawdldsqleia 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 963 ------PSW-----QLSGGYRRRlcVAIA--FIASPSVVILDEPCNGVDA 999
Cdd:PRK11819 149 mdalrcPPWdakvtKLSGGERRR--VALCrlLLEKPDMLLLDEPTNHLDA 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1628-1839 |
9.02e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAVRAENLWLAY---RRGHYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLL-------------------- 1680
Cdd:PRK10261 7 LDARDVLAVENLNIAFmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcdkmllrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1681 --------TGQLQ----PDVGQIyFEQPGISycpqsnpLDPLLTT----TECIRFY---GRLRGIRDLDQFLDRV----- 1736
Cdd:PRK10261 87 vielseqsAAQMRhvrgADMAMI-FQEPMTS-------LNPVFTVgeqiAESIRLHqgaSREEAMVEAKRMLDQVripea 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1737 ---LDTYelrPYKdvqvrnLSGGNRRKLTVAVTcCGCTPTVLM-DEPTSDMDpVTrdmVYATIEQLLLARR-----AVVL 1807
Cdd:PRK10261 159 qtiLSRY---PHQ------LSGGMRQRVMIAMA-LSCRPAVLIaDEPTTALD-VT---IQAQILQLIKVLQkemsmGVIF 224
|
250 260 270
....*....|....*....|....*....|..
gi 221500365 1808 TSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK10261 225 ITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
853-1054 |
1.02e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 853 KCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIR-QSSGKV------LLAGEHqvgvcWQDNI-------LIPTL 918
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyQGSLKIngielrELDPES-----WRKHLswvgqnpQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 TAREHLQLyAQIKIPPggsggvEEIRSEVAQT-----LQSLNFGKHesYP----SWQLSGGYRRRLCVAIAFIASPSVVI 989
Cdd:PRK11174 438 TLRDNVLL-GNPDASD------EQLQQALENAwvsefLPLLPQGLD--TPigdqAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 990 LDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYLsDSLVIMRNGRIIAQHSRDSLQR 1054
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1637-1847 |
1.11e-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: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE------------QPGISYCPQs 1704
Cdd:PRK10790 344 DNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplsslshsvlRQGVAMVQQ- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1705 nplDP-LLTTTecirFYGRLRGIRDLD-QFLDRVLDTYEL----RPYKD-------VQVRNLSGGNRRKLTVAVTCCGcT 1771
Cdd:PRK10790 423 ---DPvVLADT----FLANVTLGRDISeEQVWQALETVQLaelaRSLPDglytplgEQGNNLSVGQKQLLALARVLVQ-T 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1772 PTVL-MDEPTSDMDPVTRDmvyaTIEQLLLARRA---VVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYY 1847
Cdd:PRK10790 495 PQILiLDEATANIDSGTEQ----AIQQALAAVREhttLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGRYW 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
845-1044 |
1.23e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSK--CAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwqDNILIPTLTA-R 921
Cdd:PRK11176 346 NVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---------HDLRDYTLASlR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 922 EHLQLYAQ------------IKIPPGGSGGVEEIrSEVAQTLQSLNFGKH----------ESYPSwqLSGGYRRRLCVAI 979
Cdd:PRK11176 417 NQVALVSQnvhlfndtiannIAYARTEQYSREQI-EEAARMAYAMDFINKmdngldtvigENGVL--LSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 980 AFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMDEAKYlSDSLVIMRNGRII 1044
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1649-1833 |
1.40e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqlqpdV-------GQIYF-------------EQPGISYCPQSNPLD 1708
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-----VyphgsyeGEILFdgevcrfkdirdsEALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1709 PLLTTTECIrFYG---RLRGIRDLDQFLDR---VLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPT-- 1780
Cdd:NF040905 91 PYLSIAENI-FLGnerAKRGVIDWNETNRRareLLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTaa 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 1781 -SDMDPvtrdmvyATIEQLLLARRA----VVLTSHSVSEIEHLCQRVAVLRAGQVIAS 1833
Cdd:NF040905 170 lNEEDS-------AALLDLLLELKAqgitSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
843-1033 |
1.54e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 843 LVNVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQ- 910
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrQQVSYCAQt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 ---------DNILIPTLTAREHLQLYAQIKippggsggvEEIRSEVAQTL--QSLNfgkhesypswQLSGGYRRRlcvaI 979
Cdd:PRK10247 90 ptlfgdtvyDNLIFPWQIRNQQPDPAIFLD---------DLERFALPDTIltKNIA----------ELSGGEKQR----I 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 980 AFIAS----PSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSD 1033
Cdd:PRK10247 147 SLIRNlqfmPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADK 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1649-1839 |
1.59e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDPLL----------------- 1711
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRkkvgivfqfpehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 TTTECIRFYGRLRGIRDLD--QFLDRVLDTYELRPykDVQVRN---LSGGNRRKLTVAvTCCGCTPTVL-MDEPTSDMDP 1785
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDakQKAREMIELVGLPE--ELLARSpfeLSGGQMRRVAIA-GVLAMEPEVLvLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1786 VTR----DMVYAtieqllLARRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13634 179 KGRkemmEMFYK------LHKEKgltTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1657-1810 |
1.85e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1657 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVG--------------------QIYFE-----QPGISYCPQSNPLDP-- 1709
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelQNYFKklyngEIKVVHKPQYVDLIPkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 -------LLTTTEcirfygrLRGIrdldqfLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:PRK13409 176 fkgkvreLLKKVD-------ERGK------LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*...
gi 221500365 1783 MDPVTRdMVYATIEQLLLARRAVVLTSH 1810
Cdd:PRK13409 243 LDIRQR-LNVARLIRELAEGKYVLVVEH 269
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1645-1831 |
1.89e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1645 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS--------------NP---L 1707
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdiqfifqDPyasL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DPLLTTTECIRFYGRLRGIRDLDQFLDRV---LDTYELRPYKDVQV-RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDM 1783
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVawlLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221500365 1784 DPVTRDMVyatIEQLLLARR----AVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK10261 495 DVSIRGQI---INLLLDLQRdfgiAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1645-1831 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1645 RGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfeQPGISYCPQSNPLDplltttecirfyGRLR 1724
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI---RVGDITIDTARSLS------------QQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1725 GIRDLDQFLDRVLDTYELRPYK--------------------------------------DVQVRNLSGGNRRKLTVAVT 1766
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRtvleniiegpvivkgepkeeatararellakvglagkeTSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1767 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVI 1831
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1638-1798 |
2.33e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1638 NLWLAYRRGH---YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QP----------------- 1696
Cdd:PRK11629 10 NLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgQPmsklssaakaelrnqkl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1697 GISYcpQSNPLDPLLTTTECIRFyGRLRGIRDLDQFLDRVLDT-----YELRPYKdvQVRNLSGGNRRKLTVAVTCCGCT 1771
Cdd:PRK11629 90 GFIY--QFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMlaavgLEHRANH--RPSELSGGERQRVAIARALVNNP 164
|
170 180
....*....|....*....|....*..
gi 221500365 1772 PTVLMDEPTSDMDPVTRDMVYATIEQL 1798
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGEL 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1658-1810 |
2.33e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1658 QRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI--------------------YFE-----QPGISYCPQSNPLDPLlt 1712
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdYFKklangEIKVAHKPQYVDLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 tteciRFYGRLRGI-RDLDQF--LDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRD 1789
Cdd:COG1245 175 -----VFKGTVRELlEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180
....*....|....*....|.
gi 221500365 1790 MVYATIEQLLLARRAVVLTSH 1810
Cdd:COG1245 250 NVARLIRELAEEGKYVLVVEH 270
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1633-1839 |
2.53e-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: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRrGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG--QLQPDV---GQIYFEQPGIsYCPQSNPL 1707
Cdd:COG1117 11 KIEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLDGEDI-YDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1708 DplltttecIR------F---------------YG-RLRGIRDLDQFLDRVLDTyeLRP---YKDVQVR------NLSGG 1756
Cdd:COG1117 89 E--------LRrrvgmvFqkpnpfpksiydnvaYGlRLHGIKSKSELDEIVEES--LRKaalWDEVKDRlkksalGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1757 NRRKL----TVAVTccgctPTV-LMDEPTSDMDPVtrdmvyAT--IEQLLLA---RRAVVLTSHSVSEIEHLCQRVAVLR 1826
Cdd:COG1117 159 QQQRLciarALAVE-----PEVlLMDEPTSALDPI------STakIEELILElkkDYTIVIVTHNMQQAARVSDYTAFFY 227
|
250
....*....|...
gi 221500365 1827 AGQVIASDSPQRL 1839
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
858-1044 |
2.69e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS--SGKVLLAGEhqvgvcwqdNILIPTLTAREHLQLYAQIKIP-- 933
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGE---------SILDLEPEERAHLGIFLAFQYPie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 934 -PGGSG---------------GVEEIrsEVAQTLQSLN-----FGKHESYPSWQL----SGGYRRRLCVAIAFIASPSVV 988
Cdd:CHL00131 96 iPGVSNadflrlaynskrkfqGLPEL--DPLEFLEIINeklklVGMDPSFLSRNVnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERLR-QGRAVIFATHFMDEAKYLSDSLV-IMRNGRII 1044
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDYIKPDYVhVMQNGKII 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1649-1870 |
2.79e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-------------------YCPQSNPLDP 1709
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikqirkkvglvfQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 llTTTECIRF----YG--------------RLRGIRDldqfldrvlDTYELRPYKdvqvrnLSGGNRRKLTVAvTCCGCT 1771
Cdd:PRK13649 102 --TVLKDVAFgpqnFGvsqeeaealareklALVGISE---------SLFEKNPFE------LSGGQMRRVAIA-GILAME 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1772 PTVL-MDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQR-------LKSEH 1843
Cdd:PRK13649 164 PKILvLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDifqdvdfLEEKQ 243
|
250 260
....*....|....*....|....*...
gi 221500365 1844 GGYYAVTCFCgpaqQAILSRSLN-QRLP 1870
Cdd:PRK13649 244 LGVPKITKFA----QRLADRGISfSSLP 267
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
856-1023 |
3.79e-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: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVllagehqvGVCWQDNIL-------IPTLTAREHLqlya 928
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLflpqrpyLPLGTLREQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 929 qikippggsggveeirsevaqtlqslnfgkheSYPsWQ--LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIW 1006
Cdd:cd03223 85 --------------------------------IYP-WDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*..
gi 221500365 1007 QLIERLrqGRAVIFATH 1023
Cdd:cd03223 132 QLLKEL--GITVISVGH 146
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1628-1839 |
3.98e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAVRAENLWLAYrrGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS-YCPQ-- 1703
Cdd:PRK10253 2 TESVARLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1704 --------SNPLDPLLTTTECIRFYGRL-------RGIRDLDQFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCC 1768
Cdd:PRK10253 80 arrigllaQNATTPGDITVQELVARGRYphqplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221500365 1769 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLAR---RAVVLtsHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKgytLAAVL--HDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
867-1038 |
4.36e-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: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 867 QVSCLLGRNGAGKSTLIKLLTGQIRQSSGKvllageHQVGVCWQDNI-------LIPTLTAREHLQLYAQIK------IP 933
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGK------FDDPPDWDEILdefrgseLQNYFTKLLEGDVKVIVKpqyvdlIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 934 PGGSGGVEEIRSEVAQT------LQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQ 1007
Cdd:cd03236 101 KAVKGKVGELLKKKDERgkldelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|..
gi 221500365 1008 LIERL-RQGRAVIFATHFMDEAKYLSDSLVIM 1038
Cdd:cd03236 181 LIRELaEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1637-1825 |
4.45e-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: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGqLQPDV-GQIYF-EQPGISYCPQSnpldPLLTTt 1714
Cdd:cd03223 4 ENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRIGMpEGEDLLFLPQR----PYLPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 ecirfyGRLRgirdlDQFldrvldtyeLRPYKDVqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAT 1794
Cdd:cd03223 78 ------GTLR-----EQL---------IYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 1795 IEQLLLarrAVVLTSHSvSEIEHLCQRVAVL 1825
Cdd:cd03223 134 LKELGI---TVISVGHR-PSLWKFHDRVLDL 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
856-1041 |
9.00e-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: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVL----LAGEHQVGVCWQDNILIPTLTAREHLQLYAQIK 931
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 --IPPGGSGGVEEIRSEV-AQTLQS----LNFGKHESYPS--WQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKAR 1002
Cdd:cd03290 97 enITFGSPFNKQRYKAVTdACSLQPdidlLPFGDQTEIGErgINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221500365 1003 KDIWQ--LIERLRQG-RAVIFATHfmdEAKYL--SDSLVIMRNG 1041
Cdd:cd03290 177 DHLMQegILKFLQDDkRTLVLVTH---KLQYLphADWIIAMKDG 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1667-1815 |
9.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1667 GKNGAGKSTIFKLLTGQLQPDVGQIYF--------EQPGISYCPQSNPLDPLLTTTECIRFYGRlrgIRDLDQFLDRVLD 1738
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYkncninniAKPYCTYIGHNLGLKLEMTVFENLKFWSE---IYNSAETLYAAIH 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1739 TYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEI 1815
Cdd:PRK13541 110 YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSI 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1646-1830 |
1.04e-06 |
|
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: 51.38 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1646 GHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEqpGISYCPQSNPLD----------------P 1709
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID--GLKLTDDKKNINelrqkvgmvfqqfnlfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1710 LLTTTECIRFYGR-LRGIRDLD------QFLDRVldtyELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSD 1782
Cdd:cd03262 90 HLTVLENITLAPIkVKGMSKAEaeeralELLEKV----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQV 1830
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
865-1038 |
1.08e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSsgkvllAGEHQVGVCWqDNILiptltarEH-----LQLY------AQIK-- 931
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSW-DEVL-------KRfrgteLQNYfkklynGEIKvv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 --------IPPGGSGGVEEI---------RSEVAQTLQSLNFGKHESYpswQLSGGYRRRLCVAIAFIASPSVVILDEPC 994
Cdd:PRK13409 164 hkpqyvdlIPKVFKGKVRELlkkvdergkLDEVVERLGLENILDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 221500365 995 NGVDAKARKDIWQLIERLRQGRAVIFATHfmDEA--KYLSDSLVIM 1038
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKYVLVVEH--DLAvlDYLADNVHIA 284
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1634-1814 |
1.27e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1634 VRAENLWLAYRRgHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLL--TGQLQPDV---GQIYFEQPGIsYCPQSNPLD 1708
Cdd:PRK14243 11 LRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNL-YAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1709 -------------PLLTTT-ECIRFYGRLRGIR-DLDQFLDRVLDTYELrpYKDVQVR------NLSGGNRRKLTVAVTC 1767
Cdd:PRK14243 89 vrrrigmvfqkpnPFPKSIyDNIAYGARINGYKgDMDELVERSLRQAAL--WDEVKDKlkqsglSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221500365 1768 CGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLLARRAVVLTSHSVSE 1814
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHNMQQ 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
855-1042 |
1.35e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVC---W-----------QDNI--LIPTL 918
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWravrsdiqmifQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 TA----REHLQLYaQIKIPPggsggvEEIRSEVAQTL-------QSLNFGKHEsypswqLSGGYRRRLCVAIAFIASPSV 987
Cdd:PRK15079 116 TIgeiiAEPLRTY-HPKLSR------QEVKDRVKAMMlkvgllpNLINRYPHE------FSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGR 1042
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 ... |
1657-1825 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1657 VQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQsnpldplltttecirfygrlrgirdldqfldrv 1736
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ--------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1737 ldtyelrpYKDvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLL-ARRAVVLTSHSVSEI 1815
Cdd:cd03222 69 --------YID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEeGKKTALVVEHDLAVL 135
|
170
....*....|
gi 221500365 1816 EHLCQRVAVL 1825
Cdd:cd03222 136 DYLSDRIHVF 145
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1652-1839 |
1.73e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1652 NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIyfEQPGISYCPQSN-----------------PLDPLLTTT 1714
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI--TIAGYHITPETGnknlkklrkkvslvfqfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 --ECIRFYGRLRGIRDLD------QFLDRV---LDTYELRPYKdvqvrnLSGGNRRKLTVAvTCCGCTPTVL-MDEPTSD 1782
Cdd:PRK13641 103 vlKDVEFGPKNFGFSEDEakekalKWLKKVglsEDLISKSPFE------LSGGQMRRVAIA-GVMAYEPEILcLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 1783 MDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
967-1043 |
2.24e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 2.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 967 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1630-1848 |
2.56e-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: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1630 TGEAVRAENLWLAYRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSN---- 1705
Cdd:COG5265 354 GGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlraa 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1706 ----PLDPLL---TTTECIRfYGRL--------RGIR--DLDQFLDRVLDTYELRpykdVQVR--NLSGGNRRKLTVAVT 1766
Cdd:COG5265 434 igivPQDTVLfndTIAYNIA-YGRPdaseeeveAAARaaQIHDFIESLPDGYDTR----VGERglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1767 CCGCTPTVLMDEPTSDMDPVTRDMVYATIEQllLARRAVVLT-SHSVSEIEHlCQRVAVLRAGQVIASDSPQRLkSEHGG 1845
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALRE--VARGRTTLViAHRLSTIVD-ADEILVLEAGRIVERGTHAEL-LAQGG 584
|
...
gi 221500365 1846 YYA 1848
Cdd:COG5265 585 LYA 587
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1637-1841 |
3.30e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1637 ENLWLAYRRG---HYAVRNVNFSVQRGECFGLLGKNGAGKS----TIFKLLTGQ----LQPDV---GQ------------ 1690
Cdd:PRK15134 9 ENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpvvyPSGDIrfhGEsllhaseqtlrg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1691 -------IYFEQPGISycpqsnpLDPLLTTTEciRFYGRL---RGIR------DLDQFLDRVLDTYELRPYKDVQvRNLS 1754
Cdd:PRK15134 89 vrgnkiaMIFQEPMVS-------LNPLHTLEK--QLYEVLslhRGMRreaargEILNCLDRVGIRQAAKRLTDYP-HQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1755 GGNRRKLTVAVTCCGCTPTVLMDEPTSDMDpVTrdmVYATIEQLL--LARR---AVVLTSHSVSEIEHLCQRVAVLRAGQ 1829
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALD-VS---VQAQILQLLreLQQElnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250
....*....|..
gi 221500365 1830 VIASDSPQRLKS 1841
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1651-1848 |
3.37e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1651 RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFE-QPGISYCPQSNPLDPLLTTTECIRFYGRLRgirdl 1729
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgVPLVQYDHHYLHRQVALVGQEPVLFSGSVR----- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1730 dqflDRVldTYELRPYKDVQVRN----------------------------LSGGNRRKLTVAVTCCGcTPTVL-MDEPT 1780
Cdd:TIGR00958 573 ----ENI--AYGLTDTPDEEIMAaakaanahdfimefpngydtevgekgsqLSGGQKQRIAIARALVR-KPRVLiLDEAT 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221500365 1781 SDMDpvtrdmvyATIEQLL-----LARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGYYA 1848
Cdd:TIGR00958 646 SALD--------AECEQLLqesrsRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
871-1018 |
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 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNILIPTLTAREhlQLYAQIKIPpggsgGVEE--IRSEVA 948
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNP--LLYMMRCFP-----GVPEqkLRAHLG 612
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 949 QTLQSLNFGKHesyPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKArkdiwqlIERLRQGRAV 1018
Cdd:PLN03073 613 SFGVTGNLALQ---PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA-------VEALIQGLVL 672
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
871-1043 |
4.11e-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: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 871 LLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----HQVGV---CWQDNILIPTLTAREHLQ-------LYAQIKIPPG 935
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpQQAWIqndSLRENILFGKALNEKYYQqvleacaLLPDLEILPS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 936 GSggveeiRSEVAQtlQSLNfgkhesypswqLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI---ERL 1012
Cdd:TIGR00957 749 GD------RTEIGE--KGVN-----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGV 809
|
170 180 190
....*....|....*....|....*....|...
gi 221500365 1013 RQGRAVIFATHFMdeaKYL--SDSLVIMRNGRI 1043
Cdd:TIGR00957 810 LKNKTRILVTHGI---SYLpqVDVIIVMSGGKI 839
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1631-1836 |
5.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1631 GEAVRAENLWLAYRRGH----YAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ----PGISYCP 1702
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1703 QSNPLDPlltttECIRFYGRLRG-IRDLDQFLDRVL--DT----------------YELR--------------PYKDVQ 1749
Cdd:PRK13631 99 LITNPYS-----KKIKNFKELRRrVSMVFQFPEYQLfkDTiekdimfgpvalgvkkSEAKklakfylnkmglddSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1750 VRNLSGGNRRKLTVAvTCCGCTPTVLM-DEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAG 1828
Cdd:PRK13631 174 PFGLSGGQKRRVAIA-GILAIQPEILIfDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
....*...
gi 221500365 1829 QVIASDSP 1836
Cdd:PRK13631 253 KILKTGTP 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
967-1050 |
5.65e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 967 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL-RQGRAVIFATHFMDEAKYLSDSLVIMRNGRIIA 1045
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPELLGMCDRIYVMNEGRITG 484
|
....*
gi 221500365 1046 QHSRD 1050
Cdd:NF040905 485 ELPRE 489
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
856-1023 |
5.67e-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: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 856 VSNLSLDFARNQvSCLL-GRNGAGKSTLIKLLTGQIRQSSGKVLL-AGEHqvgvcwqdnIL-------IPTLTAREHLqL 926
Cdd:COG4178 379 LEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR---------VLflpqrpyLPLGTLREAL-L 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 927 YaqikipPGGSGGVEEirSEVAQTLQSLNFGK-----HESYPsWQ--LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDA 999
Cdd:COG4178 448 Y------PATAEAFSD--AELREALEAVGLGHlaerlDEEAD-WDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....
gi 221500365 1000 KARKDIWQLIERLRQGRAVIFATH 1023
Cdd:COG4178 519 ENEAALYQLLREELPGTTVISVGH 542
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1650-1874 |
5.83e-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: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQ----PDVGQIYFEqpGIS-------------YCPQSNPLDPLLT 1712
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYD--GITpeeikkhyrgdvvYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1713 TTECIRFYGRLRGIRDLDQFLDR----------VLDTYELRPYKDVQV-----RNLSGGNRRKLTVA-VTCCGcTPTVLM 1776
Cdd:TIGR00956 155 VGETLDFAARCKTPQNRPDGVSReeyakhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAeASLGG-AKIQCW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1777 DEPTSDMDPVTR-DMVYATIEQLLLARRAVVLTSHSVSE-IEHLCQRVAVLRAGQVIASDSPQRLKS--EHGGYyavtcF 1852
Cdd:TIGR00956 234 DNATRGLDSATAlEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPADKAKQyfEKMGF-----K 308
|
250 260
....*....|....*....|....*...
gi 221500365 1853 CGPAQ------QAILSRSLNQRLPGARD 1874
Cdd:TIGR00956 309 CPDRQttadflTSLTSPAERQIKPGYEK 336
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1649-1839 |
7.03e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTG---------------------QLQP---------DVGQIYFEqpgi 1698
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidllRLSPrerrklvghNVSMIFQE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1699 sycPQSNpLDP-------LLTTTECIRFYGRL---------RGIrdldQFLDRVldtyELRPYKDVqVRN----LSGGNR 1758
Cdd:PRK15093 98 ---PQSC-LDPservgrqLMQNIPGWTYKGRWwqrfgwrkrRAI----ELLHRV----GIKDHKDA-MRSfpyeLTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1759 RKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYAtieqlLLAR------RAVVLTSHSVSEIEHLCQRVAVLRAGQVIA 1832
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFR-----LLTRlnqnnnTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
....*..
gi 221500365 1833 SDSPQRL 1839
Cdd:PRK15093 240 TAPSKEL 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
855-1052 |
7.15e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqvgvcwqdNILIPTLTAREHLQLYAQIKIP- 933
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ---------DLLKADPEAQKLLRQKIQIVFQn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 934 PGGSggvEEIRSEVAQTLQ-----SLNFGKHES--------------------YPSwQLSGGYRRRLCVAIAFIASPSVV 988
Cdd:PRK11308 101 PYGS---LNPRKKVGQILEeplliNTSLSAAERrekalammakvglrpehydrYPH-MFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 989 ILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMRNGRIIAQHSRDSL 1052
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1643-1700 |
8.03e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.79 E-value: 8.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1643 YRRGHY-AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISY 1700
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 ... |
858-1044 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGehqvgvcwQDNILIPTLTAREHLQLYAQIKIPPGGS 937
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--------IDISTIPLEDLRSSLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 938 ggveeIRSEV--------AQTLQSLNFGKHESypswQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLI 1009
Cdd:cd03369 98 -----IRSNLdpfdeysdEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 221500365 1010 ERLRQGRAVIFATHFMDE-AKYlsDSLVIMRNGRII 1044
Cdd:cd03369 169 REEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVK 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
867-1038 |
1.69e-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: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 867 QVSCLLGRNGAGKSTLIKLLTGQIRQSsgkvllAGEHQVGVCWqDNILiptltarEH-----LQLYAQ------IK---- 931
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPN------LGDYDEEPSW-DEVL-------KRfrgteLQDYFKklangeIKvahk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 ------IPPGGSGGVEEIRS---------EVAQTLqSLNfgkhesyPSW-----QLSGGYRRRLCVAIAFIASPSVVILD 991
Cdd:COG1245 166 pqyvdlIPKVFKGTVRELLEkvdergkldELAEKL-GLE-------NILdrdisELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 992 EPCNGVDAKARKDIWQLIERL-RQGRAVIFATHfmDEA--KYLSDSLVIM 1038
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELaEEGKYVLVVEH--DLAilDYLADYVHIL 285
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
873-1015 |
1.83e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 873 GRNGAGKSTLIKLLTGQIRQSSGK--------VLLAGEHQ---VGVCWQDN---ILIPT-----LTAREHLQlyaqikip 933
Cdd:PRK10938 36 GANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLqklVSDEWQRNntdMLSPGeddtgRTTAEIIQ-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 934 pggsggvEEIRSEV--AQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIER 1011
Cdd:PRK10938 108 -------DEVKDPArcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
....
gi 221500365 1012 LRQG 1015
Cdd:PRK10938 181 LHQS 184
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
855-1029 |
1.85e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVgvcwqdnILIPT-----LTAREHLQLyaq 929
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-------IAISSglngqLTGIENIEL--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 930 ikipPGGSGGV--EEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN-GVDAKARKDIW 1006
Cdd:PRK13545 109 ----KGLMMGLtkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSvGDQTFTKKCLD 184
|
170 180
....*....|....*....|...
gi 221500365 1007 QLIERLRQGRAVIFATHFMDEAK 1029
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQVK 207
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
859-1045 |
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 221500365 859 LSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLagehqvgvcwqDNILIPTLTAREHLQLYAQI-------K 931
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL-----------DGQPVTADNREAYRQLFSAVfsdfhlfD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 932 IPPGGSGGVEEirSEVAQTLQSLNFGKHESY-----PSWQLSGGYRRRLCVAIAFIASPSVVILDEpcngvdakarkdiW 1006
Cdd:COG4615 420 RLLGLDGEADP--ARARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDE-------------W 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 1007 --------------QLIERLR-QGRAVIFATHfmDEaKY--LSDSLVIMRNGRIIA 1045
Cdd:COG4615 485 aadqdpefrrvfytELLPELKaRGKTVIAISH--DD-RYfdLADRVLKMDYGKLVE 537
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
845-998 |
2.04e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQDNI--LIPTLTARE 922
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAydFENDLTLFD 403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 923 HLQLYAQIKippggsGGVEEIRSevaqTLQSLNFGKHESYPSWQ-LSGGYRRRLCVAIAFIASPSVVILDEPCNGVD 998
Cdd:PRK15064 404 WMSQWRQEG------DDEQAVRG----TLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1634-1684 |
2.48e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1634 VRAENLWLAyRRGHYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQL 1684
Cdd:PRK13547 2 LTADHLHVA-RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL 51
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1653-1693 |
2.97e-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: 2.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 221500365 1653 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF 1693
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1649-1836 |
3.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQI----YFEQPGISYCPQSNPLDPLL------------- 1711
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKEIglvfqfpeyqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1712 TTTECIRFYGRLRGIRDLDQFLDRVLDTYEL----RPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVT 1787
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221500365 1788 RDMVYATIEQL-LLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSP 1836
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1665-1835 |
4.48e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.95 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1665 LLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------------EQPGISYCPQSNPLDPLLTTTecirfyGRLR-GIR 1727
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaekgiclppEKRRIGYVFQDARLFPHYKVR------GNLRyGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1728 --DLDQFlDRVLDTYELRPYKDVQVRNLSGGNR------RKLTVAvtccgctPTVL-MDEPTSDMD-PVTRD-MVYatIE 1796
Cdd:PRK11144 103 ksMVAQF-DKIVALLGIEPLLDRYPGSLSGGEKqrvaigRALLTA-------PELLlMDEPLASLDlPRKRElLPY--LE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 221500365 1797 QLllARRA---VVLTSHSVSEIEHLCQRVAVLRAGQVIASDS 1835
Cdd:PRK11144 173 RL--AREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1721-1841 |
5.65e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1721 GRLRGIRDLDQFLDRVLDTyelrPYKdvqvrnLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQlLL 1800
Cdd:PRK14271 142 ARLTEVGLWDAVKDRLSDS----PFR------LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LA 210
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 221500365 1801 ARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:PRK14271 211 DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
855-1044 |
6.45e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSS--GKVLLAGEH----------QVGVC--WQDNILIPTLTA 920
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdirdseALGIViiHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 921 REHLQLYAQIkippgGSGGV---EEIRSEVAQTLQSLnfGKHESyPSWQLS--GGYRRRLcVAIAFIASPSV--VILDEP 993
Cdd:NF040905 96 AENIFLGNER-----AKRGVidwNETNRRARELLAKV--GLDES-PDTLVTdiGVGKQQL-VEIAKALSKDVklLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 994 C---NGVDAKARKDiwqLIERLR-QGRAVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:NF040905 167 TaalNEEDSAALLD---LLLELKaQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1649-1846 |
6.78e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.71 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1649 AVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQSNPLDP---------LLTTT----- 1714
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQvalvsqnvhLFNDTianni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1715 --ECIRFYGRLRGIR--------DLDQFLDRVLDTyelrpykdVQVRN---LSGGNRRKLTVAVTCCGCTPTVLMDEPTS 1781
Cdd:PRK11176 438 ayARTEQYSREQIEEaarmayamDFINKMDNGLDT--------VIGENgvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221500365 1782 DMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSEHGGY 1846
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
962-1042 |
1.12e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.64 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 962 YPSwQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIMR 1039
Cdd:PRK09473 158 YPH-EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMY 236
|
...
gi 221500365 1040 NGR 1042
Cdd:PRK09473 237 AGR 239
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
873-1052 |
1.18e-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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 873 GRNGAGKSTLIKLLTGQIRQSSGKVLLAGE-----------HQVGVCWQDNILIPTlTAREHLQlYAQikipPGGSGgvE 941
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqaslrAAIGIVPQDTVLFND-TIAYNIA-YGR----PDASE--E 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 942 EIRsEVAQTLQSLNFgkHESYPS-WQ---------LSGGYRRRlcVAIA--FIASPSVVILDEPCNGVDAKARKDIWQLI 1009
Cdd:COG5265 463 EVE-AAARAAQIHDF--IESLPDgYDtrvgerglkLSGGEKQR--VAIArtLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221500365 1010 ERLRQGRAVIFATHfmdeakYLS-----DSLVIMRNGRIIAQHSRDSL 1052
Cdd:COG5265 538 REVARGRTTLVIAH------RLStivdaDEILVLEAGRIVERGTHAEL 579
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
855-1043 |
1.54e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 855 AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEhqVGVCWQDNILIPTLTAREHLQL------YA 928
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--VSVIAISAGLSGQLTGIENIEFkmlcmgFK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 929 QikippggsggvEEIRSEVAQTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCN-GVDAKARKDIWQ 1007
Cdd:PRK13546 117 R-----------KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSvGDQTFAQKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 221500365 1008 LIERLRQGRAVIFATHFMDEAKYLSDSLVIMRNGRI 1043
Cdd:PRK13546 186 IYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1653-1830 |
1.81e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.16 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1653 VNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF----------EQPG------ISYCPQSNPLDPLLTTTEC 1716
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeEARAklrakhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1717 IRFYGRLRGIRDLD--QFLDRVLDTYELRPYKDVQVRNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDmvyaT 1794
Cdd:PRK10584 109 VELPALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD----K 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221500365 1795 IEQLL--LARR---AVVLTSHSvSEIEHLCQRVAVLRAGQV 1830
Cdd:PRK10584 185 IADLLfsLNREhgtTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
851-1057 |
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 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTlikLLTGQIRQSSGKvllaGEHQV-GVCWQD---------------NIL 914
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLLSTE----GEIQIdGVSWNSvtlqtwrkafgvipqKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 915 IPTLTAREHLQLYAQIKIppggsggvEEI---------RSEVAQTLQSLNFGKHESypSWQLSGGYRRRLCVAIAFIASP 985
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSD--------EEIwkvaeevglKSVIEQFPDKLDFVLVDG--GYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221500365 986 SVVILDEPCNGVDAKArkdiWQLIER-LRQGRA---VIFATHFMDEAKYLSDSLVImrNGRIIAQHsrDSLQRLCT 1057
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 ... |
845-1044 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTG--QIRQSSGKVLlageHQVGVCWQ-DNILIP----- 916
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRII----YHVALCEKcGYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 917 -------TLTARE--------------------HLQ----LYAQIKI--------PPGGSGGVEEIRSEVaQTLQSLNFG 957
Cdd:TIGR03269 81 pcpvcggTLEPEEvdfwnlsdklrrrirkriaiMLQrtfaLYGDDTVldnvlealEEIGYEGKEAVGRAV-DLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 958 KHESYPSWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERL--RQGRAVIFATHFMDEAKYLSDSL 1035
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 221500365 1036 VIMRNGRII 1044
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
858-1071 |
3.06e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 858 NLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQS--------SGKVLLAGE--HQV---------GVCWQDNILIPTL 918
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplAAIdaprlarlrAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 919 TAREHLQLYaqiKIPPGGSGGVEEIRS-EVA-QTLQSLNFGKHESYPSWQLSGGYRRRLCVAIAF---------IASPSV 987
Cdd:PRK13547 99 SAREIVLLG---RYPHARRAGALTHRDgEIAwQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 988 VILDEPCNGVDAKARKDIWQLIERL-RQGR-AVIFATHFMDEAKYLSDSLVIMRNGRIIAQHS-RDSLQ-RLCTSNYSIR 1063
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLaRDWNlGVLAIVHDPNLAARHADRIAMLADGAIVAHGApADVLTpAHIARCYGFA 255
|
....*...
gi 221500365 1064 LRCADATG 1071
Cdd:PRK13547 256 VRLVDAGD 263
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
865-1044 |
3.36e-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: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAgehqvgvcwqdniliptltarehlqlyaqikippggsgGVEEIR 944
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------DGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 945 SEVAQTLQSLNFGKHEsypsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIE-------RLRQGRA 1017
Cdd:smart00382 43 EEVLDQLLLIIVGGKK----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLT 118
|
170 180
....*....|....*....|....*..
gi 221500365 1018 VIFATHfmDEAKYLSDSLVIMRNGRII 1044
Cdd:smart00382 119 VILTTN--DEKDLGPALLRRRFDRRIV 143
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
967-1052 |
3.44e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 967 LSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMdEAKYLSDSLVIMRNGRIIAQ 1046
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQR 530
|
....*.
gi 221500365 1047 HSRDSL 1052
Cdd:PRK10789 531 GNHDQL 536
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
845-911 |
3.52e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 3.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 845 NVSKLYGSKCAVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQIRQSSGKVLLAGEHQVGVCWQD 911
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQD 72
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1633-1848 |
4.59e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1633 AVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGIS------------ 1699
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfglmdlrkvlg 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1700 YCPQSnpldPLLtttecirFYGRLRgiRDLDQFLDR----VLDTYELRPYKDVQVR--------------NLSGGNRRKL 1761
Cdd:PLN03130 1317 IIPQA----PVL-------FSGTVR--FNLDPFNEHndadLWESLERAHLKDVIRRnslgldaevseageNFSVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1762 TVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLtSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKS 1841
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII-AHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
....*..
gi 221500365 1842 EHGGYYA 1848
Cdd:PLN03130 1462 NEGSAFS 1468
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1650-1698 |
4.67e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 4.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDV--GQIYFEQPGI 1698
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIleGDILFKGESI 73
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1641-1695 |
7.19e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 7.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 221500365 1641 LAYRRGhyaVR----NVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQ 1695
Cdd:PRK10636 7 LQIRRG---VRvlldNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1654-1691 |
7.66e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 7.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 221500365 1654 NFSVQRGEC--FGLLGKNGAGKSTIFKLLTGQLQPDVGQI 1691
Cdd:PRK15064 19 NISVKFGGGnrYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1647-1839 |
8.78e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.42 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1647 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQPGISYCPQS---------NPLDPL------- 1710
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkNQLRLLrtrltmv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1711 ---------LTTTECI-----------RFYGRLRGIRDLDQ--FLDRVLDTYELrpykdvqvrNLSGGNRRKLTVAVTCC 1768
Cdd:PRK10619 98 fqhfnlwshMTVLENVmeapiqvlglsKQEARERAVKYLAKvgIDERAQGKYPV---------HLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221500365 1769 GCTPTVLMDEPTSDMDPVTRDMVYATIEQLLLARRAVVLTSHSVSEIEHLCQRVAVLRAGQVIASDSPQRL 1839
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1660-1829 |
9.56e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1660 GECFGLLGKNGAGKSTIFKLLTGQLQPD--VGQIYFEQPGIS--------YCPQSNPLDPLLTTTECIRFYGRLRGIRDL 1729
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTkqilkrtgFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1730 DQ-----FLDRVLDTYELRPYKDVQV-----RNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIEQLL 1799
Cdd:PLN03211 174 TKqekilVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190
....*....|....*....|....*....|.
gi 221500365 1800 LARRAVVLTSHS-VSEIEHLCQRVAVLRAGQ 1829
Cdd:PLN03211 254 QKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
842-1044 |
1.33e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 842 SLVNVSKL---YGSKC----AVSNLSLDFARNQVSCLLGRNGAGKSTLIKLLTGQI----RQSSGKVLLAGEH------- 903
Cdd:PRK11022 2 ALLNVDKLsvhFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDlqrisek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 904 --------QVGVCWQDNI--LIPTLTAreHLQLYAQIKIPPGGSggvEEIRSEVAQTLQSL-----NFGKHESYPSwQLS 968
Cdd:PRK11022 82 errnlvgaEVAMIFQDPMtsLNPCYTV--GFQIMEAIKVHQGGN---KKTRRQRAIDLLNQvgipdPASRLDVYPH-QLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221500365 969 GGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQGR--AVIFATHFMDEAKYLSDSLVIMRNGRII 1044
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1628-1848 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1628 VDTGEAVRAENLWLAYRRGHYAV-RNVNFSVQRGECFGLLGKNGAGKSTI----FKLLtgqlqpDV--GQIYFEQPGISY 1700
Cdd:cd03288 14 VGLGGEIKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV------DIfdGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1701 CPQSNPLDPL-LTTTECIRFYGRLRGIRDLDQFL--DRVLDTYELRPYKDVqVRNLSG---------------GNRRKLT 1762
Cdd:cd03288 88 LPLHTLRSRLsIILQDPILFSGSIRFNLDPECKCtdDRLWEALEIAQLKNM-VKSLPGgldavvteggenfsvGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1763 VAVTCCGCTPTVLMDEPTSDMDPVTRDMVYATIeQLLLARRAVVLTSHSVSEIEHlCQRVAVLRAGQVIASDSPQRLKSE 1842
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
....*.
gi 221500365 1843 HGGYYA 1848
Cdd:cd03288 245 EDGVFA 250
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
960-1038 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 960 ESYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVI 1037
Cdd:COG4170 153 NSYP-HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTITV 231
|
.
gi 221500365 1038 M 1038
Cdd:COG4170 232 L 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
966-1040 |
1.69e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221500365 966 QLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLR--QGRAVIFATHFMDEAKYlSDSLVIMRN 1040
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRY-ANTIFVLSN 654
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1647-1693 |
1.91e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 221500365 1647 HYAVRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYF 1693
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
865-903 |
3.24e-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: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLL-------TGQIRQSSGKvllaGEH 903
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALlpeldlrTGEISEKLGR----GRH 146
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
851-1063 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 851 GSKCAVSNLSLDFARNQVSCLLGRNGAGKSTL----IKLLTGQirqssgkvllaGEHQV-GVCWQ--------------- 910
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----------GDIQIdGVSWNsvplqkwrkafgvip 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 911 DNILIPTLTAREHLQlyaqikipPGGSGGVEEI---------RSEVAQTLQSLNFgkHESYPSWQLSGGYRRRLCVAIAF 981
Cdd:cd03289 84 QKVFIFSGTFRKNLD--------PYGKWSDEEIwkvaeevglKSVIEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 982 IASPSVVILDEPCNGVDAKARKDIWQLIERLRQGRAVIFATHFMdEAKYLSDSLVIMRNGRIiaqHSRDSLQRLCTSNYS 1061
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV---RQYDSIQKLLNEKSH 229
|
..
gi 221500365 1062 IR 1063
Cdd:cd03289 230 FK 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
961-1052 |
4.32e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 961 SYPsWQLSGGYRRRLCVAIAFIASPSVVILDEPCNGVDAKARKDIWQLIERLRQ--GRAVIFATHFMDEAKYLSDSLVIM 1038
Cdd:PRK15093 154 SFP-YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWADKINVL 232
|
90
....*....|....
gi 221500365 1039 RNGRIIAQHSRDSL 1052
Cdd:PRK15093 233 YCGQTVETAPSKEL 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1650-1835 |
5.42e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1650 VRNVNFSVQRGECFGLLGKNGAGKSTIFKLLTGQLQPDVGQIYFEQpGISYCPQS----NPldpllTTTECIRFYGRLRG 1725
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-SIAYVPQQawimNA-----TVRGNILFFDEEDA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221500365 1726 IR------------DLDQfLDRVLDTyELRPyKDVqvrNLSGGNRRKLTVAVTCCGCTPTVLMDEPTSDMDPVTRDMVya 1793
Cdd:PTZ00243 750 ARladavrvsqleaDLAQ-LGGGLET-EIGE-KGV---NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV-- 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221500365 1794 tIEQLLLARRA---VVLTSHSVseieHLCQR---VAVLRAGQVIASDS 1835
Cdd:PTZ00243 822 -VEECFLGALAgktRVLATHQV----HVVPRadyVVALGDGRVEFSGS 864
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
865-896 |
8.60e-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: 8.60e-03
10 20 30
....*....|....*....|....*....|....*....
gi 221500365 865 RNQVSCLLGRNGAGKSTLIKLL-------TGQIRQSSGK 896
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALlpelvlaTGEISEKLGR 122
|
|
| |
