|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-2236 |
0e+00 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 2463.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 6 QLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYP 85
Cdd:TIGR01257 6 QIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 86 TPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQI---------KKSSSNLKLQDFLVDNETFSG 156
Cdd:TIGR01257 86 TPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFmdtlrthpeRIAGRGIRIRDILKDEEALTL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 157 FLYHNLSLPKSTVDKMLRADVILHKvFLQGY-QLHLTSL-CNGSKSEEMI----QLGDQEVSE-LCGLPREKLAAAERVL 229
Cdd:TIGR01257 166 FLMKNIGLSDSVVYLLVNSQVRPEQ-FAYGVpDLELKDIaCSEALLERFIifsqRRGAQTVRDaLCSLSQGTLQWIEDTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 230 RSNMDILKpILRTLNSTSPFPSKEL-AEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIV 308
Cdd:TIGR01257 245 YANVDFFK-LFHVLPTLLDSRSQGInLRSWGGILSDMSPRIQEFIHRPSVQDLLWVTRPLLQNGGPETFTQLMGILSDLL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 309 CGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPD 388
Cdd:TIGR01257 324 CGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 389 TPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLA 468
Cdd:TIGR01257 404 SPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPTVKDFINRQLGEEGITAEAVLNFLY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 469 KHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIEL 548
Cdd:TIGR01257 484 NGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFPDMYPWTSSL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 549 PHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYV 628
Cdd:TIGR01257 564 PPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPVGIYLQQMPYPCFV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 629 DDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGN 708
Cdd:TIGR01257 644 DDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGR 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 709 LLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFG 788
Cdd:TIGR01257 724 ILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFG 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 789 FGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFG- 867
Cdd:TIGR01257 804 FGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGg 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 868 -------EESDEKSHPGSNQKR-------ISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLG 933
Cdd:TIGR01257 884 egcstreERALEKTEPLTEEMEdpehpegINDSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 934 HNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEME 1013
Cdd:TIGR01257 964 HNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEME 1043
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1014 QMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE 1093
Cdd:TIGR01257 1044 AMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1094 ADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKdVESSLSSCRNSSSTVSYLKKEDSVsqsSSDAGLGSDHES 1173
Cdd:TIGR01257 1123 ADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRK-MKNIQSQRGGCEGTCSCTSKGFST---RCPARVDEITPE 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1174 DTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAE 1253
Cdd:TIGR01257 1199 QVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTE 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1254 ESGVDAETSDGtlpARRNRRAFGDKQSCLRPfTEDDAADPNDSDIDPESRETDLLSGM-----DGKGSYQVKGWKLTQQQ 1328
Cdd:TIGR01257 1279 DADSGSLFAGG---AQQKRENANLRHPCSGP-TEKAGQTPQASHTCSPGQPAAHPEGQpppepEDPGVPLNTGARLILQH 1354
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1329 FVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNAL 1408
Cdd:TIGR01257 1355 VQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPNSEHLEVLADVL 1434
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1409 TKDPGFGTRCMEGNPIPDTPCqAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQ 1488
Cdd:TIGR01257 1435 LNKPGFGNRCLKEEWLPEYPC-GNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPECPEGAGGLPPPQ 1513
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1489 RKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGvSNTQALPPSQE-VNDAIKQMKKHLKLAKD 1567
Cdd:TIGR01257 1514 RTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIG-GKLPAIPITGEaLVGFLSDLGQMMNVSGG 1592
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1568 SSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVA 1647
Cdd:TIGR01257 1593 PVTREASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQPLNLTKEQLSEIT 1672
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1648 LMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQK 1727
Cdd:TIGR01257 1673 VLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKK 1752
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1728 SYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNK-LNNINDILKSV 1806
Cdd:TIGR01257 1753 AYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRtLLRFNAMLRKL 1832
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1807 FLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLS 1886
Cdd:TIGR01257 1833 LIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFFLSRWIAEPAKE 1912
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1887 PLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVT 1966
Cdd:TIGR01257 1913 PIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT 1992
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1967 RGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYS 2046
Cdd:TIGR01257 1993 SGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYS 2072
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2047 GGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:TIGR01257 2073 GGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2127 SVQHLKNRFGDGYTIVVRIAGSN----PDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSslSSLARIFSILSQSKKRLH 2202
Cdd:TIGR01257 2153 TIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSS--SSLARIFQLLISHKDSLL 2230
|
2250 2260 2270
....*....|....*....|....*....|....
gi 21536376 2203 IEDYSVSQTTLDQVFVNFAKDQSDDdhlKDLSLH 2236
Cdd:TIGR01257 2231 IEEYSVTQTTLDQVFVNFAKQQTET---YDLPLH 2261
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
899-1119 |
4.25e-116 |
|
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: 366.83 E-value: 4.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLK 1119
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1912-2132 |
2.50e-115 |
|
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: 364.52 E-value: 2.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2132
Cdd:cd03263 161 TSGLDPASRRAIWD-LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
899-1136 |
1.65e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 276.94 E-value: 1.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVE 1136
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEAR 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1912-2135 |
2.31e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 250.75 E-value: 2.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRF 2135
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
899-1109 |
1.11e-65 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 220.35 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03230 79 PEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
901-1109 |
4.18e-63 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 215.88 E-value: 4.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQ 980
Cdd:COG4555 4 VENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 1061 AGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
899-1119 |
1.96e-61 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 209.92 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1059 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLK 1119
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
906-1123 |
1.26e-59 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 208.01 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 906 KVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLF 985
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 DMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1066 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLG 1123
Cdd:TIGR01188 158 RTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1927-2220 |
2.41e-58 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 204.55 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREH 2006
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2007 VEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNC 2086
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2087 ALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSnpDLKPVQDFFGLAFPGS 2166
Cdd:TIGR01188 167 IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ--SLKVEVSMLIAELGET 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2167 VL--KEKHRNMLQYQLPSSLSS--LARIFSILsqSKKRLHIEDYSVSQTTLDQVFVNF 2220
Cdd:TIGR01188 245 GLglLAVTVDSDRIKILVPDGDetVPEIVEAA--IRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1912-2132 |
4.23e-57 |
|
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: 197.59 E-value: 4.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2132
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
899-1109 |
3.53e-55 |
|
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: 191.64 E-value: 3.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMkvAVDGLALNFYEGqITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1912-2122 |
3.75e-55 |
|
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: 190.30 E-value: 3.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEffallrgvpekevgkvgewairklglvkygekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1912-2137 |
1.48e-52 |
|
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: 185.45 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2137
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
900-1108 |
4.90e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 174.19 E-value: 4.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVC 978
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1108 |
1.44e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 176.07 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 978
Cdd:COG4152 2 LELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
899-1114 |
1.23e-47 |
|
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: 170.98 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQH--NVLFdMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:COG1122 80 VFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
899-1113 |
1.17e-46 |
|
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: 167.54 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 976
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1912-2123 |
6.65e-46 |
|
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: 165.06 E-value: 6.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGeCFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2072 TTGMDPKAR-RF--LwncaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2123
Cdd:cd03264 158 TAGLDPEERiRFrnL----LSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
899-1109 |
1.04e-45 |
|
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: 164.31 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQnLGVC 978
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVkaemEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
899-1114 |
1.72e-44 |
|
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: 162.07 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:COG1127 6 IEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMLTVEEHIWFYAR-LKGLSEkhvkAEMEQMALD----VGLPSSKLKsKTSQLSGGMQRKLSVALAFVG 1049
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSE----AEIRELVLEklelVGLPGAADK-MPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
899-1109 |
1.77e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 161.15 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1059 PTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03259 157 PLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
916-1061 |
5.31e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.42 E-value: 5.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-RQNLGVCPQHNVLFDMLTVEEHI 994
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 995 WFYARLKGLSEKHVKAEMEQMALDVGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
899-1114 |
9.47e-44 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 159.97 E-value: 9.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEaVGLRGAEDL-YPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
899-1114 |
1.28e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 159.77 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
899-1105 |
4.63e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 157.25 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDG--MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstIRQNLG 976
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEADVLGDRIAIIS 1105
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
899-1108 |
6.98e-43 |
|
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: 156.29 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 978
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1911-2126 |
1.38e-42 |
|
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: 155.99 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNM 1988
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
899-1109 |
1.37e-41 |
|
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: 153.03 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 -QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPsSKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADvLGDRIAIISHGKL 1109
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1912-2121 |
1.42e-41 |
|
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: 152.76 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNiHEVHQNMGYC 1991
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
899-1108 |
3.99e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 154.96 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMeQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALV-PPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
888-1107 |
4.15e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 4.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 888 MEEEPTHLklgvSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 965
Cdd:COG1116 1 MSAAAPAL----ELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 966 SemstIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:COG1116 77 G----PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
897-1108 |
5.09e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 155.76 E-value: 5.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 976
Cdd:PRK13536 40 VAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMaLDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSL-LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
899-1101 |
6.70e-41 |
|
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: 150.71 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGL--SEKHVKAEMEQMALDvGLpsskLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLraDREAIDEALEAVGLA-GL----ADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHhmDEADVLGDRI 1101
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
899-1109 |
2.08e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 -QNLGVCPQ-HNvLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:COG1136 85 rRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADvLGDRIAIISHGKL 1109
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
900-1108 |
2.98e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 143.92 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVC 978
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQhnvlfdmltveehiwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1911-2121 |
5.39e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.80 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGY 1990
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVEFFALLRGVP----EKEVGKVGEWAirklGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSaaaaRALVPPLLEFA----KLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1115 |
8.73e-39 |
|
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: 153.52 E-value: 8.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTI 971
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 972 RQNLGVCPQH--NVLFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1115
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1912-2102 |
2.96e-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: 143.00 E-value: 2.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEvGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR-EAIDE-ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2102
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2226 |
3.13e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 146.02 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlsnIHEVHQNMGY 1990
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPqfdaitE---L---LTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:COG4152 76 LP------EergLypkMKVGEQLVYLARLKGLSKAEAKRrADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGdGYTIVV 2143
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2144 RIAGSNPDLKpvqdffglAFPGSVLKEKHRNMLQYQLPSSLSSlARIFSILSQskkRLHIEDYSVSQTTLDQVFVNFAKD 2223
Cdd:COG4152 228 EADGDAGWLR--------ALPGVTVVEEDGDGAELKLEDGADA-QELLRALLA---RGPVREFEEVRPSLNEIFIEVVGE 295
|
...
gi 21536376 2224 QSD 2226
Cdd:COG4152 296 KAE 298
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
899-1109 |
2.31e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 141.56 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
900-1114 |
5.68e-37 |
|
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: 140.26 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP 979
Cdd:cd03219 2 EVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 980 --QHNVLFDMLTVEE------------HIWFYARLKGLSEKHVKAEmeqMALD-VGLpSSKLKSKTSQLSGGMQRKLSVA 1044
Cdd:cd03219 80 tfQIPRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAE---ELLErVGL-ADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
899-1109 |
6.58e-37 |
|
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: 139.95 E-value: 6.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 QNLGVCPQH--NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD--VGLPSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1912-2126 |
7.55e-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: 138.95 E-value: 7.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSnihEVHQNMGYC 1991
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRrIDEW-LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2071 PTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
899-1108 |
1.89e-36 |
|
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: 136.36 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03228 81 VPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGK 1108
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
899-1109 |
4.08e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 4.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQ 973
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 974 NLGVCPQ-HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:COG2884 80 RIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVRE-VLDlVGL-SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
901-1108 |
7.21e-36 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 135.01 E-value: 7.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGV 977
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIwfyarlkglsekhvkaemeqmaldvGLPssklksktsqLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03229 81 VFQDFALFPHLTVLENI-------------------------ALG----------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1058 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd03229 126 EPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
914-1108 |
1.17e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 148.35 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTiRQNLGVCPQHNVLFDMLTVEE 992
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIAT-RRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 993 HIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1072
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536376 1073 ELL--LKYRQGRTIILSTHHMDEADvLGDRIAIISHGK 1108
Cdd:NF033858 438 RLLieLSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1912-2151 |
2.04e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.20 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL-KNRFGdgyTIVVRIAGSNP 2150
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALiDEHIG---CQVIEIYGGDP 276
|
.
gi 21536376 2151 D 2151
Cdd:PRK13536 277 H 277
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
899-1111 |
3.28e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 978
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQH-NVLFDM-LTVEE--------HIWFYARLKGLSEKHVKAEMEQmaldVGLpsSKLKSKT-SQLSGGMQRKLSVALAF 1047
Cdd:COG1121 81 PQRaEVDWDFpITVRDvvlmgrygRRGLFRRPSRADREAVDEALER----VGL--EDLADRPiGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCC 1111
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
899-1114 |
3.52e-35 |
|
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: 135.06 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1059 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
900-1110 |
4.31e-35 |
|
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: 134.20 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVCP 979
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 980 QH-NVLFDM-LTVEE--------HIWFYARLKglseKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:cd03235 75 QRrSIDRDFpISVRDvvlmglygHKGLFRRLS----KADKAKVDE-ALErVGL-SELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLC 1110
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
899-1114 |
5.83e-35 |
|
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: 135.17 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLG 976
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRreLARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEE--------HIWFYARLKGLSEKHVKAEMEQMALdvglpsSKLKSKT-SQLSGGMQRKLSVALAF 1047
Cdd:COG1120 79 YVPQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDREAVEEALERTGL------EHLADRPvDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1548-1869 |
2.40e-34 |
|
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: 136.37 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1548 SQEVNDaIKQMKKHLKLAKDSSADRFLNSLGRfMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHY 1627
Cdd:pfam12698 61 VQYVDS-EEEAKEALKNGKIDGLLVIPKGFSK-DLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1628 GITAFNHPLNLTKQQLSEvalmTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDM 1707
Cdd:pfam12698 139 LSTSAPIPVESTPLFNPQ----SGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1708 CNYVVPatLVIIIFICFQQksYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGInGSVATFV 1787
Cdd:pfam12698 215 LVGLLQ--LLIILLLLFGI--GIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1788 lelftdnkLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADalerfgenrfvsplswdlVGRNLFAMAVEGVVFFLIT 1867
Cdd:pfam12698 290 --------LEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWE------------------IAPSLIILLLFAVVLLLLA 343
|
..
gi 21536376 1868 VL 1869
Cdd:pfam12698 344 LL 345
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
899-1114 |
3.33e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.02 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE---MSTIR 972
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 QNLGVC---PQHNvLFDMlTVEEHIWFYARLKGLSE----KHVKAEMEQmaldVGLPSSKLKSKTS-QLSGGMQRKLSVA 1044
Cdd:PRK13637 83 KKVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEeeieNRVKRAMNI----VGLDYEDYKDKSPfELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1913-2121 |
5.59e-34 |
|
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: 131.05 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03225 81 FQ-NPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2070 EPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
900-1109 |
6.84e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 6.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGV 977
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHI--WFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:COG4619 79 VPQEPALWGG-TVRDNLpfPFQLRERKFDRERALELLER----LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
899-1109 |
8.13e-34 |
|
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: 131.15 E-value: 8.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-----PTSGTAYILGKDIRSEMSTI-- 971
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 972 -RQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSS-KLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:cd03260 79 lRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRkAALWDEvKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
900-1108 |
9.29e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.63 E-value: 9.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 976
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIWFYARLkgLSEKHVKAEMEQM-----ALDvglpsSKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERVyelfpRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1109 |
1.61e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 137.73 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYILGKDIRSEMSTIR-QN 974
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSsKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
899-1128 |
2.28e-33 |
|
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: 129.97 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTiRQNLGV 977
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 C--PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:cd03218 78 GylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEADVLGDRIAIISHGKLCCVGSS-LFLKNQLGTGYYL 1128
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD-RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPeEIAANELVRKVYL 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1913-2121 |
2.58e-33 |
|
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: 126.98 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN-IHEVHQNMGYC 1991
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFdaitelltgrehveffallrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
914-1109 |
4.27e-33 |
|
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: 129.77 E-value: 4.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFDMLTVE 991
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 992 EHI-----------WFYARLKGLSEKHVKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:COG0411 98 ENVlvaaharlgrgLLAALLRLPRARREEREARERAEEllerVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYR--QGRTIILSTHHMDEadVLG--DRIAIISHGKL 1109
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDL--VMGlaDRIVVLDFGRV 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
897-1128 |
5.09e-33 |
|
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: 137.20 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEmSTIRQN 974
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDE-DDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMlTVEEHIwfyaRL--KGLSEkhvkAEMEQMALDVGLPS----------SKLKSKTSQLSGGMQRKLS 1042
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENL----RLarPDATD----EELWAALERVGLGDwlaalpdgldTWLGEGGRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1043 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSSLFLKNQL 1122
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*.
gi 21536376 1123 GTGYYL 1128
Cdd:COG4987 561 GRYRQL 566
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
899-1114 |
6.06e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.11 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
901-1108 |
7.13e-33 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 128.84 E-value: 7.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----------RSEMS 969
Cdd:cd03256 3 VENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQNLGVCPQHNVLFDMLT--VEEHIWFYARLKGLSEKHVKAEMEqmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrLGRRSTWRSLFGLFPKEEKQRALA--ALErVGL-LDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1912-2121 |
7.68e-33 |
|
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: 128.22 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL-SNIHEVHQNMGY 1990
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQF--DAITELlTGREHVEFfALL-RGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:COG1122 80 VFQNpdDQLFAP-TVEEDVAF-GPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2068 LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
895-1113 |
1.28e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 128.92 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 895 LKLGVSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMST 970
Cdd:cd03294 21 LAKGKSKEEILK--KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 IRQN-LGVCPQHNVLFDMLTVEEHIWFYARLKGLS--EKHVKAeMEQMALdVGLPSSKlKSKTSQLSGGMQRKLSVALAF 1047
Cdd:cd03294 99 LRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPraEREERA-AEALEL-VGLEGWE-HKYPDELSGGMQQRVGLARAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03294 176 AVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
901-1113 |
3.48e-32 |
|
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: 126.68 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYRDgmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 980
Cdd:cd03299 3 VENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1061 AGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
897-1109 |
4.26e-32 |
|
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: 126.29 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVK-VYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNL 975
Cdd:cd03267 19 LIGSLKSLFKrKYRE--VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 G-VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03267 97 GvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSelLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
899-1114 |
4.62e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 131.03 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:COG4988 337 IELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIWFYARlkGLSEKHVKAEMEQ-------MALDVGLpSSKLKSKTSQLSGG-MQRkLSVALAFVG 1049
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRP--DASDEELEAALEAagldefvAALPDGL-DTPLGEGGRGLSGGqAQR-LALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1114
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGT 554
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
900-1115 |
1.14e-30 |
|
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: 122.38 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV-- 977
Cdd:TIGR04406 3 VAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIwfYARL---KGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI--MAVLeirKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1055 ILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1115
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
902-1109 |
1.72e-30 |
|
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: 120.98 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 902 QNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGV 977
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVkAEMEQMALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREI-RKRVPAALElVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1057 DEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1109 |
2.26e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.04 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYR-----DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI 959
Cdd:COG4586 2 IEVENLSKTYRvyekePGLKgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 960 LGKDIRSEMSTIRQNLGVcpqhnV-------LFDmLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKT 1030
Cdd:COG4586 82 LGYVPFKRRKEFARRIGV-----VfgqrsqlWWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVelLDLG---ELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1031 SQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:COG4586 153 RQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
..
gi 21536376 1108 KL 1109
Cdd:COG4586 232 RI 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
899-1113 |
2.51e-30 |
|
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: 120.44 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1059 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03301 157 PLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
899-1114 |
3.43e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVAL--AFVGGSKVVI 1055
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGqRQR---VALgrALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1056 LDEPTAGVDPYSR---RGiwEL--LLKyRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:COG3839 157 LDEPLSNLDAKLRvemRA--EIkrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2216 |
7.53e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.50 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP-------------------AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA- 1970
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1971 ------FLNKNSILSNIHEVhqnMGycpQ-----FDaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLvkyGE 2039
Cdd:COG4586 81 vlgyvpFKRRKEFARRIGVV---FG---QrsqlwWD-----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDL---GE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2040 KYagnysggNK--RKLS--------TAMALIGGPPVVFLDEPTTGMDPKA----RRFLwncaLSVVKE-GRSVVLTSHSM 2104
Cdd:COG4586 147 LL-------DTpvRQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSkeaiREFL----KEYNRErGTTILLTSHDM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2105 EECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKpvqdffgLAFPGSVLK-EKHRnmLQYQLPSS 2183
Cdd:COG4586 216 DDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLE-------LPRGGEVIErEGNR--VRLEVDPR 286
|
330 340 350
....*....|....*....|....*....|...
gi 21536376 2184 LsSLARIFSILSQskkRLHIEDYSVSQTTLDQV 2216
Cdd:COG4586 287 E-SLAEVLARLLA---RYPVRDLTIEEPPIEEV 315
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
899-1109 |
1.74e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 116.37 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 978
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 pqhnvlfdmLTVeehiwfyarlkglsekhvkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03216 78 ---------AMV----------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1059 PTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03216 109 PTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
899-1114 |
2.08e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.14 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLG 976
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIW--------FYARLKGLSEKhVKAEMEQMALDVglpssKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVlgleptkgGRLDRKAARAR-IRELSERYGLDV-----DPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLccVGS 1114
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
900-1113 |
2.51e-29 |
|
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: 116.38 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLGV 977
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPkeLARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLtveehiwfyarlkGLSEKHVkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03214 78 VPQALELLGLA-------------HLADRPF----------------------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1058 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03214 123 EPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
900-1115 |
4.95e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSemstiR 972
Cdd:COG1137 5 EAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkRA-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKL-KSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEAdvLG--DRIAIISHGKLCCVGSS 1115
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1912-2121 |
9.70e-29 |
|
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: 115.69 E-value: 9.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNihEVHQ-NMGY 1990
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERrNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVEFfAL-LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2070 EPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03259 156 EPLSALDAKLREEL----REELKElqrelGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
897-1114 |
1.24e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 116.28 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLG 976
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD----VGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGS 1051
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHEllklVQL--DWLADRyPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1052 KVVILDEPTAGVDPYSRRGI--WELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
899-1109 |
1.85e-28 |
|
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: 116.06 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGM--KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNL 975
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQH--NVLFDMLTVEEHIwfyAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGG-MQRklsVAL--AFVG 1049
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGqRQR---VAIarALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
908-1094 |
2.26e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 114.06 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 982
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 983 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGA--SGLRERpTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 21536376 1062 GVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEA 1094
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
899-1121 |
2.66e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGV 977
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpsSKLKSKTS-QLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK13647 84 VFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEE-ALKaVRM--WDFRDKPPyHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQ 1121
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1911-2129 |
2.72e-28 |
|
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: 115.91 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMG 1989
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDAITELLTGREHVE-----FFALLRGVPEKEVGKVgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEDREAV-EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2065 VVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2129
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEV----LELLRRlarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
881-1128 |
4.02e-28 |
|
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: 123.41 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 881 KRISEIcMEEEP-----------THLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL 949
Cdd:COG2274 446 ERLDDI-LDLPPereegrsklslPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 950 FPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIWFYArlKGLSEKHVKAEMEQMALD---VGLPS-- 1023
Cdd:COG2274 525 YEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITLGD--PDATDEEIIEAARLAGLHdfiEALPMgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1024 -SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAdvlgD 1099
Cdd:COG2274 602 dTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----D 677
|
250 260
....*....|....*....|....*....
gi 21536376 1100 RIAIISHGKLCCVGSSLFLKNQLGTGYYL 1128
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1912-2121 |
6.39e-28 |
|
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: 113.74 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRR--KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIHEV----- 1984
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 -HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEEcEALCTRMAIMVNGR 2121
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
897-1109 |
6.94e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.70 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--- 970
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 --IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK13641 81 kkLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
908-1114 |
1.98e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLAL-----NFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-----MSTIRQNLGV 977
Cdd:PRK13634 10 HRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkkLKPLRKKVGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 C---PQHNvLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:PRK13634 90 VfqfPEHQ-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1055 ILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
899-1136 |
2.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.49 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMST 970
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--SLFLKNQLGT 1124
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkELFKDKKKLA 241
|
250
....*....|....*..
gi 21536376 1125 GYYLTL-----VKKDVE 1136
Cdd:PRK13646 242 DWHIGLpeivqLQYDFE 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
899-1109 |
2.54e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 QNLGVCPQH-NvLFDMLTVEEHIWFYARLKGLSekhvKAEMEQMA---LD-VGLpSSKLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:COG1135 82 RKIGMIFQHfN-LLSSRTVAENVALPLEIAGVP----KAEIRKRVaelLElVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMdeaDV---LGDRIAIISHGKL 1109
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEM---DVvrrICDRVAVLENGRI 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1929-2073 |
2.98e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 109.27 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1929 VDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHV 2007
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2008 EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2073
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1911-2130 |
2.98e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.49 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKnsilSNIHEVHQNMGY 1990
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITEL--LTGREHVEF-----FALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMgrygrRGLFRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLGSVQH 2130
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1911-2131 |
3.93e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.47 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNKNSIL-SNIHEVHQ 1986
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLeLSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQfDAITEL--LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:COG1123 84 RIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2065 VVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
897-1133 |
5.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.92 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EM 968
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 STIRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLS-EKHVKAEMEQMALdVGLPSSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSqEEAEALAREKLAL-VGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--------SL 1116
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdifqdvDF 238
|
250 260
....*....|....*....|.
gi 21536376 1117 FLKNQLG----TGYYLTLVKK 1133
Cdd:PRK13649 239 LEEKQLGvpkiTKFAQRLADR 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
918-1109 |
6.22e-27 |
|
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: 111.21 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEmsTIRQNLGVCPQHNVLFDMLTVEEHI 994
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 995 WFYARLKgLSEKHVKAEMEQMALDVGLPSSKLK----SKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:cd03234 103 TYTAILR-LPRKSSDAIRKKRVEDVLLRDLALTriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536376 1071 IWELLLKY-RQGRTIILSTHHmDEADV--LGDRIAIISHGKL 1109
Cdd:cd03234 182 LVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
903-1109 |
8.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.48 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 903 NLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCP 979
Cdd:PRK13639 6 DLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 980 QH--NVLFdMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKtSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK13639 85 QNpdDQLF-APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
900-1109 |
1.92e-26 |
|
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: 108.88 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----RSEMSTIRQN 974
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 lgvcPQHNVLFDmlTVEEHIwfYARLKGLSEKHVKAE--MEQMALdvglpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGS 1051
Cdd:cd03226 80 ----VDYQLFTD--SVREEL--LLGLKELDAGNEQAEtvLKDLDL------YALKERHPLsLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
908-1109 |
2.28e-26 |
|
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: 109.22 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF- 985
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 ----DMLTV------EEHIWFYARLKGLSE---KHVKAemeqMALDVGlpssklkSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAELAGVTDfvnKHPNG----LDLQIG-------ERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKL 1109
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1912-2133 |
3.93e-26 |
|
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: 109.06 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEV------ 1984
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 --HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWA---IRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
900-1108 |
5.59e-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: 108.53 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 976
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-LPPhriARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEH--IWFYARLKGLSEKHVKAEMEQMaldvgLPssKLKSKTSQ----LSGGMQRKLSVALAFVGG 1050
Cdd:COG0410 82 YVPEGRRIFPSLTVEENllLGAYARRDRAEVRADLERVYEL-----FP--RLKERRRQragtLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
915-1109 |
2.23e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 105.21 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC-----PQHNVLFDMLT 989
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 990 VEEHIwfyarlkglsekhvkaemeqmALdvglpssklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:cd03215 95 VAENI---------------------AL------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536376 1070 GIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03215 142 EIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1912-2133 |
3.76e-25 |
|
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: 106.09 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHE-VHQNMG 1989
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2070 EPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
901-1109 |
5.89e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK11153 4 LKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHnvlFDML---TVEEHIWFYARLKGLSEKHVKAEMEQMaLD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:PRK11153 84 IGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTEL-LElVGL-SDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1108 |
6.25e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEM 968
Cdd:COG1101 2 LELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 -STIRQN--LGVCPQhnvlfdmLTVEEHIWF-YARLK------GLSEKHVKAEMEQMA-LDVGLPSsKLKSKTSQLSGGm 1037
Cdd:COG1101 82 iGRVFQDpmMGTAPS-------MTIEENLALaYRRGKrrglrrGLTKKRRELFRELLAtLGLGLEN-RLDTKVGLLSGG- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1038 QRK-LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:COG1101 153 QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
899-1109 |
6.41e-25 |
|
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: 104.92 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNL 975
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQHNVLFDMLTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1055 ILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
923-1109 |
7.63e-25 |
|
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: 104.17 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 923 FYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTAYILGKDirSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 1000
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP--LDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 KGLSekhvkaemeqmaldvglpssklksktsqlsGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ 1080
Cdd:cd03213 110 RGLS------------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
170 180 190
....*....|....*....|....*....|.
gi 21536376 1081 -GRTIILSTHH-MDEADVLGDRIAIISHGKL 1109
Cdd:cd03213 160 tGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
899-1093 |
1.68e-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: 104.78 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNlVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSG-TAYILGKDIRSE-MSTIRQNLG 976
Cdd:COG1119 4 LELRN-VTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCpqHNVLFDMLTVEEHIW------FYARLkGLSeKHVKAEMEQMALD----VGLpsSKLKSKT-SQLSGGMQRKLSVAL 1045
Cdd:COG1119 82 LV--SPALQLRFPRDETVLdvvlsgFFDSI-GLY-REPTDEQRERAREllelLGL--AHLADRPfGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDE 1093
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
908-1130 |
2.26e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 982
Cdd:PRK13636 15 YSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 983 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK13636 94 QLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI--EHLKDKpTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1062 GVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG--SSLFLKNQLGTGYYLTL 1130
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRL 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1911-2140 |
5.34e-24 |
|
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: 108.84 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIY---RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL----SNIHE 1983
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 VHQNMGYCPQ--FDAITELLTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDG 2138
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
..
gi 21536376 2139 YT 2140
Cdd:COG1123 500 YT 501
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1911-2131 |
7.15e-24 |
|
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: 102.66 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIY--RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSN--IHEV 1984
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQ-FDaiteLLTGR---EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:cd03258 81 RRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
899-1095 |
8.29e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.14 E-value: 8.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIWFYARlkGLSEKHVKAEMEQMALD---VGLPS---SKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP--DASDAEIREALERAGLDefvAALPQgldTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAD 1095
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1912-2121 |
1.01e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 102.03 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRK-------------------PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA-- 1970
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1971 -----FLNKNSILSNIHEVhqnmgycpqFDAITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYA 2042
Cdd:cd03267 81 aglvpWKRRKKFLRRIGVV---------FGQKTQLWWDLPVIDSFYLLAaiyDLPPARFKKRLDELSELLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2043 GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1911-2121 |
1.02e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 102.81 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIY---RrkrkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEV-- 1984
Cdd:COG0411 4 LLEVRGLTKRFgglV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 ------HQNMGYCPQFDAITELLTG---REHVEFFALLRGVP-----EKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNK 2050
Cdd:COG0411 79 lgiartFQNPRLFPELTVLENVLVAahaRLGRGLLAALLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2051 RKLSTAMALIGGPPVVFLDEPTTGMDP-----------KARRflwncalsvvKEGRSVVLTSHSMEECEALCTRMAIMVN 2119
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPeeteelaelirRLRD----------ERGITILLIEHDMDLVMGLADRIVVLDF 228
|
..
gi 21536376 2120 GR 2121
Cdd:COG0411 229 GR 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
899-1125 |
1.03e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.83 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 978
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA----RHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQ---------HNvLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGL------PSSKLksktsqlSGGMQRKLSV 1043
Cdd:NF033858 76 PRiaympqglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLapfadrPAGKL-------SGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR---TIILSTHHMDEADVLgDRIAIISHGKLCCVGSSLFLKN 1120
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
....*
gi 21536376 1121 QLGTG 1125
Cdd:NF033858 227 RTGAD 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
899-1114 |
1.39e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRseMSTIR--QNLG 976
Cdd:COG1129 5 LEMRGISKSF-GGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VC--PQHNVLFDMLTVEEHIWF---YARLKGLSEKHVKAEMEQMALDVGLPSSkLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:COG1129 81 IAiiHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1052 KVVILDEPTAgvdPYSRRGIWELL-----LKyRQGRTIILSTHHMDEADVLGDRIAIISHGKLccVGS 1114
Cdd:COG1129 160 RVLILDEPTA---SLTEREVERLFriirrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
901-1114 |
1.75e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYrDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 980
Cdd:PRK11607 22 IRNLTKSF-DG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1061 AGVDPYSR-RGIWELL-LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK11607 178 GALDKKLRdRMQLEVVdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1912-2117 |
1.89e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 101.01 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYR--RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnknSILSN---IHEVHQ 1986
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG-------EVLVDgepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVV-KEGRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
919-1113 |
2.20e-23 |
|
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: 100.26 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWF-- 996
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 997 --YARLKGLSEKHVKAEMEQMALDvglpsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1074
Cdd:cd03298 96 spGLKLTAEDRQAIEVALARVGLA-----GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536376 1075 LLKYRQGR--TIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1913-2126 |
3.06e-23 |
|
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: 99.92 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsNIHEVHQNMGYCP 1992
Cdd:cd03235 1 EVEDLT--VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1993 QFDAI--TELLTGREHVE-----FFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03235 75 QRRSIdrDFPISVRDVVLmglygHKGLFRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2066 VFLDEPTTGMDPKARRFLwncaLSVVK----EGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLG 2126
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDI----YELLRelrrEGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
902-1109 |
3.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 902 QNLVKVYRDG----MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNL 975
Cdd:PRK13633 8 KNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQH--NVLFDMLtVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK13633 88 GMVFQNpdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1054 VILDEPTAGVDPYSRR----GIWELLLKYrqGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK13633 166 IIFDEPTAMLDPSGRRevvnTIKELNKKY--GITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
899-1103 |
3.91e-23 |
|
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: 102.82 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMS 969
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQN-LGVCPQhnvlfD-------MLTVEEHIW-FYARLKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQ 1038
Cdd:COG0444 82 KIRGReIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAI 1103
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAV 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
900-1114 |
5.09e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS----EMSTIRqnl 975
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQHNVL-FDmLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSKT-SQLSGG-MQRklsVALAFV---- 1048
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDL--AHLAGRDyPQLSGGeQQR---VQLARVlaql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1049 ----GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1911-2121 |
5.32e-23 |
|
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: 99.89 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEV---- 1984
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQfDAITEL---LTGREHVE--FFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03257 81 RKEIQMVFQ-DPMSSLnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQI----LDLLKKlqeelGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
899-1110 |
5.42e-23 |
|
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: 99.49 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTV-----------EEHIWfyarlKGLSEKHVKAEMEQMA--LDvglpsSKLKSKTSQLSGGmQRKL-SV 1043
Cdd:cd03244 83 IPQDPVLFSG-TIrsnldpfgeysDEELW-----QALERVGLKEFVESLPggLD-----TVVEEGGENLSVG-QRQLlCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKLC 1110
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1913-2126 |
5.77e-23 |
|
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: 98.28 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:cd03214 1 EVENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQfdaitelltgrehveffallrgvpekevgkvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2072 TTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:cd03214 125 TSHLDIAHQIEL----LELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1900-2146 |
5.80e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 102.89 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1900 QRILDGGGQNDIlEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAG--KSSTFKMLTGDTTVTRGDAFLnknSI 1977
Cdd:NF000106 3 RKTISNGARNAV-EVRGLVKHFGEVK--AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*---TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1978 LSNIHEVHQNMG-YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:NF000106 77 CANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFG 2136
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
250
....*....|
gi 21536376 2137 dGYTIVVRIA 2146
Cdd:NF000106 237 -GRTLQIRPA 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
916-1116 |
7.72e-23 |
|
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: 99.46 E-value: 7.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQnlgVCPQHNVLFDMLTVEEHIW 995
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 996 FYAR--LKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWE 1073
Cdd:TIGR01184 77 LAVDrvLPDLSKSERRAIVEEHIALVGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 1074 LLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSL 1116
Cdd:TIGR01184 156 ELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIL 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
926-1108 |
9.29e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE------MSTIRQnlgvcpQHNvLFDMLTVEEHIWF--Y 997
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaerpVSMLFQ------ENN-LFPHLTVAQNIGLglR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 998 ARLKgLSEKHvKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRRGIWEL 1074
Cdd:COG3840 98 PGLK-LTAEQ-RAQVEQALERVGL-AGLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 21536376 1075 L--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:COG3840 172 VdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
899-1109 |
1.25e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST----- 970
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 --------------------IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLPSS 1024
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVS----KEEAKKRAAKyielVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1025 KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAI 1103
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*.
gi 21536376 1104 ISHGKL 1109
Cdd:PRK13651 238 FKDGKI 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1928-2121 |
2.21e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.59 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQ-FDAITElLTGREH 2006
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaFSLYGE-LTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2007 VEFFALLRGVPEKEV-GKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2085
Cdd:NF033858 360 LELHARLFHLPAAEIaARVAE-MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536376 2086 --CALSvVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2121
Cdd:NF033858 439 llIELS-REDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
911-1115 |
3.03e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPPTSGTAYIL--GKDI---RSEMSTIRQNLGVCPQHN 982
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPEVTITGSIVynGHNIyspRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 983 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMAL-------DVglpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK14239 96 NPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLkgasiwdEV---KDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1115
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
909-1133 |
3.04e-22 |
|
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: 98.00 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDM 987
Cdd:cd03249 13 RPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 988 lTVEEHIwFYARLKGLSEKHVKAEMEQMALD--VGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:cd03249 92 -TIAENI-RYGKPDATDEEVEEAAKKANIHDfiMSLPdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1063 VDPYSRRGIWELLLKYRQGRTIILSTHHMdeADVLG-DRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLVKK 1133
Cdd:cd03249 170 LDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRNaDLIAVLQNGQVVEQGTHDELMAQ--KGVYAKLVKA 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1912-2135 |
3.65e-22 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 97.31 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS------NIHEVH 1985
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03300 79 QNYALFPH-------LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRF 2135
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
881-1114 |
4.71e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.32 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 881 KRISEIcMEEEP-----------THLKLGVSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL 949
Cdd:COG1132 312 ERIFEL-LDEPPeipdppgavplPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 950 FPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwFYARlKGLSEKHVKAEMEQMALD---VGLPS-- 1023
Cdd:COG1132 390 YDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG-TIRENI-RYGR-PDATDEEVEEAAKAAQAHefiEALPDgy 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1024 -SKLKSKTSQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH------HMdead 1095
Cdd:COG1132 467 dTVVGERGVNLSGG-QRqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA---- 541
|
250
....*....|....*....
gi 21536376 1096 vlgDRIAIISHGKLCCVGS 1114
Cdd:COG1132 542 ---DRILVLDDGRIVEQGT 557
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
910-1107 |
4.93e-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: 96.91 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 988
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIwFYARLKGLSEKHVKAEMEQMALDVG--LPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEAAKEAGAHDFImkLPNgydTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 1064 DPYSRRGIWELLLKYRQGRTIILSTHHM------DEADVLgDRIAIISHG 1107
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIIIAHRLstiknaDKILVL-DDGKIIEEG 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1911-2117 |
7.75e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.47 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlsniHEVHQNM 1988
Cdd:COG1116 7 ALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAiteLL---TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:COG1116 83 GVVFQEPA---LLpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
900-1105 |
1.08e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTiRqnlGV 977
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVP----KAERRARAEEllalVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIIS 1105
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
899-1109 |
1.22e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 94.30 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMlTVEEhiwfyarlkglsekhvkaemeqmalDVGLpssklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03247 81 NQRPYLFDT-TLRN-------------------------NLGR----------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLgDRIAIISHGKL 1109
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1912-2121 |
1.26e-21 |
|
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: 96.94 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVG----------------------IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGD 1969
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGkskeeilkktgqtvgvndvsldVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1970 AFLNKNSILS------------NIHEVHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKY 2037
Cdd:cd03294 81 VLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2038 GEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAI 2116
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
....*
gi 21536376 2117 MVNGR 2121
Cdd:cd03294 234 MKDGR 238
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
915-1109 |
1.38e-21 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 95.90 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGKD-----IRS-EMSTIRQNlgvcPQhNVL 984
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPllplsIRGrHIATIMQN----PR-TAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 985 FDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536376 1063 VDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
902-1114 |
1.51e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 902 QNLVKVYRdGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCP 979
Cdd:PRK10895 7 KNLAKAYK-GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 980 QHNVLFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHI--EHLRDSMGQsLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1912-2126 |
2.54e-21 |
|
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: 94.63 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS------NIHEVH 1985
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03301 79 QNYALYPH-------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1912-2140 |
2.77e-21 |
|
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: 95.26 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYR--RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHEVHQNM 1988
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQfDAITEL---LTGREHVEFFALLRGVPEKEVgKVGEwAIRKLGLvkyGEKYAGNY----SGGNKRKLSTAMALIG 2061
Cdd:COG1124 82 QMVFQ-DPYASLhprHTVDRILAEPLRIHGLPDREE-RIAE-LLEQVGL---PPSFLDRYphqlSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2062 GPPVVFLDEPTTGMDPKARRFLWNcALSVVKE--GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGY 2139
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILN-LLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
.
gi 21536376 2140 T 2140
Cdd:COG1124 235 T 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1915-2121 |
4.56e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.00 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1915 KELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTV--TRGDAFLN-KNSILSNIHEVhqnMGYC 1991
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgRPLDKRSFRKI---IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHS-MEECEALCTRMAIMVNGR 2121
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
888-1114 |
5.08e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 888 MEEEPTHLKLGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSE 967
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 MSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAE-MEQMALdVGLpSSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRvMEALRM-VQL-EEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1047 FVGGSKVVILDEPTAGVDpYSRRGIWELLLKYRQ---GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1912-2131 |
5.45e-21 |
|
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: 94.29 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL--VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1913-2120 |
5.82e-21 |
|
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: 93.09 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-----LSNIHEVHQN 1987
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYcpQFdaitelltGREHVeFFALLRGVPEK-EVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03226 80 VDY--QL--------FTDSV-REELLLGLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
899-1130 |
7.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRdGMKVAVDGLalNFYEGQIT--SFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNL 975
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNI--NFIAPRNSriAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQH--NVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK13652 81 GLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHhLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--SLFLKNQLGTGYYL 1128
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHL 237
|
..
gi 21536376 1129 TL 1130
Cdd:PRK13652 238 DL 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
905-1090 |
8.13e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 905 VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNV 983
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 984 LFDMlTVEEHIWFyARlKGLSEkhvkAEMEQMALDVGLP----------SSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:TIGR02868 420 LFDT-TVRENLRL-AR-PDATD----EELWAALERVGLAdwlralpdglDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHH 1090
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
921-1114 |
9.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-----YILGKDIRSEMSTIRQNLGVCPQ--HNVLFDMlTVEEH 993
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 994 IWFYARLKGLSekhvKAEMEQMALD----VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:PRK13643 106 VAFGPQNFGIP----KEKAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1070 GIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13643 182 EMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
914-1094 |
1.14e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDirsemstirqNLGVCPQHNVLFDML--TVE 991
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 992 E--------HIWFYARLKGLSEKHVKAEMEQMALDvGLpsskLKSKTSQLSGG-MQRKLsVALAFVGGSKVVILDEPTAG 1062
Cdd:NF040873 76 DlvamgrwaRRGLWRRLTRDDRAAVDDALERVGLA-DL----AGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 21536376 1063 VDPYSRRGIWELLLKY-RQGRTIILSTHHMDEA 1094
Cdd:NF040873 150 LDAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
899-1113 |
1.42e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.95 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL-----------GKDI 964
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 965 RSE----MSTIRQNLGVCPQHNVLfDMLTVEEHIWF---YARLK--------GLSEKHVKAEMEQMaldvglpssklksk 1029
Cdd:TIGR03269 360 RGRakryIGILHQEYDLYPHRTVL-DNLTEAIGLELpdeLARMKavitlkmvGFDEEKAEEILDKY-------------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1030 TSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*.
gi 21536376 1108 KLCCVG 1113
Cdd:TIGR03269 505 KIVKIG 510
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1936-2102 |
1.54e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 92.72 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNKNSilSNIHEVHQNMGYCPQFDAITELLTGREHVEFFAL 2012
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQP--RKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2013 LR-------GVPEKEVGKVGewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPkarrFLwn 2085
Cdd:cd03234 108 LRlprkssdAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FT-- 178
|
170 180
....*....|....*....|....
gi 21536376 2086 cALSVV-------KEGRSVVLTSH 2102
Cdd:cd03234 179 -ALNLVstlsqlaRRNRIVILTIH 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
909-1109 |
1.90e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsemSTIRQNLGVCPqhnvlfdML 988
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----SLLGLGGGFNP-------EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSkLKSKTSQLSGGMQRKL--SVALAFvgGSKVVILDEPTAGVDPY 1066
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21536376 1067 SRRGIWELLL-KYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03220 177 FQEKCQRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1911-2121 |
2.10e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSN--IHE-VHQN 1987
Cdd:COG1137 3 TLEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2068 LDEPTTGMDPKAR-------RFLwncalsvvKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG1137 160 LDEPFAGVDPIAVadiqkiiRHL--------KErGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1912-2121 |
2.39e-20 |
|
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: 92.63 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHE-------- 1983
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 ---VHQNMGYCPQFDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03256 80 igmIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARR-----FLWNCAlsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRqvmdlLKRINR----EEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1912-2122 |
2.72e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQ----FDAitellTGREHVEFFALLRGVPEKEvGKVGEWaIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:COG4619 79 VPQepalWGG-----TVRDNLPFPFQLRERKFDR-ERALEL-LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
909-1108 |
4.09e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFD 986
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 987 MLTVEE------HIWFYAR-LKGL--SEKHVKAEMEQMA-----LD-VGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:PRK11300 94 EMTVIEnllvaqHQQLKTGlFSGLlkTPAFRRAESEALDraatwLErVGLLEHANRQ-AGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
915-1114 |
4.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA----YILGKDIRS--EMSTIRQNLGVC---PQHNVLF 985
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 DmlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1066 YSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13645 184 KGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1893-2122 |
6.80e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1893 EDVRRERQRILdgggQNDILEIKELTKIY---RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGD 1969
Cdd:TIGR03269 265 SEVEKECEVEV----GEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1970 ---------------AFLNKNSILSNIHEVHQNMGYCPQFDaITELLTGREHVEF---FALLRGVPE-KEVGKVGEWAIR 2030
Cdd:TIGR03269 341 vnvrvgdewvdmtkpGPDGRGRAKRYIGILHQEYDLYPHRT-VLDNLTEAIGLELpdeLARMKAVITlKMVGFDEEKAEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2031 KLglvkygEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEA 2109
Cdd:TIGR03269 420 IL------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLD 493
|
250
....*....|...
gi 21536376 2110 LCTRMAIMVNGRF 2122
Cdd:TIGR03269 494 VCDRAALMRDGKI 506
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
912-1097 |
8.56e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 912 MKVAVDGLA-----------LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTIRQNLGv 977
Cdd:PRK13539 1 MMLEGEDLAcvrggrvlfsgLSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 cpQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDvglPSSKLKSKTsqLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK13539 80 --HRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVGLA---PLAHLPFGY--LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHH---MDEADVL 1097
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLaQGGIVIAATHIplgLPGAREL 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
915-1109 |
8.90e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCP---QHNVLFDMLT 989
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 990 VEEHIWF-----YARLKGLSEKHVKAEMEQM--ALDVGLPSskLKSKTSQLSGGMQRKlsVALA--FVGGSKVVILDEPT 1060
Cdd:COG1129 347 IRENITLasldrLSRGGLLDRRRERALAEEYikRLRIKTPS--PEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1061 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1109
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
899-1109 |
9.01e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 9.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRsemstirqnLGVC 978
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETVK---------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDM-LTVEEHIWFYARlkGLSEKHVKAEMEQMaldvGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:COG0488 384 DQHQEELDPdKTVLDELRDGAP--GGTEQEVRGYLGRF----LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYrQGrTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1936-2133 |
1.05e-19 |
|
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: 90.25 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNI----HEVHQNMGYCPQFDAITELLTGREHVEFFa 2011
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMGMLFQSGALFDSLTVFENVAFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2012 lLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:cd03261 102 -LRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 2089 SVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:cd03261 181 SLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
909-1132 |
1.33e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIR-QNLGVCPQHNV 983
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 984 LFDMLTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGIN----AEERREKALDalrqVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1060 TAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVK 1132
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
899-1114 |
2.52e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.63 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS---GTAYILGKDIRSE-MSTIRQN 974
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
909-1090 |
3.10e-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: 88.18 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 988
Cdd:TIGR01189 10 RGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWFYARLKGLSEKHVKAEMEQMALD--VGLPSsklksktSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAVGLTgfEDLPA-------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*
gi 21536376 1067 SRRGIWELLLKY-RQGRTIILSTHH 1090
Cdd:TIGR01189 162 GVALLAGLLRAHlARGGIVLLTTHQ 186
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
900-1114 |
3.22e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.41 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC- 978
Cdd:COG4674 12 YVEDLTVSF-DGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 ----PqhNVlFDMLTVEEH----------IW--FYARLKGlsekHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLS 1042
Cdd:COG4674 90 kfqkP--TV-FEELTVFENlelalkgdrgVFasLFARLTA----EERDRIEEVLETIGL-TDKADRLAGLLSHGQKQWLE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1043 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1912-2121 |
3.93e-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: 88.42 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIH--EVHQNMG 1989
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDpaDLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQ-----FDAITELLT-GREHVEFFALLRGVpekEVGKVGEWAIR-KLGL-VKYGEKYAGnYSGGNKRKLSTAMALIG 2061
Cdd:cd03245 82 YVPQdvtlfYGTLRDNITlGAPLADDERILRAA---ELAGVTDFVNKhPNGLdLQIGERGRG-LSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2062 GPPVVFLDEPTTGMDPKA-RRFLWNcaLSVVKEGRSVVLTSH--SMEEceaLCTRMAIMVNGR 2121
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1909-2121 |
4.04e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-------LS 1979
Cdd:COG1136 2 SPLLELRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1980 NIHevHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1136 82 RLR--RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSmEECEALCTRMAIMVNGR 2121
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
899-1109 |
4.21e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMST 970
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 IRQNlgvcPQHNvlFDMLTVEEHIWFyarlkGLSEKHVkaEMEQM------ALD-VGLpSSKLKSKTSQLSGGmqRKLSV 1043
Cdd:PRK13635 86 VFQN----PDNQ--FVGATVQDDVAF-----GLENIGV--PREEMvervdqALRqVGM-EDFLNREPHRLSGG--QKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1044 ALAFVGGS--KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK13635 150 AIAGVLALqpDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
913-1107 |
5.08e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCPQHNVLfdmlt 989
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 990 veEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536376 1070 GIWELLLK--YRQGRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:PRK11248 166 QMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
908-1109 |
6.07e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.06 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 986
Cdd:cd03253 10 YDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 987 MlTVEEHIwFYARLKGLSEKHVKAEMEQMALD--VGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:cd03253 89 D-TIGYNI-RYGRPDATDEEVIEAAKAAQIHDkiMRFPdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536376 1062 GVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
899-1113 |
7.15e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG-- 976
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFDMLTVEEHIwFYARLK-----GL-----SEKHVKAEMeqMALDVGLPSSkLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK09700 84 IIYQELSVIDELTVLENL-YIGRHLtkkvcGVniidwREMRVRAAM--MLLRVGLKVD-LDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1047 FVGGSKVVILDEPTAGVdpySRRGIWELLLKYRQ----GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
899-1114 |
7.47e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMK---VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI----LGKDIRSEMSTI 971
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 972 -------------RQNLGVC---PQHNVLFDmlTVEEHIWFYARLKGLS--EKHVKAE--MEQMaldvGLPSSKLKSKTS 1031
Cdd:PRK13631 102 npyskkiknfkelRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKksEAKKLAKfyLNKM----GLDDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1032 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLC 1110
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....
gi 21536376 1111 CVGS 1114
Cdd:PRK13631 256 KTGT 259
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
899-1109 |
8.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNL-VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMS 969
Cdd:PRK13650 5 IEVKNLtFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQNlgvcPQHNvlFDMLTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLPSSKLKsKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK13650 85 MVFQN----PDNQ--FVGATVEDDVAFGLENKGIPHEEMKERVNE-ALElVGMQDFKER-EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1909-2121 |
8.35e-19 |
|
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: 88.22 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFlnknSIL------SNIH 1982
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFgerrggEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 EVHQNMGYC-PQF-DAITELLTGREHVE--FFA---LLRGVPEKEVGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLST 2055
Cdd:COG1119 75 ELRKRIGLVsPALqLRFPRDETVLDVVLsgFFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVV-----KEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELL----LALLdklaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1911-2133 |
9.69e-19 |
|
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: 87.73 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL----SNIHEVHQ 1986
Cdd:COG1127 5 MIEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQ----FDAitelLTGREHVEFFalLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1127 83 RIGMLFQggalFDS----LTVFENVAFP--LRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
928-1128 |
9.84e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 928 ITSFLGHNGAGKTTTMSILTGLFP------PTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 1000
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 KGLSEK-HVKAEMEQMALDVGL---PSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLL 1076
Cdd:PRK14246 118 HGIKEKrEIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1077 KYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS--LFL--KNQLGTGYYL 1128
Cdd:PRK14246 198 ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSneIFTspKNELTEKYVI 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1912-2136 |
1.01e-18 |
|
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: 92.52 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQ----FDA-ITE-LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL---VkyGEkYAGNYSGGNKRKLSTA 2056
Cdd:COG4987 414 VPQrphlFDTtLREnLRLARPDAtdeELWAALERV------GLGDW-LAALpdGLdtwL--GE-GGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFG 2136
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLA-DLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1903-2126 |
1.04e-18 |
|
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: 87.20 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1903 LDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsiLSNIH 1982
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 EVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:cd03220 90 GL--GGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2063 PPVVFLDEPTTGMDP----KARRFLwncaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:cd03220 161 PDILLIDEVLAVGDAafqeKCQRRL----RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1911-2168 |
1.05e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIhEVHQ-NMG 1989
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGL-PPEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDAiteL---LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:COG3842 81 MVFQDYA---LfphLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2067 FLDEPTTGMDPKARRflwncalSVVKE--------GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNR 2134
Cdd:COG3842 158 LLDEPLSALDAKLRE-------EMREElrrlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATR 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 21536376 2135 FgdgytivvriagsnpdlkpVQDFFGLA--FPGSVL 2168
Cdd:COG3842 231 F-------------------VADFIGEAnlLPGTVL 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
917-1090 |
1.07e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 917 DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWF 996
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 997 YARLKGLsekhVKAEMEQMALD-VGL------PssklkskTSQLSGGMQRKlsVALA--FVGGSKVVILDEP-----TAG 1062
Cdd:PRK13538 98 YQRLHGP----GDDEALWEALAqVGLagfedvP-------VRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQG 164
|
170 180
....*....|....*....|....*...
gi 21536376 1063 VDPYSRRgiweLLLKYRQGRTIILSTHH 1090
Cdd:PRK13538 165 VARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
892-1109 |
1.12e-18 |
|
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: 87.14 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 892 PTHLKLGVSIQNLVKVYRDGMKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMS 969
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQNLGVCPQHNVLFDMlTVEEHIWF------YARLKGLSEK-HVKAEMEQMALDvglPSSKLKSKTSQLSGGMQRKLS 1042
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYglqscsFECVKEAAQKaHAHSFISELASG---YDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1043 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKL 1109
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
901-1114 |
1.32e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsEMSTIRQ---NLGV 977
Cdd:PRK11231 5 TENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSRQlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEE--------HIWFYARLKGLSEKHVKAEMEQMALDvGLPSSKLksktSQLSGGMQRKLSVALAFVG 1049
Cdd:PRK11231 81 LPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRIN-HLADRRL----TDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
925-1109 |
1.33e-18 |
|
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: 86.58 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 925 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK---DIRSE--MSTIRQNLGVCPQHNVLFDMLTVEEHIWFyaR 999
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKinLPPQQRKIGLVFQQYALFPHLNVRENLAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1000 LKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LK 1077
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqIK 178
|
170 180 190
....*....|....*....|....*....|..
gi 21536376 1078 YRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1912-2123 |
1.79e-18 |
|
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: 86.33 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHE-VHQNMG 1989
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDAITELLTGREHVEFFALLRGvpekevGKVGEWAIRKLglvkYG---------EKYAGNYSGGNKRKLSTAMALI 2060
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERV----YElfprlkerrKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2123
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
899-1109 |
1.92e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQ-HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK10908 81 IGMIFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSA-ALDkVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
899-1109 |
2.20e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.69 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG---KDIRSEMSTIRQNL 975
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQHNVLFDMLTVEEHIWFYA-RLKGLSekhvKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPlRVRGAS----KEEAEKQAREllakVGL-AERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1051 SKVVILDEPTAGVDPYSRRgiwELLLKYR----QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRH---EVLKVMQdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
898-1123 |
2.41e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.02 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAgktttmSILTGLFPptsgtAYILGKDIR----------SE 967
Cdd:NF000106 13 AVEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GPDAGrrpwrf*twcAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 MSTIRQNLGVC-PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSkTSQLSGGMQRKLSVALA 1046
Cdd:NF000106 80 RRALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIW-ELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLG 1123
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWdEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
901-1109 |
2.44e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYRDG-MKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR-Q 973
Cdd:PRK10535 7 LKDIRRSYPSGeEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQLRrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 974 NLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
899-1109 |
3.63e-18 |
|
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: 86.78 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGM-------KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSE 967
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 MSTIRQNLGVCPQ--HNVLFDMLTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVA 1044
Cdd:TIGR02769 83 RRAFRRDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1909-2128 |
3.89e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYR--------------------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRG 1968
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1969 DAFLNKN--SILsnihEVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGK----VGEWAirklGLVKYGEKYA 2042
Cdd:COG1134 82 RVEVNGRvsALL----EL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeIVEFA----ELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2043 GNYSGGNKRKL--STAMALigGPPVVFLDEPTTGMDP----KARRFLwncaLSVVKEGRSVVLTSHSMEECEALCTRMAI 2116
Cdd:COG1134 145 KTYSSGMRARLafAVATAV--DPDILLVDEVLAVGDAafqkKCLARI----RELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|..
gi 21536376 2117 MVNGRFRCLGSV 2128
Cdd:COG1134 219 LEKGRLVMDGDP 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
899-1108 |
4.04e-18 |
|
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: 85.75 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIwFYARLkGLSEKHVKAEMEQ-------MALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03251 81 VSQDVFLFND-TVAENI-AYGRP-GATREEVEEAARAanahefiMELPEGY-DTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTII-----LSThhMDEAdvlgDRIAIISHGK 1108
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1911-2131 |
4.43e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL-SNIHEVHQNMG 1989
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQF--DAITELlTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:PRK13652 82 LVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2068 LDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1908-2121 |
6.10e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI---LSNIHEV 1984
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK13636 81 RESVGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2063 PPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
881-1127 |
7.36e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 881 KRISEIcMEEEP------THL----KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF 950
Cdd:PRK11160 312 RRINEI-TEQKPevtfptTSTaaadQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 951 PPTSGTAYILGKDIR--SEmSTIRQNLGVCPQHNVLFDMlTVEEHiwfyarLKGLSEKHVKAEMEQMALDVGLpsSKLKS 1028
Cdd:PRK11160 391 DPQQGEILLNGQPIAdySE-AALRQAISVVSQRVHLFSA-TLRDN------LLLAAPNASDEALIEVLQQVGL--EKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1029 KTS-----------QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH------HM 1091
Cdd:PRK11160 461 DDKglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF 540
|
250 260 270
....*....|....*....|....*....|....*.
gi 21536376 1092 deadvlgDRIAIISHGKLCCVGSSLFLKNQLGtGYY 1127
Cdd:PRK11160 541 -------DRICVMDNGQIIEQGTHQELLAQQG-RYY 568
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
915-1131 |
8.00e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.18 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEH 993
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 994 IWFYAR--------LKGLSEKHVKAEMEQMALDVGlpsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:TIGR01193 568 LLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1066 YSRRGIWELLLKYrQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1131
Cdd:TIGR01193 645 ITEKKIVNNLLNL-QDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1912-2121 |
8.34e-18 |
|
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: 83.39 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---KNSILSNIHEVHQNM 1988
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAITELLTGREHVEFfallrgvpekevgkvgewairklGLvkygekyagnySGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL-----------------------GL-----------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
899-1109 |
8.58e-18 |
|
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: 89.78 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIwFYARLKGLSEKHVKAEMEQM-ALDV--GLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:TIGR02203 411 VSQDVVLFND-TIANNI-AYGRTEQADRAEIERALAAAyAQDFvdKLPlglDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKL 1109
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1911-2122 |
8.79e-18 |
|
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: 83.25 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTkiyrrkRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHEVHQN-M 1988
Cdd:cd03215 4 VLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYcpqfdaitelltgrehveffallrgVPE--KEVGKVGEWAIRK-LGLVKYgekyagnYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03215 78 AY-------------------------VPEdrKREGLVLDLSVAEnIALSSL-------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1912-2121 |
8.84e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 82.82 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQfDAIteLLTG--REHveffaLLrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03228 81 VPQ-DPF--LFSGtiREN-----IL--------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2069 DEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2121
Cdd:cd03228 121 DEATSALDPETEALILE-ALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
909-1090 |
9.38e-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: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 988
Cdd:cd03231 10 RDG-RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWFYARLkglsekHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR 1068
Cdd:cd03231 89 SVLENLRFWHAD------HSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 21536376 1069 RGIWELLLKY-RQGRTIILSTHH 1090
Cdd:cd03231 162 ARFAEAMAGHcARGGMVVLTTHQ 184
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
918-1089 |
1.06e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMSTirQNLGVCPQHNVLFDMLTV 990
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeeaRAKLRA--KHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 991 EEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|.
gi 21536376 1071 IWELL--LKYRQGRTIILSTH 1089
Cdd:PRK10584 185 IADLLfsLNREHGTTLILVTH 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
899-1109 |
1.72e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLG 976
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-EPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1056 LDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
888-1109 |
2.25e-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: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 888 MEEEPTHLKLGVSIQNLvKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPP--TSGTAYILGK 962
Cdd:COG1117 1 MTAPASTLEPKIEVRNL-NVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 963 DIRS---EMSTIRQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMAL-DVGLP---SSKLKSKTSQLSG 1035
Cdd:COG1117 79 DIYDpdvDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLrKAALWdevKDRLKKSALGLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1036 GMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
899-1123 |
2.54e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.93 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemSTIrQNLGVC 978
Cdd:PRK11432 7 VVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSI-QQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 P--QHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEM-EQMALdVGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK11432 82 MvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVkEALEL-VDLAGFEDRY-VDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1056 LDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS---------SLFLKNQLG 1123
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMASFMG 238
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
899-1114 |
2.79e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYR------DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY 958
Cdd:COG1134 5 IEVENVSKSYRlyhepsRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 959 ILGKdirseMSTIrqnLGVcpqhNVLFDM-LTVEEHIWFYARLKGLSEKHVK---------AEMEQmALDvgLPsskLKS 1028
Cdd:COG1134 85 VNGR-----VSAL---LEL----GAGFHPeLTGRENIYLNGRLLGLSRKEIDekfdeivefAELGD-FID--QP---VKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1029 ktsqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY----SRRGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAII 1104
Cdd:COG1134 147 ----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|
gi 21536376 1105 SHGKLCCVGS 1114
Cdd:COG1134 220 EKGRLVMDGD 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1912-2102 |
4.44e-17 |
|
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: 81.64 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2102
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
916-1115 |
4.75e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.04 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLT 989
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 990 VEEHIWFYARLKGLS------EKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLwdEV---KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1062 GVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1115
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
911-1109 |
4.97e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCPQHNVLFDML 988
Cdd:PRK11288 16 GVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIW---FYARL----KGLSEKHVKAEMEQMALDVGlPSSKLKSktsqLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK11288 95 TVAENLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDID-PDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1062 GVdpySRRGIwELLLKY-----RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK11288 170 SL---SAREI-EQLFRVirelrAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
900-1109 |
4.98e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 80.72 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVC 978
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMlTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03246 82 PQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMdEADVLGDRIAIISHGKL 1109
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
912-1113 |
8.09e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 912 MKVAVDGLALNFYEGQ---------------ITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDIRSEMST- 970
Cdd:PRK14267 1 MKFAIETVNLRVYYGSnhvikgvdlkipqngVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 --IRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLS------EKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRK 1040
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALwdEV---KDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
916-1110 |
8.77e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstirqnlgVCPQ--------------- 980
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQdglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDMLTVEEHIWFYArLKGLSEK--HVKAEMEQMALD--VGLPSSKLKSKTSQ---LSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10762 338 RDGLVLGMSVKENMSLTA-LRYFSRAggSLKHADEQQAVSdfIRLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEadVLG--DRIAIISHGKLC 1110
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRIS 474
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
918-1114 |
1.00e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----------RSEMSTIRQNlgvcPQHNVLFDm 987
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalRQQVATVFQD----PEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 988 lTVEEHIWFYARLKGLSEKHVKAEMEQmALDVgLPSSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:PRK13638 94 -DIDSDIAFSLRNLGVPEAEITRRVDE-ALTL-VDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536376 1067 SRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13638 171 GRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1912-2128 |
1.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRK---RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS---NIHEVH 1985
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMG----YcPQFDAITEllTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLV--KYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:PRK13637 83 KKVGlvfqY-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2128
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1912-2129 |
1.24e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:PRK13548 3 LEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI------GGPP 2064
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2065 VVFLDEPTTGMDPK--------ARRFLWNCALSVVkegrsVVLtsHSMEECEALCTRMAIMVNGRFRCLGSVQ 2129
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvlrlARQLAHERGLAVI-----VVL--HDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
908-1128 |
1.25e-16 |
|
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: 81.38 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 986
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 987 MLTVE-----------EHIWFYARLKGLSE--KHVKAEMEQMALDVGlpssklksktSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:cd03252 90 RSIRDnialadpgmsmERVIEAAKLAGAHDfiSELPEGYDTIVGEQG----------AGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYL 1128
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1939-2129 |
1.34e-16 |
|
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: 81.23 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPE 2018
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2019 KEVG-KVGEWAiRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSV 2097
Cdd:cd03299 104 KEIErKVLEIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVT 182
|
170 180 190
....*....|....*....|....*....|...
gi 21536376 2098 VL-TSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2129
Cdd:cd03299 183 VLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1884-2142 |
1.46e-16 |
|
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: 86.04 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1884 KLSPLNDEDEDVRRERQRILDGGGQNDIlEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDT 1963
Cdd:COG2274 447 RLDDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1964 TVTRGDAFLNKNSILS-NIHEVHQNMGYCPQfDaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGLVKY--- 2037
Cdd:COG2274 526 EPTSGRILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEI----IEAARLAGLHDFiea 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2038 ---------GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMeECE 2108
Cdd:COG2274 597 lpmgydtvvGEG-GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE-NLRRLLKGRTVIIIAHRL-STI 673
|
250 260 270
....*....|....*....|....*....|....
gi 21536376 2109 ALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIV 2142
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1911-2135 |
1.82e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSiLSNIHEVHQNMGY 1990
Cdd:PRK11607 19 LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEV-GKVGEwairKLGLV---KYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIaSRVNE----MLGLVhmqEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2067 FLDEPTTGMDPKARRFLwncALSVV----KEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS----VQHLKNRF 2135
Cdd:PRK11607 172 LLDEPMGALDKKLRDRM---QLEVVdileRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRY 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
923-1114 |
2.02e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 923 FYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEMstIRQNLGVCPQHNVLFDMLTVEEHIWFYAR 999
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1000 LK---GLSEKHVKAEMEQMALDVGLPSSKlKSKTSQ------LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLRKCA-NTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1071 IWELLLKYRQGRTIILSTHHMDEADV--LGDRIAIISHGKLCCVGS 1114
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
915-1109 |
2.13e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNLGVCPQHNVLFDMLTVEE 992
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 993 HI---WFYARlkglsekhvKAEMEQMALDVGLPSSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK11614 100 NLamgGFFAE---------RDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 1066 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK11614 171 IIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1911-2121 |
2.44e-16 |
|
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: 80.41 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHE-VHQNM 1988
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRiARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKevgkvGEWAIRKLG-----LVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAE-----VRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1911-2105 |
2.53e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.10 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkPAVDRICVGIPPGE-CFgLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSN--IHEVH 1985
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKRreIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMGYCPQ-FdaitELLTGR---EHVEFFALLRGVPEKEVGK-VGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:COG2884 79 RRIGVVFQdF----RLLPDRtvyENVALPLRVTGKSRKEIRRrVRE-VLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2105
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
911-1108 |
2.54e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---------SEMSTIRQNLGVCPQh 981
Cdd:PRK10762 16 GVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeAGIGIIHQELNLIPQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 982 nvlfdmLTVEEHIW----FYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK10762 94 ------LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1058 EPT-AGVDPYSR---RGIWELllkYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK10762 167 EPTdALTDTETEslfRVIREL---KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
916-1110 |
2.70e-16 |
|
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: 84.49 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT-SGTAYILGK--DIRSEMSTIRQNLGVCPQ----HNVLFDMl 988
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWFyARLKGLSEK-HVKAEMEQMALDVGLpsSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:TIGR02633 355 GVGKNITL-SVLKSFCFKmRIDAAAELQIIGSAI--QRLKVKTAspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1061 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLC 1110
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
903-1098 |
3.02e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 903 NLVKVYRDGmKVAVDGL---ALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIR-----QN 974
Cdd:PRK11629 10 NLCKRYQEG-SVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQ-HNVLFDmLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK11629 89 LGFIYQfHHLLPD-FTALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLG 1098
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1911-2121 |
3.86e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI---LSNIHEVHQN 1987
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYCPQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13639 80 VGIVFQ-NPDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
899-1109 |
5.73e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.40 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG4181 9 IELRGLTKTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 -QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEqmaLD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL---LErVGL-GHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDEADVL-GDRIAIISHGKL 1109
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1912-2127 |
6.38e-16 |
|
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: 79.69 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIHEVHQNMGYC 1991
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGV----PEKEV-GKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIrAKVHE-LLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2127
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
902-1102 |
6.85e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 902 QNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSI---LTGLFPP--TSGTAYILGKDI---RSEMSTIRQ 973
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 974 NLGVCPQHNVLFDMlTVEEHIWFYARL---KGLSEKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELVERSLRQAALwdEV---KDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIA 1102
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1912-2121 |
7.92e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.08 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnknSILSNIHEVHqnmgyc 1991
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG-------EILVDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 pqFDAITElltgrehveffALLRGVpekevgkvgeWAIRKLglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03216 66 --FASPRD-----------ARRAGI----------AMVYQL-------------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1912-2121 |
7.94e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 78.60 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSiLSNIHE-----VHQ 1986
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGraipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1934-2139 |
8.93e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.00 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1934 VGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL----SNIHEVH-QNMGYCPQFDAITELLTGREHVE 2008
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2009 FFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2089 SV-VKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGY 2139
Cdd:PRK10070 209 KLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1909-2134 |
1.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHEVHQN 1987
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13647 81 VGLVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR 2134
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
899-1109 |
1.29e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 79.10 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-YILGKDIRSEMSTI------ 971
Cdd:TIGR02323 4 LQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 972 ---RQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKH---VKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:TIGR02323 82 rlmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHygnIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
899-1114 |
1.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLG 976
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGS 1114
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
899-1114 |
1.71e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQHNVLFDMLTVEEHIWF----YARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQL--AHLADRyPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELL------LKYrqgrTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1911-2121 |
1.98e-15 |
|
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: 77.86 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYR-----RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNI---- 1981
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1982 -HEVH----QNMGYCPQFdaiteL-----LTGREHVEFFALLRGVPEKE-VGKVGEWaIRKLGLvkyGEK----YAGNYS 2046
Cdd:COG4778 84 pREILalrrRTIGYVSQF-----LrviprVSALDVVAEPLLERGVDREEaRARAREL-LARLNL---PERlwdlPPATFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2047 GGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRflwncalsVVKE--------GRSVVLTSHSMEECEALCTRMAIMV 2118
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA--------VVVElieeakarGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 21536376 2119 NGR 2121
Cdd:COG4778 227 PFS 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1936-2102 |
2.04e-15 |
|
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: 76.90 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTT--VTRGDAFLNKNSILSNIHEVhqnMGYCPQFDAITELLTGREHVEFFALL 2013
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2014 RGVpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCALS 2089
Cdd:cd03232 107 RGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAynivRFLKKLADS 157
|
170
....*....|...
gi 21536376 2090 vvkeGRSVVLTSH 2102
Cdd:cd03232 158 ----GQAILCTIH 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
900-1109 |
2.19e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVkVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---------RSEMST 970
Cdd:COG3845 259 EVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 I---RQNLGVCPqhnvlfDMlTVEEHIWF-------YARLKGLSEKHVKAEMEQM--ALDVGLPSskLKSKTSQLSGGMQ 1038
Cdd:COG3845 338 IpedRLGRGLVP------DM-SVAENLILgryrrppFSRGGFLDRKAIRAFAEELieEFDVRTPG--PDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
899-1109 |
2.47e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.87 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI------LGKDIRSEMSTIR 972
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 973 ---QNLGVCPQHNVLFDMLTVEEHIwfyarLKG--LSEKHVKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSV 1043
Cdd:PRK11264 82 qlrQHVGFVFQNFNLFPHRTVLENI-----IEGpvIVKGEPKEEATARAREllakVGL-AGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1044 ALAFVGGSKVVILDEPTAGVDPysrRGIWELLLKYRQ----GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
898-1117 |
2.58e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLVkVYRDGmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGK-----DIRSEM 968
Cdd:PRK10418 4 QIELRNIA-LQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 -STIRQNlgvcPQH--NVLFDMLTveehiwfYAR--LKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQRKL 1041
Cdd:PRK10418 81 iATIMQN----PRSafNPLHTMHT-------HARetCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1042 SVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL--CCVGSSLF 1117
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveQGDVETLF 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
903-1120 |
3.58e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 903 NLVKV----YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMLTVEEHIWFYARLKG-LSEKHVKAEMeQMALD-VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTV-MMKLEaVGLRGAA-KLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKN 1120
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
901-1109 |
3.71e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyILGKDIRsemstirqnLGVCPQ 980
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDMLTVEEHIW--------FYARLKGLSEKHVKAEMEQMALD------------------------VGLPSSKLKS 1028
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgdaelraLEAELEELEAKLAEPDEDLERLAelqeefealggweaearaeeilsgLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1029 KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRgiW--ELLLKYRqGrTIILSTHhmDEA--DVLGDRIAII 1104
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSH--DRYflDRVATRILEL 222
|
....*
gi 21536376 1105 SHGKL 1109
Cdd:COG0488 223 DRGKL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
918-1109 |
4.15e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV--CPQHNVLFDMLTVEEHIW 995
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylVPQEPLLFPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 996 FYARLKGLSEKHVKAEMEQMA--LDVGLPSSKLKSKTSQLSGGMqRKLsvalafVGGSKVVILDEPTAGVDPYSR----R 1069
Cdd:PRK15439 109 FGLPKRQASMQKMKQLLAALGcqLDLDSSAGSLEVADRQIVEIL-RGL------MRDSRILILDEPTASLTPAETerlfS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536376 1070 GIWELLlkyRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK15439 182 RIRELL---AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1911-2127 |
4.22e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHE-VHQNM 1988
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsLLPLHArARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKV-GEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2068 LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2127
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
909-1109 |
4.74e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.32 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--------------SEMSTIRQN 974
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMLTVEEHIWFY-ARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1928-2133 |
6.02e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------KNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1999 ELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2078
Cdd:PRK09700 100 NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2079 ARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1883-2131 |
6.53e-15 |
|
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: 80.57 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1883 AKLSPLNDEDEDVRRERQRILDGGGQNDIlEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGD 1962
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1963 TTVTRGDAFLNKNSILS-NIHEVHQNMGYCPQFdaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGL---VK 2036
Cdd:COG4988 387 LPPYSGSILINGVDLSDlDPASWRRQIAWVPQN---PYLFAGtiRENLRLGR--PDASDEEL----EAALEAAGLdefVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2037 Y---------GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEEC 2107
Cdd:COG4988 458 AlpdgldtplGEG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ-ALRRLAKGRTVILITHRLALL 535
|
250 260
....*....|....*....|....
gi 21536376 2108 eALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:COG4988 536 -AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1912-2121 |
8.35e-15 |
|
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: 76.07 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFL---NKNSILSNIHE 1983
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 VHQNMGYCPQ----FDAitellTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGLVKYGEK--YAGNYSGGNKRKLSTA 2056
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEE-LIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1938-2121 |
9.44e-15 |
|
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: 75.41 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1938 PGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--------KNSILSniheVHQ-NMGYCPQFDAITELLTGREHVE 2008
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrKKINLP----PQQrKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2009 FfALLRGVPEKEVGKVGEWAIRkLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:cd03297 98 F-GLKRKRNREDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....
gi 21536376 2089 SVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03297 176 QIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1926-2072 |
9.50e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilSNIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 HV-----EFFALLRGVPE-----KEVGKV-------GEWAIR--------KLGL-VKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG0488 88 ELraleaELEELEAKLAEpdedlERLAELqeefealGGWEAEaraeeilsGLGFpEEDLDRPVSELSGGWRRRVALARAL 167
|
170
....*....|...
gi 21536376 2060 IGGPPVVFLDEPT 2072
Cdd:COG0488 168 LSEPDLLLLDEPT 180
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1909-2121 |
1.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.05 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYRR----KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNK--NSILSNIH 1982
Cdd:PRK13633 2 NEMIKCKNVSYKYESneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 EVHQNMGYCPQ------FDAITElltgrEHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYgEKYAGNY-SGGNKRKLST 2055
Cdd:PRK13633 82 DIRNKAGMVFQnpdnqiVATIVE-----EDVAFGPENLGIPPEEIRERVDESLKKVGMYEY-RRHAPHLlSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGR 2121
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1936-2106 |
1.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAiTELL--TGREHVE 2008
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPE-SQLFeeTVLKDVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2009 FFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCA 2087
Cdd:PRK13643 108 FGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF 187
|
170
....*....|....*....
gi 21536376 2088 LSVVKEGRSVVLTSHSMEE 2106
Cdd:PRK13643 188 ESIHQSGQTVVLVTHLMDD 206
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1912-2102 |
1.19e-14 |
|
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: 74.84 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03231 1 LEADELT--CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 21536376 2072 TTGMDPK-----ARRFLWNCAlsvvkEGRSVVLTSH 2102
Cdd:cd03231 153 TTALDKAgvarfAEAMAGHCA-----RGGMVVLTTH 183
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
932-1109 |
1.36e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 932 LGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMSTIRQNLGVCPQHNVLFDMLTVEEHIWF--YARLKgLSEKHvK 1009
Cdd:PRK10771 31 LGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRPVSMLFQENNLFSHLTVAQNIGLglNPGLK-LNAAQ-R 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1010 AEMEQMALDVGLpSSKLKSKTSQLSGGmQRKlSVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TII 1085
Cdd:PRK10771 108 EKLHAIARQMGI-EDLLARLPGQLSGG-QRQ-RVALArcLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLL 184
|
170 180
....*....|....*....|....
gi 21536376 1086 LSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10771 185 MVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
901-1109 |
1.49e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKvyRDGMKVAVDGLALNfyEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLGVC 978
Cdd:PRK09700 268 VRNVTS--RDRKKVRDISFSVC--RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 PQH---NVLFDMLTVEEHIWFY-----ARLKG----LSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK09700 344 TESrrdNGFFPNFSIAQNMAISrslkdGGYKGamglFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
899-1113 |
1.86e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVkVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMS-TIRQNLGV 977
Cdd:PRK09536 4 IDVSDLS-VEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSArAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVL---FDMLTVEE-----HIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSKTSqLSGGMQRKLSVALAFVG 1049
Cdd:PRK09536 82 VPQDTSLsfeFDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMER----TGVAQFADRPVTS-LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1050 GSKVVILDEPTAGVDpySRRGIWELLLKYR---QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:PRK09536 157 ATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1911-2121 |
2.23e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS---NIHEVHQN 1987
Cdd:PRK09493 1 MIEFKNVSK--HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYC-PQFDAITELlTGREHVEFFAL-LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK09493 79 AGMVfQQFYLFPHL-TALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
910-1109 |
2.32e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.85 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 988
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIwfyaRL----KGLSEKHVKAEMEQmALDVGLPSSK-----LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:PRK13657 424 SIEDNI----RVgrpdATDEEMRAAAERAQ-AHDFIERKPDgydtvVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1060 TAGVDPYSRRGIWELLLKYRQGRT--II---LSThhMDEAdvlgDRIAIISHGKL 1109
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRV 547
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1912-2122 |
2.64e-14 |
|
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: 73.12 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQfdaitelltgREHVeFFALLRgvpeKEVGKvgewairklglvkygekyagNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03247 81 NQ----------RPYL-FDTTLR----NNLGR--------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEgRSVVLTSHSMEECEALcTRMAIMVNGRF 2122
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
918-1131 |
2.78e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwF 996
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENI-A 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 997 YARLKGLSEKHVKAEMEQMALD--VGLPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGI 1071
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDfiMEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1072 WEllLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1131
Cdd:TIGR00958 657 QE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1909-2108 |
2.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--------DTTVTRGDAFLNKNSILsN 1980
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1981 IHE----VHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLS 2054
Cdd:PRK13640 82 IREkvgiVFQN----PdnQFVGATV----GDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2055 TAMALIGGPPVVFLDEPTTGMDPKARrflwNCALSVVKE-----GRSVVLTSHSMEECE 2108
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
908-1107 |
4.48e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGVCPQHNVLF 985
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-STLKpeIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 DMlTVEEHIWF--YARLKGLSEKHVKAEMEQMaldvGLPSSKLKSKTSQLSGGMQRKLSVA--LAFVggSKVVILDEPTA 1061
Cdd:PRK10247 94 GD-TVYDNLIFpwQIRNQQPDPAIFLDDLERF----ALPDTILTKNIAELSGGEKQRISLIrnLQFM--PKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536376 1062 GVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1927-2103 |
4.50e-14 |
|
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: 77.40 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIH-EVHQNMGYCPQ----FDA-ITE- 1999
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQdahlFDTtVREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2000 LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL-VKYGEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2073
Cdd:TIGR02868 429 LRLARPDAtdeELWAALERV------GLADW-LRALpdGLdTVLGEG-GARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|
gi 21536376 2074 GMDPKARRFLWNcALSVVKEGRSVVLTSHS 2103
Cdd:TIGR02868 501 HLDAETADELLE-DLLAALSGRTVVLITHH 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1913-2128 |
4.63e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.99 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSN--IHEVHQ 1986
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtaLSEkeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQ-FDaiteLLTGREHVEFFAL---LRGVPEKEVGK-VGEWairkLGLVKYGEK---YAGNYSGGNKRKLSTAMA 2058
Cdd:PRK11153 83 QIGMIFQhFN----LLSSRTVFDNVALpleLAGTPKAEIKArVTEL----LELVGLSDKadrYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2128
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSI----LELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1913-2121 |
4.73e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.64 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFL--------NKNSILSNIHEV 1984
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskeNLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNmgycP--QFDAITelltgrehVE---FFALL-RGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:PRK13632 89 FQN----PdnQFIGAT--------VEddiAFGLEnKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2121
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGK 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
915-1109 |
5.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQH-NVLFDMLTVEE 992
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 993 HIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1072
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536376 1073 ELLLKYRQGR--TIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PRK13648 183 DLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
899-1108 |
6.99e-14 |
|
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: 76.79 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDI--RSEMSTIRQN 974
Cdd:TIGR02633 2 LEMKGIVKTF-GGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEM----EQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1911-2121 |
7.01e-14 |
|
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: 75.09 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNKNSILS----NI 1981
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1982 HEV-HQNMGYCPQfDAITEL---LTGREHV-EFFALLRGVPEKEVGKVgewAIRKLGLVK--YGEKYAGNY----SGGNK 2050
Cdd:COG0444 81 RKIrGREIQMIFQ-DPMTSLnpvMTVGDQIaEPLRIHGGLSKAEARER---AIELLERVGlpDPERRLDRYphelSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2051 RKLSTAMALIGGPPVVFLDEPTTGMDpkarrflwncaLSV-----------VKE-GRSVVLTSHSMEECEALCTRMAIMV 2118
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALD-----------VTIqaqilnllkdlQRElGLAILFITHDLGVVAEIADRVAVMY 225
|
...
gi 21536376 2119 NGR 2121
Cdd:COG0444 226 AGR 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1912-2102 |
1.18e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIyrRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:PRK13538 2 LEARNLACE--RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEW-AIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDEA----LWeALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 21536376 2071 PTTGMDPKA-----RRFLWNCAlsvvkEGRSVVLTSH 2102
Cdd:PRK13538 156 PFTAIDKQGvarleALLAQHAE-----QGGMVILTTH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
899-1121 |
1.29e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMkvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP----PTSGTAYI---------LGKDIR 965
Cdd:PRK09984 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvqregrLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 966 SEmstiRQNLGVCPQHNVLFDMLTVEEHIW--------FYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGM 1037
Cdd:PRK09984 83 KS----RANTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1038 QRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1115
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
....*.
gi 21536376 1116 LFLKNQ 1121
Cdd:PRK09984 238 QQFDNE 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
898-1102 |
1.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS-----GTAYILGKDI---RSEMS 969
Cdd:PRK14258 7 AIKVNNL-SFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQNLG-VCPQHNvLFDMlTVEEHIWFYARLKGLSEK-HVKAEMEQMALDVGL---PSSKLKSKTSQLSGGMQRKLSVA 1044
Cdd:PRK14258 85 RLRRQVSmVHPKPN-LFPM-SVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIA 1102
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1911-2121 |
1.82e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTkiyrrkRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHE-VHQNM 1988
Cdd:COG1129 256 VLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQ-------------FDAITelLTGREHVEFFALLRgvpEKEVGKVGEWAIRKLGlVKYG--EKYAGNYSGGNKRKL 2053
Cdd:COG1129 330 AYVPEdrkgeglvldlsiRENIT--LASLDRLSRGGLLD---RRRERALAEEYIKRLR-IKTPspEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2054 STAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCAlsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKaeiyRLIRELA----AEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1922-2141 |
1.94e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1922 RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSS-----TFKMLTGdtTVTRGDAFLNKNSIlsNIHEVHQNMGYCPQFDA 1996
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPI--DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1997 ITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAG------NYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2068 LDEPTTGMDPkarrFLwncALSVVK-------EGRSVVLTSH--SMEECEaLCTRMAIMVNGRFRCLGSVQHLKNRFGD- 2137
Cdd:TIGR00955 190 CDEPTSGLDS----FM---AYSVVQvlkglaqKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDl 261
|
....
gi 21536376 2138 GYTI 2141
Cdd:TIGR00955 262 GHPC 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1886-2102 |
2.02e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1886 SPLNDEDEDVRRERQriLDGGGQNDILEIKELT---KIYRRKRK--PAVDRICVgipPGECFGLLGVNGAGKSSTFKMLT 1960
Cdd:TIGR00956 736 TDLTDESDDVNDEKD--MEKESGEDIFHWRNLTyevKIKKEKRVilNNVDGWVK---PGTLTALMGASGAGKTTLLNVLA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1961 GDTT---VTRGDAFLNKNSILSNIHevhQNMGYCPQFDAITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGL 2034
Cdd:TIGR00956 811 ERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEM 887
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2035 VKYGEKYAGNYSGG----NKRKLSTAMALIGGPP-VVFLDEPTTGMDPKARrflWN-CAL--SVVKEGRSVVLTSH 2102
Cdd:TIGR00956 888 ESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTA---WSiCKLmrKLADHGQAILCTIH 960
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
900-1114 |
2.97e-13 |
|
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: 70.63 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFP---PTSGTAYILGKDIrSEMST---IRQ 973
Cdd:cd03217 2 EIKDL-HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 974 NLGVCPQHNVLFDMLTVEEHIWFyarlkglsekhvkaemeqmaLDVGLpssklksktsqlSGGMQRKLSVALAFVGGSKV 1053
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNADFLRY--------------------VNEGF------------SGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEAD-VLGDRIAIISHGKLCCVGS 1114
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
914-1114 |
3.02e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 914 VAVDG----LALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIR----SEMSTIRQNLgvCPQHNVLF 985
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaAELARHRAYL--SQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 DMltveeHIWFYARL---KGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVALAFV---------GGSK 1052
Cdd:PRK03695 83 AM-----PVFQYLTLhqpDKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGeWQR---VRLAAVvlqvwpdinPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1926-2140 |
3.41e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHE---VHQNMGYCPQFDAItellt 2002
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2003 grEHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2082
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2083 LWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRClgsVQHLKNRFGDGYT 2140
Cdd:PRK11248 167 MQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1908-2121 |
3.49e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNKNS---ILS 1979
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlllpeAGTITVGGMVLSEETvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1980 NIHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:PRK13635 82 QVGMVFQN----PdnQFVGATV----QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2058 ALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2121
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
899-1108 |
3.59e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQN-INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNV-----LFDMLTVEEHIwfyarlkglSEKHVKAEME--QMALDV-GLPS---SKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK10790 420 VQQDPVvladtFLANVTLGRDI---------SEEQVWQALEtvQLAELArSLPDglyTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGK 1108
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRGQ 551
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1911-2122 |
3.70e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrkrkPAV---DRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHE--- 1983
Cdd:COG1129 4 LLEMRGISKSF-----GGVkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 -----VHQNMGYCPQFDaITE-LLTGREhveffallrgvpekevgkvgewaIRKLGLVKYGEKYA--------------- 2042
Cdd:COG1129 79 agiaiIHQELNLVPNLS-VAEnIFLGRE-----------------------PRRGGLIDWRAMRRrarellarlgldidp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2043 ----GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVK----EGRSVVLTSHSMEECEALCTRM 2114
Cdd:COG1129 135 dtpvGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL----FRIIRrlkaQGVAIIYISHRLDEVFEIADRV 210
|
....*...
gi 21536376 2115 AIMVNGRF 2122
Cdd:COG1129 211 TVLRDGRL 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
898-1118 |
3.76e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 977
Cdd:PRK11000 3 SVTLRNVTKAY-GDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1058 EPTAGVDPYSR---RgIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFL 1118
Cdd:PRK11000 159 EPLSNLDAALRvqmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1911-2121 |
4.97e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMG 1989
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDAITELLTGREHVE--------FFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAygrspwlsLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
889-1109 |
5.13e-13 |
|
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: 74.40 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 889 EEEPTHL---KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 965
Cdd:COG4618 318 EPERMPLprpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 966 S-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwfyARLKGL-SEKHVKAEmeQMA----LDVGLP---SSKLKSKTSQLSGG 1036
Cdd:COG4618 398 QwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDAdPEKVVAAA--KLAgvheMILRLPdgyDTRIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1037 -MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMdeaDVLG--DRIAIISHGKL 1109
Cdd:COG4618 472 qRQR---IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIraLK-ARGATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
913-1109 |
5.33e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY-----ILGKDIRS--EMSTIRQNLGVCPQHNVLF 985
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 DMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSS---KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536376 1063 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1912-2117 |
5.57e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 71.43 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIY--RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHE---VHQ 1986
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NmgycpqfDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:COG4525 84 K-------DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1936-2102 |
5.81e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTtvtRGDAFLNKnsILSN----IHEVHQNMGYCPQFDAITELLTGREHVEFFA 2011
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRI---QGNNFTGT--ILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2012 LLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGN-----YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2083
Cdd:PLN03211 166 LLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170
....*....|....*....
gi 21536376 2084 WNCALSVVKEGRSVVLTSH 2102
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMH 264
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
900-1109 |
7.04e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDG-------MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEM 968
Cdd:PRK10419 5 NVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 STIRQNL---------GVCPQHnvlfdmlTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQ 1038
Cdd:PRK10419 85 KAFRRDIqmvfqdsisAVNPRK-------TVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1912-2121 |
9.87e-13 |
|
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: 69.48 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS---NIHEVHQNM 1988
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQ----------FDAITELLTgrehveffaLLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03262 79 GMVFQqfnlfphltvLENITLAPI---------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
902-1108 |
1.10e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 902 QNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDIR------SE---MST 970
Cdd:PRK13549 9 KNITKTF-GGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQasnirdTEragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 IRQNLGVCPQhnvlfdmLTVEEHI-----WFYARLKGLSEKHVKAE--MEQMALDVglpssKLKSKTSQLSGGMQRKLSV 1043
Cdd:PRK13549 87 IHQELALVKE-------LSVLENIflgneITPGGIMDYDAMYLRAQklLAQLKLDI-----NPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1929-2120 |
1.20e-12 |
|
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: 69.80 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1929 VDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHE---VHQNMGYCPqfdaiteLLTGRE 2005
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 HVEFF--ALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2083
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536376 2084 WNCALSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:TIGR01184 154 QEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1911-2121 |
1.74e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.26 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSN--IHEV 1984
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtaLSEreLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQ-FDaiteLLTGR---EHVEfFAL-LRGVPEKEV-GKVGEWairkLGLVKYGEKyAGNY----SGGNKRKLS 2054
Cdd:COG1135 81 RRKIGMIFQhFN----LLSSRtvaENVA-LPLeIAGVPKAEIrKRVAEL----LELVGLSDK-ADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2055 TAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSI----LDLLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1911-2145 |
1.94e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFK----MLTGDTTVTR-----GDAFLNKNSILSNI 1981
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1982 HEVHQNMGYCPQFDAITELLTGREHVEFFAL---------LRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRK 2052
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2053 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVK-EGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*
gi 21536376 2132 KN-RFGDGYTIVVRI 2145
Cdd:PRK09984 241 DNeRFDHLYRSINRV 255
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1928-2084 |
2.30e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTF-------KMLTGDTTVTRGDaflnknsILSNIH--EVHQNMGYCPQfdait 1998
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagarKIQQGRVEVLGGD-------MADARHrrAVCPRIAYMPQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1999 EL-------LTGREHVEFFALLRGVPEKEvgkvGEWAIRKL----GLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:NF033858 84 GLgknlyptLSVFENLDFFGRLFGQDAAE----RRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170
....*....|....*..
gi 21536376 2068 LDEPTTGMDPKARRFLW 2084
Cdd:NF033858 160 LDEPTTGVDPLSRRQFW 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
916-1109 |
2.31e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYILGK--DIRSEMSTIRQNLGVCP----QHNVLFDMl 988
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIVPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWF--YARLKGLSekHVKAEMEQMALDVGLpsSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:PRK13549 357 GVGKNITLaaLDRFTGGS--RIDDAAELKTILESI--QRLKVKTAspelaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1060 TAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1109
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPE--VLGlsDRVLVMHEGKL 483
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1912-2121 |
2.46e-12 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 67.24 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNkNSILSNIHEVH--QNMG 1989
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNElgDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQFDaitELLTGrehveffallrgvpekevgkvgewAIrklglvkygekyAGN-YSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03246 80 YLPQDD---ELFSG------------------------SI------------AENiLSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2121
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1928-2121 |
3.24e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSNiHEV--------HQNMGYCPQFDAI 1997
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPG-HQIarmgvvrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1998 TELLTGR-EHVE--FFALLRGVP-----EKE-VGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:PRK11300 99 ENLLVAQhQQLKtgLFSGLLKTPafrraESEaLDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1913-2102 |
3.29e-12 |
|
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: 68.41 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQfDAIteLLTG--REHVEFFALLrgVPEKEVGKVGEWA-----IRKL--GLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:cd03254 83 LQ-DTF--LFSGtiMENIRLGRPN--ATDEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536376 2063 PPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSH 2102
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQE-ALEKLMKGRTSIIIAH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1910-2180 |
3.30e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.38 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1910 DILEIKELTKIYRR-KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFL--------NKNSILSN 1980
Cdd:PRK13650 3 NIIEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdgdllteeNVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1981 IHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:PRK13650 83 IGMVFQN----PdnQFVGATV----EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2137
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 21536376 2138 GYTIVVRIAGSNPDLKPVQDfFGLAFPGSVLKEKHrnmLQYQL 2180
Cdd:PRK13650 234 LLQLGLDIPFTTSLVQSLRQ-NGYDLPEGYLTEKE---LEEQL 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1912-2105 |
3.96e-12 |
|
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: 71.16 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELlTGREHVEFFAllRGVPEKEVgkvgEWAIRKLGL------------VKYGEKYAGnYSGGNKRKLSTAMA 2058
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEI----REALERAGLdefvaalpqgldTPIGEGGAG-LSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536376 2059 LIGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKEGRSVVLTSHSME 2105
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLA 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1908-2120 |
4.17e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAflnknSIL--SNIHEVH 1985
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILgqPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNM-GYCPQ-------FDAITE--LLTGRE-HVeffALLRgVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLS 2054
Cdd:PRK15056 77 KNLvAYVPQseevdwsFPVLVEdvVMMGRYgHM---GWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2055 TAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTrMAIMVNG 2120
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
897-1109 |
4.26e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMS 969
Cdd:COG4161 1 MSIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 970 TIRQNLGVCPQHNVLFDMLTVEEH-IWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1911-2135 |
7.00e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS------NIHEV 1984
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenrHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:PRK09452 92 FQSYALFPH-------MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2065 VVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRF 2135
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
900-1108 |
7.33e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKD---------------- 963
Cdd:PRK11701 8 SVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 964 -IRSEMSTIRQN------LGVCPQHNVlfdmltVEehiwfyaRLKGLSEKHVkAEMEQMALD----VGLPSSKLKSKTSQ 1032
Cdd:PRK11701 86 lLRTEWGFVHQHprdglrMQVSAGGNI------GE-------RLMAVGARHY-GDIRATAGDwlerVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1033 LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
640-841 |
8.80e-12 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 68.96 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 640 MPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILkLGNLLPYSDPSVVF 719
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 720 VFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLcVAWQDYVGFTLKIFASLLSPVAFGFGceyfalFEE 799
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGG-LFPLEDPPSFLQWIFSIIPFFSPIDG------LLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536376 800 QGIGVQWDNLFespveedgfnltTSVSMMLFDTFLYGVMTWY 841
Cdd:pfam12698 316 LIYGDSLWEIA------------PSLIILLLFAVVLLLLALL 345
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1907-2119 |
9.10e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1907 GQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI----LSNIH 1982
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 E----VHQN-----MGYCPQFDaitelltgrehVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKL 2053
Cdd:PRK13648 83 KhigiVFQNpdnqfVGSIVKYD-----------VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2054 STAMALIGGPPVVFLDEPTTGMDPKARRFLWNCaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVN 2119
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1936-2123 |
1.01e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSiLSNIHEVH------QNMGYCPQFDAITELLTGREHVEF 2009
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2010 FALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2089
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 21536376 2090 VVKE-GRSVVLTSHSmEECEALCTRMAIMVNGRFR 2123
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
926-1109 |
1.09e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCPQ---HNVLFDMLTVEEHIWFYARL 1000
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 KGL--------------SEKHVKAemeqmaLDVGLPSSKlkSKTSQLSGGMQRK--LSVALAfvGGSKVVILDEPTAGVD 1064
Cdd:PRK11288 359 HHLragclinnrweaenADRFIRS------LNIKTPSRE--QLIMNLSGGNQQKaiLGRWLS--EDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536376 1065 PYSRRGIWELLLKY-RQGRTIILSTHhmDEADVLG--DRIAIISHGKL 1109
Cdd:PRK11288 429 VGAKHEIYNVIYELaAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1912-2129 |
1.22e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-------LSNIHEV 1984
Cdd:COG4559 2 LEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HqnmgycPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKyagNY---SGGNKRKLSTAMALI- 2060
Cdd:COG4559 80 L------PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGR---SYqtlSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2061 ------GGPPVVFLDEPTTGMDPK--------ARRFlwncalsvVKEGRSVV-------LTSHsmeeceaLCTRMAIMVN 2119
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQL--------ARRGGGVVavlhdlnLAAQ-------YADRILLLHQ 215
|
250
....*....|
gi 21536376 2120 GRFRCLGSVQ 2129
Cdd:COG4559 216 GRLVAQGTPE 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
911-1108 |
1.27e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---------RSEMSTIRQNLGVCPQH 981
Cdd:PRK10982 10 GVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 982 NVLfdmltveEHIWF--YArLKGLSEKH------VKAEMEQMALDVGlPssklKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10982 89 SVM-------DNMWLgrYP-TKGMFVDQdkmyrdTKAIFDELDIDID-P----RAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
911-1114 |
1.34e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGVCPQHNVLFDMLT 989
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 990 VEE--------HIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK10253 98 VQElvargrypHQPLFTRWRKEDEEAVTKAMQA----TGITHLADQS-VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1062 GVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK10253 173 WLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
908-1107 |
1.46e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG--LFPPTSGTAYILGKDIRSEMSTIrqnlgvcpqhnvlf 985
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 986 dmltveEHIWfyarlkglSEKHVKAEMEQMAlDVGLPSSKL-KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:COG2401 104 ------DAIG--------RKGDFKDAVELLN-AVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536376 1065 P-YSRRG--IWELLLKyRQGRTIILSTHHMDEADVLG-DRIAIISHG 1107
Cdd:COG2401 169 RqTAKRVarNLQKLAR-RAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
898-1091 |
1.49e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemsTIRQNL-G 976
Cdd:PRK15056 6 GIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHN-------VLFD---MLTVEEHIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKsKTSQLSGGMQRKLSVALA 1046
Cdd:PRK15056 82 YVPQSEevdwsfpVLVEdvvMMGRYGHMGWLRRAKKRDRQIVTAALAR----VDMVEFRHR-QIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHM 1091
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
899-1108 |
1.70e-11 |
|
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: 64.01 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayilgkdirsemstirqnlgvc 978
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 pqhnvlfdmltveehiwfYARLKGLSEKHVkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03221 57 ------------------VTWGSTVKIGYF----------------------EQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRqgRTIILSTHhmDEA--DVLGDRIAIISHGK 1108
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1912-2121 |
1.79e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.32 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKpavdRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHE------- 1983
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAErpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 ----------VHQNMGycpqfdaitelltgrehvefFAL---LR-GVPEKEvgKVgEWAIRKLGLVKYGEKYAGNYSGGN 2049
Cdd:COG3840 78 qennlfphltVAQNIG--------------------LGLrpgLKlTAEQRA--QV-EQALERVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2050 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEM----LDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
899-1065 |
1.81e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG-----------KDIRSe 967
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 mstIRQNLGVCPQHNVLFDMLTVEEH-IWFYARLKGLSEKHVKAEMEQMaldvgLPSSKLKSKTS----QLSGGMQRKLS 1042
Cdd:PRK11124 80 ---LRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKL-----LERLRLKPYADrfplHLSGGQQQRVA 151
|
170 180
....*....|....*....|...
gi 21536376 1043 VALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
926-1089 |
1.95e-11 |
|
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: 65.34 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSIL-----TGLfppTSGTAYILGKDIRSemsTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 1000
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDK---NFQRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 KGLSekhvkaeMEQmaldvglpssklksktsqlsggmQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-R 1079
Cdd:cd03232 107 RGLS-------VEQ-----------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaD 156
|
170
....*....|
gi 21536376 1080 QGRTIILSTH 1089
Cdd:cd03232 157 SGQAILCTIH 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1927-2191 |
2.29e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--KNSILSNIHEVHQNMGYCPQfDAITELL--T 2002
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIRKLVGIVFQ-NPETQFVgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2003 GREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2082
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2083 LWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKnrfgdgytivvriagSNPDLKpvqdFFGLA 2162
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL---------------SDVSLQ----TLGLT 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 21536376 2163 FPGSV-LKE---KHRNMLQYQLPSSLSSLA----RIF 2191
Cdd:PRK13644 235 PPSLIeLAEnlkMHGVVIPWENTSSPSSFAeeicRLF 271
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1909-2123 |
2.56e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsniheVHqnM 1988
Cdd:COG0488 313 KKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------VK--I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQ-FDAITELLTGREHVEffALLRGVPEKEVGKVgewairkLGlvKYG------EKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDELR--DGAPGGTEQEVRGY-------LG--RFLfsgddaFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2062 GPPVVFLDEPTTGMDPKARRFLwNCALSVVkEGrSVVLTSHSMEECEALCTRMAIMVNGRFR 2123
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEAL-EEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1899-2121 |
2.86e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1899 RQRILDGGGQNDILEIKELTkiyRRKRKPAVDrICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--KNS 1976
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT---SRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1977 ILSNIHEVHQNMGYcpqfdaITElltGREHVEFF---------ALLRGVpeKEVGKVGEWAI-------------RKLGL 2034
Cdd:PRK09700 329 PRSPLDAVKKGMAY------ITE---SRRDNGFFpnfsiaqnmAISRSL--KDGGYKGAMGLfhevdeqrtaenqRELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2035 VKYG--EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCT 2112
Cdd:PRK09700 398 LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
....*....
gi 21536376 2113 RMAIMVNGR 2121
Cdd:PRK09700 478 RIAVFCEGR 486
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1927-2106 |
3.74e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDaflnknsilsnihevHQNMGYCPQFDAITELL 2001
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlrptSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2002 --TGREHVE--FFA---LLRGvPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2074
Cdd:NF040873 71 plTVRDLVAmgRWArrgLWRR-LTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|..
gi 21536376 2075 MDPKARRFLWNCALSVVKEGRSVVLTSHSMEE 2106
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1936-2103 |
5.82e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GDAFLNKNSILS---NIHEVHQNMGYCPQFDAITELLTGREHV 2007
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTllrTFNRLLELNEEARveGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2008 EFFALLRGV--PEKEVGKVGEWAIRKLGL---VKYGEK-YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK14267 107 AIGVKLNGLvkSKKELDERVEWALKKAALwdeVKDRLNdYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180
....*....|....*....|..
gi 21536376 2082 FLWNCALSvVKEGRSVVLTSHS 2103
Cdd:PRK14267 187 KIEELLFE-LKKEYTIVLVTHS 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1926-2121 |
6.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.62 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFK-----MLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAiTEL 2000
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnalLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPE-AQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2001 L--TGREHVEFFALLRGVPEKEV-GKVGEWaIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK13641 99 FenTVLKDVEFGPKNFGFSEDEAkEKALKW-LKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 2077 PKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1912-2105 |
6.10e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRK---PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG------------------DTTVTRGDA 1970
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1971 FLNKNSI-------LSNIHEVHQNMGYCPQFdAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL-VKYGEK 2040
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2041 YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2105
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
900-1109 |
7.53e-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: 67.40 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYR--DGMKVAVDGLALNFYEGQITSFLGHNGAGKT-TTMSILtGLFPP----TSGTAYILGKDI----RSEM 968
Cdd:COG4172 8 SVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 STIRQN------------LgvcpqhNVLFdmlTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGL--PSSKLKSKTSQL 1033
Cdd:COG4172 87 RRIRGNriamifqepmtsL------NPLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdPERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1034 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDEADV--LGDRIAIISHGKL 1109
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH--DLGVVrrFADRVAVMRQGEI 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1939-2121 |
7.80e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--KNSILSNIHEVHQNMGYCPQ---FDAITELLTGRE-------- 2005
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADninisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 -HVEFFALLRGVPEKEVGkvgEWAIRKLGlVK--YGEKYAGNYSGGNKRK------LSTAMAliggppVVFLDEPTTGMD 2076
Cdd:PRK11288 359 hHLRAGCLINNRWEAENA---DRFIRSLN-IKtpSREQLIMNLSGGNQQKailgrwLSEDMK------VILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 2077 PKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2121 |
7.89e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.11 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKR---KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL--------S 1979
Cdd:COG1101 1 MLELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1980 NIHEVHQN--MGYCPQfdaitelLTGREHV-------EFFALLRGVPEKEVGKVGEW-AIRKLGLvkygEKY----AGNY 2045
Cdd:COG1101 81 YIGRVFQDpmMGTAPS-------MTIEENLalayrrgKRRGLRRGLTKKRRELFRELlATLGLGL----ENRldtkVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2046 SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRsvvLTS----HSMEECEALCTRMAIMVNGR 2121
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1927-2121 |
1.01e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-----NIHEVHQNMGYCPQFdAITELL 2001
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQF-PESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2002 --TGREHVEFFALLRGVPEKEVGKVgewAIRKLGLVKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2075
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAEAL---AREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 2076 DPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
916-1097 |
1.14e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLalnFYEGQITSFLGHNGAGKTTTMSILTGlfppTSGTAYILGKDI----RSEMSTIRQNLGVCPQHNVLFDMLTVE 991
Cdd:TIGR00956 782 VDGW---VKPGTLTALMGASGAGKTTLLNVLAE----RVTTGVITGGDRlvngRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 992 EHIWFYARLK-----GLSEK--HVKA-----EMEQMAlD--VGLPSSKLKSKtsqlsggmQRK-LSVALAFVGGSKVVI- 1055
Cdd:TIGR00956 855 ESLRFSAYLRqpksvSKSEKmeYVEEvikllEMESYA-DavVGVPGEGLNVE--------QRKrLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHH-----MDEADVL 1097
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1938-2102 |
1.15e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.56 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1938 PGECFGLLGVNGAGKSSTFKMLTGDTT--VTRGD----AFLNKNSILSNIHevhqnmGYCPQFDAITELLTGREHVEFFA 2011
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDirisGFPKKQETFARIS------GYCEQNDIHSPQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2012 LLRgVPeKEVGK------VGEwAIRKLGLVKYGEKYAG-----NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2080
Cdd:PLN03140 979 FLR-LP-KEVSKeekmmfVDE-VMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180
....*....|....*....|..
gi 21536376 2081 RFLWNCALSVVKEGRSVVLTSH 2102
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
892-1109 |
1.21e-10 |
|
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: 63.20 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 892 PTHLKlgVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMST 970
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 971 IRQNLGVCPQHNVLFdMLTVEEHIWFYARlkgLSEKHVKAemeqmALDVglpssklKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03369 80 LRSSLTIIPQDPTLF-SGTIRSNLDPFDE---YSDEEIYG-----ALRV-------SEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKL 1109
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1912-2103 |
1.44e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIyrRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-KNSILSNIHEV-----H 1985
Cdd:PRK13539 3 LEGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNmgycpqfdAITELLTGREHVEFFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13539 81 RN--------AMKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536376 2066 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHS 2103
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1911-2121 |
1.45e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrkrkPAV---DRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------KNSIL 1978
Cdd:COG3845 5 ALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1979 SNIHEVHQN-MgycpQFDAIT--E-LLTGREHVEFFALLRGVPEKEVGKVGEwairklglvKYG-----EKYAGNYSGGN 2049
Cdd:COG3845 80 LGIGMVHQHfM----LVPNLTvaEnIVLGLEPTKGGRLDRKAARARIRELSE---------RYGldvdpDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2050 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
889-1109 |
2.81e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 889 EEEPTHLKLGVSI--QNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFPPTSGTAYILGKDIRS 966
Cdd:PRK11174 338 GEKELASNDPVTIeaEDLEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 967 -EMSTIRQNLGVCPQHNVLFDMlTVEEHIwfyarLKG---LSEKHVKAEMEQM-------ALDVGLpSSKLKSKTSQLSG 1035
Cdd:PRK11174 416 lDPESWRKHLSWVGQNPQLPHG-TLRDNV-----LLGnpdASDEQLQQALENAwvseflpLLPQGL-DTPIGDQAAGLSV 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1036 GMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKL 1109
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1927-2150 |
2.93e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 HVEFFA---LLRGVPEKEVGK-VGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD-PKAR 2080
Cdd:PRK09536 97 VVEMGRtphRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2081 RFLwNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG------SVQHLKNRFgDGYTIVvriaGSNP 2150
Cdd:PRK09536 177 RTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAF-DARTAV----GTDP 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
919-1109 |
3.45e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC------PQHNVLFDM----- 987
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 988 ---LTVEEHIWFyarlkgLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PRK15439 362 vcaLTHNRRGFW------IKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1065 PYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
915-1123 |
4.03e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEH 993
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 994 IwFYARlkglSEKHVKAEMEQMA-----------LDVGLPSSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:PRK11176 437 I-AYAR----TEQYSREQIEEAArmayamdfinkMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 1063 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGSSLFLKNQLG 1123
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
915-1064 |
4.54e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNLGVCPQHNV--LFDML 988
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHI-----WFYARlkgLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PRK15079 116 TIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
.
gi 21536376 1064 D 1064
Cdd:PRK15079 193 D 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1916-2121 |
5.12e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.35 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1916 ELTKIYRRKRKPAVDRICVgIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-------------------KNS 1976
Cdd:cd03298 2 RLDKIRFSYGEQPMHFDLT-FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaappadrpvsmlfqENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1977 ILSNIhEVHQNMGYCpqfdaitelLTGREHveffalLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:cd03298 81 LFAHL-TVEQNVGLG---------LSPGLK------LTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
890-1109 |
5.50e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 890 EEPTHLKLG--VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtAYILGkdiRSE 967
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---TAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 MSTIRQNLGVCPQHNVLFDMLTVEEHIwfyarlkGLSEK-HVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:PRK11247 76 LAEAREDTRLMFQDARLLPWKKVIDNV-------GLGLKgQWRDAALQ-ALAaVGL-ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
921-1089 |
6.19e-10 |
|
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: 64.43 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 921 LNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--------RSEMSTIRQNlgvcpQHnvLFDMLtve 991
Cdd:COG4615 353 LTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreayRQLFSAVFSD-----FH--LFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 992 ehiwfYARLKGLSEKHVKAEMEQMALDvglpsSKLKSK-----TSQLSGGmQRK-LSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:COG4615 422 -----LGLDGEADPARARELLERLELD-----HKVSVEdgrfsTTDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDP 490
|
170 180
....*....|....*....|....*....
gi 21536376 1066 YSRRgiW---ELL--LKyRQGRTIILSTH 1089
Cdd:COG4615 491 EFRR--VfytELLpeLK-ARGKTVIAISH 516
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
900-1112 |
7.08e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 900 SIQNLVKVYRDGMKV--AVDGLALNFYEGQITSFLGHNGAGKT-TTMSILTGLfpPTSGTAYILGkDIR----------- 965
Cdd:PRK15134 7 AIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 966 --------SEMSTIRQNLGVC--PQHNV---LFDMLTVEehiwfyarlKGLSEKHVKAEMEQMALDVGL--PSSKLKSKT 1030
Cdd:PRK15134 84 qtlrgvrgNKIAMIFQEPMVSlnPLHTLekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1031 SQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
....
gi 21536376 1109 lcCV 1112
Cdd:PRK15134 235 --CV 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
928-1114 |
7.09e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 63.21 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 928 ITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMSTIRQNLGVCPQHNVLFDMLTVEEHIWF-YARLK 1001
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1002 GLSEKHVKAEMEQMaldVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ- 1080
Cdd:TIGR02142 105 PSERRISFERVIEL---LGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAe 180
|
170 180 190
....*....|....*....|....*....|....*
gi 21536376 1081 -GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:TIGR02142 181 fGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1926-2141 |
7.61e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT-------GDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1999 ELLTGREHVEFFALLRGVPEK-EVGKVGEWAIRKLGLVKygEKY------AGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWK--EVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2072 TTGMDPKARRFLWNCaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRFGDGYTI 2141
Cdd:PRK14246 181 TSMIDIVNSQAIEKL-ITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1912-2121 |
7.85e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT-----GDTTVTRGDAFLNKNSILSN----IH 1982
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpEAGTIRVGDITIDTARSLSQqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 EVHQNMGYCPQFDAITELLTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1932-2131 |
8.97e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1932 ICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFdaiTELLTGREH 2006
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQF---PEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2007 VE----FFALLRGVPEKEVGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK13634 103 VEkdicFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2082 FLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:PRK13634 183 EMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1911-2121 |
9.68e-10 |
|
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: 61.74 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYR-------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAF--------LNKN 1975
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1976 SILSNIHEVHQNMGYCPqfDAITELLTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKL 2053
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSP--SAVNPRMTVRQIIgEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2054 STAMALIGGPPVVFLDEPTTGMDpkarRFLWNCALSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
888-1118 |
9.80e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 888 MEEEPTHLKLGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE 967
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVS--FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 968 MS-TIRQNLGVCPQHNVLFDMLTVEEHI------WFYARLKGLSEKHVKAEmEQMALdVGLP--SSKLkskTSQLSGGMQ 1038
Cdd:PRK10575 79 SSkAFARKVAYLPQQLPAAEGMTVRELVaigrypWHGALGRFGAADREKVE-EAISL-VGLKplAHRL---VDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSL 1116
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
..
gi 21536376 1117 FL 1118
Cdd:PRK10575 234 EL 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
899-1109 |
1.00e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYR------DGMK------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyil 960
Cdd:PRK13546 5 VNIKNVTKEYRiyrtnkERMKdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 961 gkDIRSEMSTIRQNLGVCPQhnvlfdmLTVEEHIWFYARLKGLSEKHVKAEMEQMaldvgLPSSKLKSKTSQ----LSGG 1036
Cdd:PRK13546 82 --DRNGEVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKI-----IEFSELGEFIYQpvkkYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1037 MQRKLSVALAFVGGSKVVILDEP-TAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1908-2081 |
1.03e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.81 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-----KNSIlsnih 1982
Cdd:PRK11432 3 QKNFVVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1983 evhQNMGYCPQFD--AITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:PRK11432 76 ---QQRDICMVFQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180
....*....|....*....|.
gi 21536376 2061 GGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRR 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1912-2121 |
1.31e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKiyrrkrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN----------- 1980
Cdd:PRK10762 258 LKVDNLSG-------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1981 -IHE------------VHQNMGYCpqfdAITEL--LTGRehveffalLRGVPEKEVgkVGEWaIRkLGLVKYG--EKYAG 2043
Cdd:PRK10762 331 yISEdrkrdglvlgmsVKENMSLT----ALRYFsrAGGS--------LKHADEQQA--VSDF-IR-LFNIKTPsmEQAIG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2044 NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
911-1108 |
1.89e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL--G-----KDIR-SE---MSTIRQNLGVCP 979
Cdd:NF040905 13 GVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILfdGevcrfKDIRdSEalgIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 980 QhnvlfdmLTVEEHIWF---YARlKGL---SEKHVKAEmEQMAlDVGL---PSSKLKsktsQLSGGMQRKLSVALAFVGG 1050
Cdd:NF040905 92 Y-------LSIAENIFLgneRAK-RGVidwNETNRRAR-ELLA-KVGLdesPDTLVT----DIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1108
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1925-2121 |
2.05e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.41 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1925 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsnihevhqnMGYCPQFDAItelLTG- 2003
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWI---QNGt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2004 -REHVEFfallrGVPEKEvgkvgEW---AIRKLGLVK------------YGEKyaG-NYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03250 82 iRENILF-----GKPFDE-----ERyekVIKACALEPdleilpdgdlteIGEK--GiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2067 FLDEPTTGMDPKARRFLW-NCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2121
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1936-2076 |
2.38e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAF-----LNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFF 2010
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2011 ALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK11629 112 LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1912-2102 |
2.56e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.84 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsnihevhQNMGYC 1991
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFdaitelltgrehveffallrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNcALSvvKEGRSVVLTSH 2102
Cdd:cd03221 98 TNHLDLESIEALEE-ALK--EYPGTVILVSH 125
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1936-2122 |
2.66e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI--LSNIHEVHQNMGYCPQ--------FDA-----ITEL 2000
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnVCAL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2001 LTGRehVEFFalLRgvPEKEvGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2079
Cdd:PRK15439 366 THNR--RGFW--IK--PARE-NAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536376 2080 RRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1937-2076 |
3.15e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1937 PPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF------ 2009
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwh 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2010 FALLR-GVPEKEvgKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK10575 115 GALGRfGAADRE--KVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
899-1110 |
3.82e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQnlgv 977
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRK---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 cpqhnvLFDmlTVEEHIWFYARLKGLSEKHVKAEmeqmALDVGLPSSKLKSKTS---------QLSGGMQRKLSVALAFV 1048
Cdd:PRK10522 398 ------LFS--AVFTDFHLFDQLLGPEGKPANPA----LVEKWLERLKMAHKLEledgrisnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHmDEADVLGDRIAIISHGKLC 1110
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
921-1107 |
4.11e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYARL 1000
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 KglSEKHVKA---EMEQMALDV--GLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL 1075
Cdd:PLN03232 706 E--SERYWRAidvTALQHDLDLlpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
170 180 190
....*....|....*....|....*....|...
gi 21536376 1076 LKYR-QGRTIILSTHHMDEADVLgDRIAIISHG 1107
Cdd:PLN03232 784 MKDElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
899-1114 |
4.42e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNL-VKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI--------------LGK 962
Cdd:PRK10261 13 LAVENLnIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrqvieLSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 963 DIRSEMSTIR-QNLGVCPQHNV--LFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGG 1036
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1037 MQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1114
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1911-2122 |
4.76e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYrrkrkP---AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGdttVTRGDA----FLNKNSILSN--- 1980
Cdd:PRK10762 4 LLQLKGIDKAF-----PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG---IYTRDAgsilYLGKEVTFNGpks 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1981 -----IHEVHQNMGYCPQFDAITELLTGREHVEFFAllrGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLST 2055
Cdd:PRK10762 76 sqeagIGIIHQELNLIPQLTIAENIFLGREFVNRFG---RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1911-2121 |
5.19e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGDAFLNKNSI----LS 1979
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYWSGSPLKASNIrdteRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1980 NIHEVHQNMGYCPQFDAITELLTGREhveffALLRG--VPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNE-----ITLPGgrMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1888-2076 |
5.28e-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: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1888 LNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--- 1961
Cdd:TIGR03719 296 LLSQEFQKRNETAEIYIPPGPrlgDKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqeq 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1962 -DT-TVTRGDAflnknsilsniheVHqnMGYCPQFdaiTELLTGREHVeFFALLRGVPEKEVGKVgEWAIRK-LGLVKYG 2038
Cdd:TIGR03719 374 pDSgTIEIGET-------------VK--LAYVDQS---RDALDPNKTV-WEEISGGLDIIKLGKR-EIPSRAyVGRFNFK 433
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536376 2039 ----EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:TIGR03719 434 gsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
921-1064 |
6.68e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 921 LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIW 995
Cdd:cd03233 26 FSGVvkPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLD 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 996 FYARLKGlsekhvkaemEQMaldvglpssklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:cd03233 106 FALRCKG----------NEF--------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1909-2120 |
7.01e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELtkIYRRKRKPAVDR---ICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEV 1984
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 HQNMGYCPQF-DAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNG 2120
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1909-2126 |
7.65e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIYR--RKRKP----------------AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDa 1970
Cdd:PRK13546 2 NVSVNIKNVTKEYRiyRTNKErmkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1971 fLNKNSILSNIhevHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNK 2050
Cdd:PRK13546 81 -VDRNGEVSVI---AISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2051 RKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNCaLSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2126
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGD---QTFAQKC-LDKIYEfkeqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1912-2135 |
7.80e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDttvtrgDAFLNKNSilsnihEVHQNMGYC 1991
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM------DQYEPTSG------RIIYHVALC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQF-------------------------------DAITELLTGREHVEF---FAL------LRGVPE--KEVGKVGEWAI 2029
Cdd:TIGR03269 67 EKCgyverpskvgepcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLqrtFALygddtvLDNVLEalEEIGYEGKEAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2030 RK----LGLVKYGEKY---AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTS 2101
Cdd:TIGR03269 147 GRavdlIEMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 21536376 2102 HSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRF 2135
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1912-2131 |
8.36e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIHE--VHQNMG 1989
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 YCPQfdaitelltgREHVeFFALLR-----GVPEKEVGKVGEwAIRKLGLVKYGEKYAG----------NYSGGNKRKLS 2054
Cdd:PRK11160 418 VVSQ----------RVHL-FSATLRdnlllAAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2055 TAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE---GRSVVLTSH---SMEECEALCtrmaIMVNGRFRCLGSV 2128
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQI----LELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTH 557
|
...
gi 21536376 2129 QHL 2131
Cdd:PRK11160 558 QEL 560
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
926-1090 |
8.74e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFyarlkGLSE 1005
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY-----DIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1006 KHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTI 1084
Cdd:PRK13540 102 SPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAV 180
|
....*.
gi 21536376 1085 ILSTHH 1090
Cdd:PRK13540 181 LLTSHQ 186
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1925-2126 |
8.91e-09 |
|
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: 60.53 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1925 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHEVHQNMGYCPQfdaitelltg 2003
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsQWDREELGRHIGYLPQ---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2004 reHVEFF--------ALLRGV-PEKevgkVGEWA--------IRKL--GlvkY----GEkyAGNY-SGGNKRKLSTAMAL 2059
Cdd:COG4618 414 --DVELFdgtiaeniARFGDAdPEK----VVAAAklagvhemILRLpdG---YdtriGE--GGARlSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKE-GRSVVLTSHSMeecEAL--CTRMAIMVNGRFRCLG 2126
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKArGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1911-2121 |
9.05e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKiyrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL-SNIHEVHQNmg 1989
Cdd:PRK10982 250 ILEVRNLTS----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINH-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1990 ycpQFDAITEL-----LTGREHVEFFALLRGVpEKEVGKVG-----------EWAIRKLGLVKYGEKYA-GNYSGGNKRK 2052
Cdd:PRK10982 324 ---GFALVTEErrstgIYAYLDIGFNSLISNI-RNYKNKVGlldnsrmksdtQWVIDSMRVKTPGHRTQiGSLSGGNQQK 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2053 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1936-2134 |
9.48e-09 |
|
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: 59.74 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--------KNSILSnIHE-----VHQNMGYCPQFDAITELLT 2002
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsrKGIFLP-PEKrrigyVFQEARLFPHLSVRGNLRY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2003 GREHVEffALLRGVPEKEVgkvgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR- 2081
Cdd:TIGR02142 99 GMKRAR--PSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYe 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2082 ---FLWNCALSVvkeGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR 2134
Cdd:TIGR02142 170 ilpYLERLHAEF---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
926-1102 |
9.83e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 60.60 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF-DmlTVEEHIWfYARLkGL 1003
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRP-DA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1004 SEkhvkAEMEQMA----LD---VGLPSSK--------LKsktsqLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDP 1065
Cdd:COG5265 460 SE----EEVEAAAraaqIHdfiESLPDGYdtrvgergLK-----LSGGeKQR---VAIArtLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21536376 1066 YSRRGIWELLLKYRQGRT--II---LST-HHMDEADVLGD-RIA 1102
Cdd:COG5265 528 RTERAIQAALREVARGRTtlVIahrLSTiVDADEILVLEAgRIV 571
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2015-2105 |
1.03e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2015 GVPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE 2093
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90
....*....|..
gi 21536376 2094 GRSVVLTSHSME 2105
Cdd:PRK13631 226 NKTVFVITHTME 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1912-2128 |
1.08e-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: 57.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGDAFLNKNSILS-NIHEvHQNM 1988
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDlPPEE-RARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 G------YCPQFDAITelltgrehVEFFalLRGVPEkevgkvgewairklglvkygekyagNYSGGNKRKLSTAMALIGG 2062
Cdd:cd03217 78 GiflafqYPPEIPGVK--------NADF--LRYVNE-------------------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 2063 PPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEAL-CTRMAIMVNGRFRCLGSV 2128
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
923-1064 |
1.24e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 923 FYEGQITSFLGHNGAGKTTTMSILTGlfPPTSGtaYILGkDIRSEMSTIRQNL-----GVCPQHNVLFDMLTVEEHIWFY 997
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISGFPKKQETfarisGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 998 ARLK-----GLSEK--HVKAEMEQMALD------VGLPSsklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PLN03140 978 AFLRlpkevSKEEKmmFVDEVMELVELDnlkdaiVGLPG------VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
901-1107 |
1.31e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 57.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKVY----RDGMK-VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILgkdIRSEMSTIrqnl 975
Cdd:COG4778 7 VENLSKTFtlhlQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS--IL---VRHDGGWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 gvcpqhnvlfDMLTVEEHIWFYARlkglseKH--------------VKAE--MEQMALDVGLPSSKLKSKTSQL------ 1033
Cdd:COG4778 78 ----------DLAQASPREILALR------RRtigyvsqflrviprVSALdvVAEPLLERGVDREEARARARELlarlnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1034 ------------SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDR 1100
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADR 221
|
....*..
gi 21536376 1101 IAIISHG 1107
Cdd:COG4778 222 VVDVTPF 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1921-2105 |
1.36e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.48 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1921 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAF-------LNKNSILSniheVHQNMGYCPQ 1993
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldYSKRGLLA----LRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1994 FDAITELLTGREHVEFFALLR-GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190
....*....|....*....|....*....|...
gi 21536376 2073 TGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2105
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1911-2108 |
1.40e-08 |
|
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: 57.48 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYR-RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHE-VHQNM 1988
Cdd:cd03248 11 IVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GycpqfdaitelLTGREHVEFFALLR-----GVPEKEVGKVGEWA--------IRKLGLVKY---GEKyAGNYSGGNKRK 2052
Cdd:cd03248 91 S-----------LVGQEPVLFARSLQdniayGLQSCSFECVKEAAqkahahsfISELASGYDtevGEK-GSQLSGGQKQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2053 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKEGRSVVLTSHSMEECE 2108
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVE 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1921-2136 |
1.55e-08 |
|
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: 57.50 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1921 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI-LSNIHEVHQNMGYCPQfdaiTE 1999
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2000 LLTGREHVEFFALLR-GVPEKEVGKVGEWA-----IRKLGL---VKYGEKYAGnYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:cd03252 86 VLFNRSIRDNIALADpGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2071 PTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFG 2136
Cdd:cd03252 165 ATSALDYESEHAIMR-NMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1887-2121 |
1.77e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1887 PLNDEDEDVRRERQRILDGGGQND-ILEIKELTKIY--------RRKRK-PAVDRICVGIPPGECFGLLGVNGAGKSSTF 1956
Cdd:PRK10261 288 PLISLEHPAKQEPPIEQDTVVDGEpILQVRNLVTRFplrsgllnRVTREvHAVEKVSFDLWPGETLSLVGESGSGKSTTG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1957 KMLTGDTTVTRGDAFLNKNSI----LSNIHEVHQNMGYCPQ------------FDAITELLtgREHveffALLRGvpeKE 2020
Cdd:PRK10261 368 RALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQdpyasldprqtvGDSIMEPL--RVH----GLLPG---KA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2021 VGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVV 2098
Cdd:PRK10261 439 AAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYL 518
|
250 260
....*....|....*....|...
gi 21536376 2099 LTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK10261 519 FISHDMAVVERISHRVAVMYLGQ 541
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
921-1108 |
1.84e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.71 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKdirsemstirqnLGVCPQHNVLFDMlTVEEHIWFYARL 1000
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQNG-TIRENILFGKPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 -KGLSEKHVKA-----EMEQMAL----DVGlpssklkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:cd03250 93 dEERYEKVIKAcalepDLEILPDgdltEIG-------EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536376 1071 IWELLL--KYRQGRTIILSTHHMD---EAdvlgDRIAIISHGK 1108
Cdd:cd03250 166 IFENCIlgLLLNNKTRILVTHQLQllpHA----DQIVVLDNGR 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
926-1090 |
2.29e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDiRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL---KG 1002
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1003 LSEKHVKAEMEQMALDVGLPSSKL----KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR-RGIWELLLK 1077
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENtiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSL 252
|
170
....*....|...
gi 21536376 1078 YRQGRTIILSTHH 1090
Cdd:PLN03211 253 AQKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1944-2127 |
2.46e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1944 LLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQ------NMGYC---PQFDAITEllTGREHVEFFALLR 2014
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVfqfPEYQLFQE--TIEKDIAFGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2015 GVPEKEV-GKVGEWairkLGLVKYGEKYAG----NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2089
Cdd:PRK13645 120 GENKQEAyKKVPEL----LKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536376 2090 VVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2127
Cdd:PRK13645 196 LNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
899-1114 |
3.02e-08 |
|
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: 59.57 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 978
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 pQHNVLFDmltveehiwfyarlKGLSEKHVKAEMEQMAL--DVG-LPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:TIGR00957 716 -RENILFG--------------KALNEKYYQQVLEACALlpDLEiLPSgdrTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1053 VVILDEPTAGVDPYSRRGIWELLLKYR---QGRTIILSTHHMD---EADVlgdrIAIISHGKLCCVGS 1114
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISylpQVDV----IIVMSGGKISEMGS 844
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1939-2105 |
3.47e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsNIHEVHQNMGYCPQFDAIT-ELLTGR-----EHV---EF 2009
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKVADKNQlRLLRTRltmvfQHFnlwSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2010 FALLRGVPEKEVGKVG-------EWAIRKLGLVKYGEKYAGNY----SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2078
Cdd:PRK10619 107 MTVLENVMEAPIQVLGlskqearERAVKYLAKVGIDERAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*..
gi 21536376 2079 ARRFLWNCALSVVKEGRSVVLTSHSME 2105
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1928-2122 |
3.61e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------KNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfastTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1999 ELLTGREHVEFFALLRGVPEKEVGKvgewAIRKLGL-------VKYgekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK11288 99 NLYLGQLPHKGGIVNRRLLNYEARE----QLEHLGVdidpdtpLKY-------LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2072 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
919-1089 |
3.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGVCPQhnvlfdmLTVEEHI 994
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLGLKLE-------MTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 995 WFYarlkglSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1074
Cdd:PRK13541 92 KFW------SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*.
gi 21536376 1075 L-LKYRQGRTIILSTH 1089
Cdd:PRK13541 166 IvMKANSGGIVLLSSH 181
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1926-2134 |
3.79e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSST----FKMLTGDTTVTRGDAFLNKNSILSN------IHEVHQNmgycPQfD 1995
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgrkIATIMQN----PR-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1996 AITELLTGREHVEFFALLRGVPEKEVGKVGewAIRKLGLVKYG---EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2073 TGMDPKAR-RFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR 2134
Cdd:PRK10418 169 TDLDVVAQaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1928-2137 |
3.95e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEvhqnmgycpqfdAITELLTGREHV 2007
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2008 EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNC- 2086
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKKCl 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2087 -ALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2137
Cdd:PRK13545 184 dKMNEFKEqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
910-1089 |
4.30e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMSTIRQNlgvcpQHN 982
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRAE-----QIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 983 VLF-DMLT-------VEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSKLKSKT--SQLSGGMQRKLSVALAFVGGS 1051
Cdd:PRK09473 101 MIFqDPMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536376 1052 KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTH 1089
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1909-2123 |
5.77e-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: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1909 NDILEIKELTKIY----RRKRkpaVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGD-TTVTRGDAFLNKNSI------ 1977
Cdd:TIGR02633 255 DVILEARNLTCWDvinpHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnpa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1978 ------LSNIHEVHQNMGYCPQFdAITELLTGREHVEFFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYA-GNYSGGNK 2050
Cdd:TIGR02633 332 qairagIAMVPEDRKRHGIVPIL-GVGKNITLSVLKSFCFKMRIDAAAELQIIGS-AIQRLKVKTASPFLPiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2051 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2123
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1915-2120 |
7.45e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1915 KELTKIYRRK---RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN-----IHEVHQ 1986
Cdd:PRK13646 6 DNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQF--DAITELLTGREhVEFFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:PRK13646 86 RIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2064 PVVFLDEPTTGMDPKARRFLWNCALSV-VKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1932-2133 |
9.61e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.41 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1932 ICVGIPPGECFGLLGVNGAGKSSTFKML-------TGDTTVTrGDAF-LNKNSILSNIHEVHQNMGYCPQFDAITELLTG 2003
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIA-GNHFdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2004 REH-VEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrf 2082
Cdd:PRK11124 100 QQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2083 LWNCALSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2133
Cdd:PRK11124 176 ITAQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1926-2131 |
9.77e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GDAFLNKNSILS--NIHEVHQNMGYCPQ----- 1993
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSGYRysGDVLLGGRSIFNyrDVLEFRRRVGMLFQrpnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1994 -FDAITELLTG-REHV-----EFfallRGVPEKEVGKVGEWAIRKLGLvkygEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK14271 114 pMSIMDNVLAGvRAHKlvprkEF----RGVAQARLTEVGLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2067 FLDEPTTGMDP----KARRFLWNCAlsvvkEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:PRK14271 186 LLDEPTSALDPttteKIEEFIRSLA-----DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
911-1087 |
9.80e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYiLGKDIRsemstirqnLGVCPQHNVLFdMLTV 990
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-LAKGIK---------LGYFAQHQLEF-LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 991 EEHIWFYARLkglsekhVKAEMEQMALD----VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:PRK10636 392 ESPLQHLARL-------APQELEQKLRDylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|.
gi 21536376 1067 SRRGIWELLLKYrQGRTIILS 1087
Cdd:PRK10636 465 MRQALTEALIDF-EGALVVVS 484
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1032-1089 |
1.08e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.52 E-value: 1.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1032 QLSGGMQRKLSVALAF----VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTH 1089
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITH 139
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1912-2121 |
1.22e-07 |
|
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: 57.03 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNK--------NSILSNIHE 1983
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 VHQNMGYcpqFDAitellTGREHVEFFALlRGVPEKEVGKVGEWAIRK-------LGL-VKYGEKyAGNYSGGNKRKLST 2055
Cdd:TIGR02203 411 VSQDVVL---FND-----TIANNIAYGRT-EQADRAEIERALAAAYAQdfvdklpLGLdTPIGEN-GVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2056 AMALIGGPPVVFLDEPTTGMDPKARRfLWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2121
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGR 544
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1911-2122 |
1.36e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTkIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI------------L 1978
Cdd:COG3845 257 VLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrrlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1979 SNIHEVHQNMGYCPQFDaITE--LLTGREHVEF--FALLRGvpekevGKVGEWAIRKLglvkygEKY----------AGN 2044
Cdd:COG3845 336 AYIPEDRLGRGLVPDMS-VAEnlILGRYRRPPFsrGGFLDR------KAIRAFAEELI------EEFdvrtpgpdtpARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2045 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1913-2102 |
1.41e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1913 EIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:COG4604 3 EIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEF--FALLRGVPEKE-VGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrFPYSKGRLTAEdREIIDE-AIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536376 2069 DEPTTGMDPKA--------RRflwncalsVVKE-GRSVVLTSH 2102
Cdd:COG4604 160 DEPLNNLDMKHsvqmmkllRR--------LADElGKTVVIVLH 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1912-2129 |
1.60e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNIHEVHQNMGYC 1991
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 PQFDAITELLTGREHVEFFalLRGVPEKEvgKVGEWAIRK-----LGLVKYG---EKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG--LTVLPRRE--RPNAAAIKAkvtqlLEMVQLAhlaDRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2064 PVVFLDEPTTGMDPKARRFL--WNCALSVVKEGRSVVLTsHSMEECEALCTRMAIMVNGRFRCLGSVQ 2129
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELrrWLRQLHEELKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1938-2076 |
1.83e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1938 PGECFGLLGVNGAGKSSTFKMLTGDTTVT---RGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLR 2014
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2015 GvpeKEVgkvgewaIRKLglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:cd03233 112 G---NEF-------VRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
899-1092 |
2.03e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIWFYARLKglsekhvKAEMEQMALDVGLPSS----------KLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQWS-------DEEIWKVAEEVGLKSVieqfpdkldfVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMD 1092
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
899-1109 |
2.59e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGV 977
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLF------DMLTVEEH----IWfyarlKGLSEKHVKAEMEQMALdvGLpSSKLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:PLN03232 1315 IPQSPVLFsgtvrfNIDPFSEHndadLW-----EALERAHIKDVIDRNPF--GL-DAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1109
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
911-1114 |
2.68e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyilgkdIRSEMSTIrqnlGVCPQhNVLFDM--- 987
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRI----GYVPQ-KLYLDTtlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 988 LTVEEhiwfYARLKGlsekHVKAEMEQMALDVGLPSSKLKSKTSQLSGG-MQRKLsVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:PRK09544 84 LTVNR----FLRLRP----GTKKEDILPALKRVQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536376 1067 SRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHgKLCCVGS 1114
Cdd:PRK09544 155 GQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGT 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1908-2121 |
2.72e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS--NIHEVH 1985
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMGYCPQFDAITELLTGREHVE---FFALlRGVPEKEVGKVGEWAIRklgLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAmggFFAE-RDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2063 PPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1911-2120 |
2.77e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT--GD----TTVTrgdaflnkNSILSNIHEV 1984
Cdd:PRK14239 5 ILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpeVTIT--------GSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1985 hqnmgYCPQFDAItEL---------------LTGREHVEFFALLRGVPEKEV-GKVGEWAIRKLGL---VK-YGEKYAGN 2044
Cdd:PRK14239 75 -----YSPRTDTV-DLrkeigmvfqqpnpfpMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdeVKdRLHDSALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2045 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSvVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1911-2121 |
2.81e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIY-RRKrkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA-FLNKNSILSNIHE----- 1983
Cdd:PRK11701 6 LLSVRGLTKLYgPRK---GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYAlseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 -----------VHQN--MGYCPQFDA---ITElltgRehveffalLRGVPEKEVGKVGEWAIRKLGLVKYGEK----YAG 2043
Cdd:PRK11701 83 rrrllrtewgfVHQHprDGLRMQVSAggnIGE----R--------LMAVGARHYGDIRATAGDWLERVEIDAAriddLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2044 NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD--PKARrfLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
.
gi 21536376 2121 R 2121
Cdd:PRK11701 229 R 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1927-2076 |
3.09e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 55.90 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1927 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIlSNI--HEVHQNMGYCPQ----FD-AITE 1999
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIdrHTLRQFINYLPQepyiFSgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2000 -LLTGREhveffallRGVPEKEVGKVGEWA-IRK------LGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:TIGR01193 567 nLLLGAK--------ENVSQDEIWAACEIAeIKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 21536376 2072 TTGMD 2076
Cdd:TIGR01193 639 TSNLD 643
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1926-2102 |
3.11e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 HVeFFALLRGVPEKEVGKVgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2085
Cdd:PRK13540 94 NC-LYDIHFSPGAVGITEL----CRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*..
gi 21536376 2086 CALSVVKEGRSVVLTSH 2102
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSH 185
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1912-2109 |
3.26e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 53.25 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTkIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTT---VTRGDAFLNKNSILS-NIHEvhQN 1987
Cdd:COG4136 2 LSLENLT-ITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTAlPAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1988 MGYCPQfdaiTELLtgrehveF----------FALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:COG4136 78 IGILFQ----DDLL-------FphlsvgenlaFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2058 ALIGGPPVVFLDEPTTGMDP----KARRFLWNcalSVVKEGRSVVLTSHSMEECEA 2109
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAalraQFREFVFE---QIRQRGIPALLVTHDEEDAPA 199
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
915-1089 |
4.49e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYIL---GKDIR------------SEMSTIRQN--LG 976
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLefnGQDLQrisekerrnlvgAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 977 VCPQHNVLFD-MLTVEEHiwfyarlKGLSekhvKAEMEQMALD----VGLP--SSKLKSKTSQLSGGMQRKLSVALAFVG 1049
Cdd:PRK11022 102 LNPCYTVGFQiMEAIKVH-------QGGN----KKTRRQRAIDllnqVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536376 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTH 1089
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITH 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
901-1115 |
4.55e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 901 IQNLVKV--YRDGM-----KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK-----DIRSEM 968
Cdd:PRK15112 7 VRNLSKTfrYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 969 STIRQ-----NLGVCPQHNV--LFDM-------LTVEEHiwfyarlkglsEKHVKAEMEQmaldVGLPSSKLKSKTSQLS 1034
Cdd:PRK15112 87 QRIRMifqdpSTSLNPRQRIsqILDFplrlntdLEPEQR-----------EKQIIETLRQ----VGLLPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1035 GGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCV 1112
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
...
gi 21536376 1113 GSS 1115
Cdd:PRK15112 232 GST 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1921-2114 |
5.57e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1921 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNihEVHQNMGYCPQFDAITEL 2000
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2001 LTGREHVEFFALLRGV-PEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2079
Cdd:PRK13543 97 LSTLENLHFLCGLHGRrAKQMPGS----ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180 190
....*....|....*....|....*....|....*
gi 21536376 2080 RRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRM 2114
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1912-2121 |
5.66e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.14 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDaFLNKNSILSNIHEVHQNMgyc 1991
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDTRLM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 pqfdaitelltgrehvefFALLRGVPEKEV------GKVGEW------AIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:PRK11247 87 ------------------FQDARLLPWKKVidnvglGLKGQWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKAR-------RFLWNcalsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRiemqdliESLWQ------QHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1938-2102 |
5.87e-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: 53.14 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1938 PGECFGLLGVNGAGKSSTFKMLTGdttvtrgdaflnknsilsnihEVHQNMG-YC--PQFDAITELLTGREHVEFFALLR 2014
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSELQNYFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2015 G--------------VPEKEVGKVGE------------WAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03236 84 EgdvkvivkpqyvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....
gi 21536376 2069 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2102
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
899-1109 |
6.40e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMlTVEEHIWFYarlkglsEKHVKAEMEQMALDVGLPSS----------KLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPY-------GKWSDEEIWKVAEEVGLKSVieqfpgqldfVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKL 1109
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
933-1065 |
6.97e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 933 GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVCPQhnvLFDMLTVEEHIWFyarLKGLSEKHVKaE 1011
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAK-Q 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 1012 MEQMALD-VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK13543 117 MPGSALAiVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
923-1108 |
7.14e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.22 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 923 FYEGqITSFLGHNGAGKTTTMS----ILTGLFPPTSGTAYILGKDIRSEMS----------------TIRQNLGV----- 977
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGEVraqvklafenangkkyTITRSLAIlenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 -CPQhnvlfdmltvEEHIWFYARLKGlsekhvkaemeqmaldvglpssklksktsQLSGGMQRKLSV----ALAFVGGSK 1052
Cdd:cd03240 99 fCHQ----------GESNWPLLDMRG-----------------------------RCSGGEKVLASLiirlALAETFGSN 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1053 --VVILDEPTAGVDPYSRRGIWELLLKYRQG---RTIILSTHHMDEADVLGD--RIAIISHGK 1108
Cdd:cd03240 140 cgILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1925-2076 |
7.63e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1925 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNI-HEVHQNMGYCPQfDAIT----- 1998
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRIGLLAQ-NATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1999 --ELLT-GR-EHVEFFALLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2074
Cdd:PRK10253 98 vqELVArGRyPHQPLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 21536376 2075 MD 2076
Cdd:PRK10253 174 LD 175
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1939-2076 |
1.32e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.80 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1939 GECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNKNSILsNIHEVHQNMGYCPQF-----DAITEL----LTGREH 2006
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREIL-NLPEKELNKLRAEQIsmifqDPMTSLnpymRVGEQL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 2007 VEFFALLRGVPEKEVGkvgEWAIRKLGLVKYGEK------YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK09473 121 MEVLMLHKGMSKAEAF---EESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
926-1091 |
1.41e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.56 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-----RQNLGVCPQHNVLFDMlTVEEHIWFYARL 1000
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1001 kglSEKHVKAEMEQMAL--DVGL----PSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY-SRRGIWE 1073
Cdd:cd03290 106 ---NKQRYKAVTDACSLqpDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQE 182
|
170 180
....*....|....*....|
gi 21536376 1074 LLLKYRQG--RTIILSTHHM 1091
Cdd:cd03290 183 GILKFLQDdkRTLVLVTHKL 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
897-1127 |
1.50e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 897 LGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILGKDI---RSEMSTIRQ 973
Cdd:PRK10789 314 LDVNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIpltKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 974 NLGVCPQHNVLFDMlTV------------EEHIWFYARLKGLSEKHVKaemeqmaldvgLPS---SKLKSKTSQLSGGMQ 1038
Cdd:PRK10789 390 RLAVVSQTPFLFSD-TVannialgrpdatQQEIEHVARLASVHDDILR-----------LPQgydTEVGERGVMLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKLCCVGSSLFL 1118
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQL 536
|
....*....
gi 21536376 1119 KNQlgTGYY 1127
Cdd:PRK10789 537 AQQ--SGWY 543
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1926-2102 |
1.54e-06 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnknSIL---SNIHEVHQN-----MGYCPQ---- 1993
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSG-------SILidgQDIREVTLDslrraIGVVPQdtvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1994 FDAITE--LLTGR-----EHVEFFA-------LLRGVPEKEVGKVGEwaiRKLGLvkygekyagnySGGNKRKLSTAMAL 2059
Cdd:cd03253 87 FNDTIGynIRYGRpdatdEEVIEAAkaaqihdKIMRFPDGYDTIVGE---RGLKL-----------SGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536376 2060 IGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSH 2102
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQA-ALRDVSKGRTTIVIAH 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
915-1113 |
1.85e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNLGVCPQ--HNVLFDML 988
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 989 TVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYS 1067
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536376 1068 RRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1113
Cdd:PRK10261 499 RGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2043-2123 |
2.07e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2043 GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2122
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
.
gi 21536376 2123 R 2123
Cdd:PRK13549 484 K 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
919-1109 |
2.64e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTI----------RQNLGVCPQHNVLFD 986
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 987 MLtVEEHIWFYARLKGLSEKHVKAEMEQM--ALDVGLPSSKlkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PRK10982 347 SL-ISNIRNYKNKVGLLDNSRMKSDTQWVidSMRVKTPGHR--TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536376 1065 PYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10982 424 VGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
899-1064 |
2.74e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLF------DMLTVEEH----IWfyarlKGLSEKHVKAEMEQMALdvGLpSSKLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:PLN03130 1318 IPQAPVLFsgtvrfNLDPFNEHndadLW-----ESLERAHLKDVIRRNSL--GL-DAEVSEAGENFSVGQRQLLSLARAL 1389
|
170
....*....|....*..
gi 21536376 1048 VGGSKVVILDEPTAGVD 1064
Cdd:PLN03130 1390 LRRSKILVLDEATAAVD 1406
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
899-1087 |
3.07e-06 |
|
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: 52.24 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRseMSTIRQNlgvc 978
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETVK--LAYVDQS---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 979 pqHNVLFDMLTVEEHIwfyarLKGLSEKHV-KAEMEQMALdVG---LPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:TIGR03719 394 --RDALDPNKTVWEEI-----SGGLDIIKLgKREIPSRAY-VGrfnFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|...
gi 21536376 1055 ILDEPTAGVDPYSRRGIWELLLKYrQGRTIILS 1087
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNF-AGCAVVIS 497
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1936-2076 |
3.50e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTtvtrgDAFL-NKNSILS-NIHEVHQNMG-------YCPQFDAITELLTGREH 2006
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNT-----DGFHiGVEGVITyDGITPEEIKKhyrgdvvYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2007 VEFFALLR-------GVPEKE-VGKVGEWAIRKLGL-----VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2073
Cdd:TIGR00956 159 LDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 21536376 2074 GMD 2076
Cdd:TIGR00956 239 GLD 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1911-2121 |
3.77e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSIL----SNIHEVHQ 1986
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2067 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
899-1093 |
3.98e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST---IRQNL 975
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSGETiwdIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GV------------CPQHNVL----FDmltveeHIWFYarlKGLSEKHVKAEMEQMALdVGLPSSKLKSKTSQLSGGMQR 1039
Cdd:PRK10938 339 GYvssslhldyrvsTSVRNVIlsgfFD------SIGIY---QAVSDRQQKLAQQWLDI-LGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536376 1040 KLSVALAFVGGSKVVILDEPTAGVDPYSR---RGIWELLLkyRQGRTIILSTHHMDE 1093
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI--SEGETQLLFVSHHAE 463
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1773-2105 |
5.88e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.47 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1773 VNLFIGINGSVATFVLELFtdnklnnindilksvflifphfclgRGLIDMVKNQAMADALERFGENRFVSPLSWDLvGRN 1852
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEAL-------------------------RFLADFDALVIGLTDERSRNGGIGGIPSLLNG-IDP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1853 LFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLND-------EDEDVRRERQRILDGGGQNDILEIKELTKIYRRKR 1925
Cdd:pfam13304 55 KEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTllekrllLREDSEEREPKFPPEAEELRLGLDVEERIELSLSE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1926 KPAVDRICVGIPPGECFgllgvNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEvhqnmgYCPQFDAITELLTGRE 2005
Cdd:pfam13304 135 LSDLISGLLLLSIISPL-----SFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR------LVRGLKLADLNLSDLG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 HVEFFALLRGVPEKEVGKVgeWAIRKLGlvkyGEKYAGNYSGGNKRKLSTAMALI---GGPPVVFLDEPTTGMDPKARRF 2082
Cdd:pfam13304 204 EGIEKSLLVDDRLRERGLI--LLENGGG----GELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRR 277
|
330 340
....*....|....*....|...
gi 21536376 2083 LWNCALSVVKEGRSVVLTSHSME 2105
Cdd:pfam13304 278 LLELLKELSRNGAQLILTTHSPL 300
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2042-2122 |
8.31e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2042 AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
.
gi 21536376 2122 F 2122
Cdd:NF040905 482 I 482
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
898-1107 |
9.84e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 898 GVSIQNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 977
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKTSQLSGGmQRKlSVAL--AFVGGSKV 1053
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAAriLELE---PLLDRKPRELSGG-QRQ-RVAMgrAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 1054 VILDEPTAGVDPYSR---RgiWELL-LKYRQGRTIILSTHHMDEADVLGDRIAIISHG 1107
Cdd:PRK11650 156 FLFDEPLSNLDAKLRvqmR--LEIQrLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1031-1089 |
1.39e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 49.31 E-value: 1.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1031 SQLSGGMQRKLSVALAF---VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRT-IILSTH 1089
Cdd:pfam13304 235 FELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1937-2121 |
1.52e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1937 PPGECFGLLGVNGAGKSSTFKML-------TGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREH-VE 2008
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPSEKAIRLLRQKVGMVFQQYNLWPHLTVMENlIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2009 FFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrfLWNCAL 2088
Cdd:COG4161 106 APCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQVV 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 21536376 2089 SVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:COG4161 182 EIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1936-2102 |
1.52e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTV-----TRGDAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF 2009
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2010 -FALLRGVPEK-EVGKVGEWAIRKLGL---VKYG-EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2083
Cdd:PRK14247 106 gLKLNRLVKSKkELQERVRWALEKAQLwdeVKDRlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170
....*....|....*....
gi 21536376 2084 WNCALSVVKEgRSVVLTSH 2102
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
909-1109 |
1.94e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG---------LFP---------------PTSGTAYILGKDi 964
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsyTFPgnwqlawvnqetpalPQPALEYVIDGD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 965 rSEMSTIRQNLGVCPQHNVLFDMLTVeehiwfYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVA 1044
Cdd:PRK10636 89 -REYRQLEAQLHDANERNDGHAIATI------HGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536376 1045 LAFVGGSKVVILDEPTAGVDPYSRrgIW-ELLLKYRQGrTIILSTHHMDEADVLGDRIAIISHGKL 1109
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAV--IWlEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
908-1114 |
1.96e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQHNVLFD 986
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYgLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 987 ---MLTVE-------EHIWFYARLKGLSEkHVKAEMEqmaldvGLPSSKLKSKtSQLSGGMQRKLSVALAFVG-GSKVVI 1055
Cdd:PTZ00243 1398 gtvRQNVDpfleassAEVWAALELVGLRE-RVASESE------GIDSRVLEGG-SNYSVGQRQLMCMARALLKkGSGFIL 1469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 1056 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLgDRIAIISHGKLCCVGS 1114
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
911-1080 |
2.11e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYILGKDI----RSEMSTIRQNLGVCPQ--HNVL 984
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 985 FDMLTVEEHIWFYARL--KGLS----EKHVKAEMEQMALDvglPSSKLKSKtSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSaaqrEQQVIAVMEEVGLD---PETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180
....*....|....*....|..
gi 21536376 1059 PTAGVDPYSRRGIWELLLKYRQ 1080
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQ 473
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
905-1091 |
2.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 905 VKVYRDgmkvavdgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG----KDIrsEMSTIRQNLGVCPQ 980
Cdd:PTZ00265 398 VEIYKD--------LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLFDML---TVEEHIWFYARLKGLSEK---------------------------------------HVKAEMEQM--- 1015
Cdd:PTZ00265 468 DPLLFSNSiknNIKYSLYSLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIkds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1016 -ALDV-----------GLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKY 1078
Cdd:PTZ00265 548 eVVDVskkvlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKG 627
|
250
....*....|...
gi 21536376 1079 RQGRTIILSTHHM 1091
Cdd:PTZ00265 628 NENRITIIIAHRL 640
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
916-1109 |
2.34e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 916 VDGLALNFYEGQITSFLGHNGAGKT-TTMSILT---GLFppTSGTAYILGKDIRseMSTI--------------RQNLGV 977
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyGRN--ISGTVFKDGKEVD--VSTVsdaidaglayvtedRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 978 cpqhnVLFDmlTVEEHIWFyARLKGLSEKHVKAEMEQMAL------DVGLPSSKLKSKTSQLSGGMQRKlsVALA---FV 1048
Cdd:NF040905 352 -----NLID--DIKRNITL-ANLGKVSRRGVIDENEEIKVaeeyrkKMNIKTPSVFQKVGNLSGGNQQK--VVLSkwlFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 1049 GgSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1109
Cdd:NF040905 422 D-PDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPE--LLGmcDRIYVMNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1929-2095 |
2.81e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1929 VDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILsnihevhqnmGYCPQFDaiTELLTGRE--- 2005
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL----------GYFAQHQ--LEFLRADEspl 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2006 -HveffaLLRGVPekevgKVGEWAIRK-LGLVKY-GEKYA---GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2079
Cdd:PRK10636 396 qH-----LARLAP-----QELEQKLRDyLGGFGFqGDKVTeetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180
....*....|....*....|..
gi 21536376 2080 RRFL------WNCALSVVKEGR 2095
Cdd:PRK10636 466 RQALtealidFEGALVVVSHDR 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
926-1109 |
2.96e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLS- 1004
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERy 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1005 EKHVKAEMEQMALDVgLPSSKLKS---KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-Q 1080
Cdd:PLN03130 711 ERAIDVTALQHDLDL-LPGGDLTEigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190
....*....|....*....|....*....|..
gi 21536376 1081 GRTIILST---HHMDEAdvlgDRIAIISHGKL 1109
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMI 817
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
933-1064 |
3.53e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 933 GHNGAGKTTTMSILTGLFPPTSGTaYILGKDI----------RSEMSTIRQNL--GVCPQ-------HNVLFDMLT--VE 991
Cdd:PRK11147 36 GRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLivarlqqdppRNVEGTVYDFVaeGIEEQaeylkryHDISHLVETdpSE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 992 EHIWFYARLKGLSEKH--------VKAEMEQMALDvglPSSKLksktSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PRK11147 115 KNLNELAKLQEQLDHHnlwqlenrINEVLAQLGLD---PDAAL----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHL 187
|
.
gi 21536376 1064 D 1064
Cdd:PRK11147 188 D 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
913-1115 |
3.88e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYilgkdirSEMStirqnLGVCPQHNVLFDMlTVEE 992
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERS-----IAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 993 HIWFY-----ARLkglsekHVKAEMEQMALDVGLPSSKLKS----KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PTZ00243 740 NILFFdeedaARL------ADAVRVSQLEADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1064 DPY-SRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSS 1115
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS 865
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1936-2131 |
4.54e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKN------------SIL---SNI--H-EVHQN--MGYCPQFD 1995
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvSMLfqeNNLfsHlTVAQNigLGLNPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1996 aitelLTGREHveffallrgvpekevGKVGEWAiRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2075
Cdd:PRK10771 102 -----LNAAQR---------------EKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536376 2076 DPKARrflwNCALSVVKE---GRSVVL--TSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2131
Cdd:PRK10771 161 DPALR----QEMLTLVSQvcqERQLTLlmVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
925-1104 |
5.17e-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: 48.63 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 925 EGQITSFLGHNGAGKTTTMSILTGLF---------PPT--------SGTA---YIlgKDIRS-EMSTIRQnlgvcPQHnv 983
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfRGTElqdYF--KKLANgEIKVAHK-----PQY-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 984 lFDML------TVEEhiwfyaRLKGLSEKHVKAE-MEQMALDvglpsSKLKSKTSQLSGG-MQRkLSVALAFVGGSKVVI 1055
Cdd:COG1245 169 -VDLIpkvfkgTVRE------LLEKVDERGKLDElAEKLGLE-----NILDRDISELSGGeLQR-VAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536376 1056 LDEPTAGVDPYSR----RGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAII 1104
Cdd:COG1245 236 FDEPSSYLDIYQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1908-2133 |
5.23e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSI----LSNIHE 1983
Cdd:PRK11831 4 VANLVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 VHQNMGYCPQFDAITELLTGREHVEFfallrgvPEKEVGKVGEWAIRKLGLVKY---GEKYAGNY-----SGGNKRKLST 2055
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKLeavGLRGAAKLmpselSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2056 AMALIGGPPVVFLDEPTTGMDPKARRFL------WNCALSVvkegrSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2129
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLvkliseLNSALGV-----TCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
....
gi 21536376 2130 HLKN 2133
Cdd:PRK11831 230 ALQA 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1911-2121 |
5.31e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGDAFLNKNSIL----S 1979
Cdd:PRK13549 5 LLEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyEGEIIFEGEELQASNIRdterA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1980 NIHEVHQNMGYCPQFDAITELLTGREHVEFfallrGVP--EKEVGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPG-----GIMdyDAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536376 2058 ALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2121
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVL----LDIIRDlkahGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1911-2102 |
5.45e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGDAFLNKNSILSNIHEVHQNM 1988
Cdd:CHL00131 7 ILEIKNLHA--SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1989 GYCPQFDAITElLTGREHVEFFAL-------LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNY-----SGGNKRK---L 2053
Cdd:CHL00131 85 GIFLAFQYPIE-IPGVSNADFLRLaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNvnegfSGGEKKRneiL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536376 2054 StaMALIgGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2102
Cdd:CHL00131 164 Q--MALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
981-1092 |
6.17e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLfDMlTVEEHIWFYARLKGLSEKHvkaemeQMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVALAF-VGGSKVVILD 1057
Cdd:cd03271 126 ADVL-DM-TVEEALEFFENIPKIARKL------QTLCDVGLGYIKLGQPATTLSGGeAQRiKLAKELSKrSTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....*.
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMD 1092
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLD 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1912-2102 |
6.23e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.18 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1912 LEIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEV-HQNMGY 1990
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQ---------FDAITellTGR-----------EHVEFFALLRGVPEKEVGKVGEwairklglvkygekYAGNYSGGNK 2050
Cdd:PRK10790 420 VQQdpvvladtfLANVT---LGRdiseeqvwqalETVQLAELARSLPDGLYTPLGE--------------QGNNLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2051 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSH 2102
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQ-ALAAVREHTTLVVIAH 533
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
899-1106 |
7.69e-05 |
|
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: 45.22 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTSGTayilgkdirsemstirqnL 975
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGR------------------I 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 976 GVCPQHNVLFdmltVEEHIWFYA-RLKglsekhvkaemEQMALdvglPSSKlksktsQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:cd03223 59 GMPEGEDLLF----LPQRPYLPLgTLR-----------EQLIY----PWDD------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536376 1055 ILDEPTAGVDPYSRRGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAIISH 1106
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLL---KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1932-2104 |
8.21e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1932 ICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnknsilSNIHEVHQNMGYCPQ---FDAITELLTGRehve 2008
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2009 FFALLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:PRK09544 89 FLRLRPGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170
....*....|....*..
gi 21536376 2089 SVVKE-GRSVVLTSHSM 2104
Cdd:PRK09544 165 QLRRElDCAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1911-2076 |
1.20e-04 |
|
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: 47.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSilsnihevhqNMGY 1990
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI----------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1991 CPQFDAITELLTGREHVE--------------------------FFALLR--GVPEKEVGKVGEWAI-RKLGLVKY---- 2037
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEegvaeikdaldrfneisakyaepdadFDKLAAeqAELQEIIDAADAWDLdSQLEIAMDalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536376 2038 --GEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:TIGR03719 153 ppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1911-2076 |
1.23e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKML-------TGDTTVTRGDAFLNKNSILSNI 1981
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1982 HEVHqnMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK10535 84 RREH--FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170
....*....|....*
gi 21536376 2062 GPPVVFLDEPTTGMD 2076
Cdd:PRK10535 162 GGQVILADEPTGALD 176
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1911-2102 |
1.27e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYR-------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDaflnknsILSNIHE 1983
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE-------LLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1984 VH-QNMGYCPQ-----FDAITELLTGREHV----EFFALLR---GVPEKEvgKVGEWAIRKLGLVK-YGEKYAGNYSGGN 2049
Cdd:PRK15112 77 LHfGDYSYRSQrirmiFQDPSTSLNPRQRIsqilDFPLRLNtdlEPEQRE--KQIIETLRQVGLLPdHASYYPHMLAPGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 2050 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVV-KEGRS-VVLTSH 2102
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISyIYVTQH 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1905-2076 |
2.01e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.88 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1905 GGGQNDILEIKELTKIY-------RRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKN 1975
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfGRTVGVvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1976 SILS-----------NIHEVHQNmgycPQ---------FDAITELLtgREHveffallRGVPEKEV-GKVGEwAIRKLGL 2034
Cdd:COG4608 81 DITGlsgrelrplrrRMQMVFQD----PYaslnprmtvGDIIAEPL--RIH-------GLASKAERrERVAE-LLELVGL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536376 2035 -VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:COG4608 147 rPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1888-2076 |
2.08e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1888 LNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYRrkrkpavDRICV-----GIPPGECFGLLGVNGAGKSSTFKML 1959
Cdd:PRK11819 298 LLSEEYQKRNETNEIFIPPGPrlgDKVIEAENLSKSFG-------DRLLIddlsfSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1960 TG----DT-TVTRGDAflnknsilsniheVHqnMGYCPQFdaitelltgREHVEffallrgvPEKEVGKV--GEWAIRKL 2032
Cdd:PRK11819 371 TGqeqpDSgTIKIGET-------------VK--LAYVDQS---------RDALD--------PNKTVWEEisGGLDIIKV 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536376 2033 GLVK-----Y-------G---EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK11819 419 GNREipsraYvgrfnfkGgdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1936-2168 |
3.00e-04 |
|
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: 45.48 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNkNSILSNIHE-----VHQ-NMGYCPQfDAitEL---LTGREH 2006
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVLQDSARgiflpPHRrRIGYVFQ-EA--RLfphLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2007 VEFfALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR----F 2082
Cdd:COG4148 98 LLY-GRKRAPRAERRISFDE-VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAeilpY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2083 LwncaLSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRfgdgytivvriagsnPDLKPVQDFFGl 2161
Cdd:COG4148 176 L----ERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR---------------PDLLPLAGGEE- 235
|
....*..
gi 21536376 2162 afPGSVL 2168
Cdd:COG4148 236 --AGSVL 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
899-1116 |
3.14e-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: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTA-YILG---KDIRSEM-STI 971
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiYHVAlceKCGYVERpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 972 RQNLGVCPQHNVLFD--------------------ML----------TVEEHIwfyarLKGLSEKHVKAEME-QMALDVg 1020
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEvdfwnlsdklrrrirkriaiMLqrtfalygddTVLDNV-----LEALEEIGYEGKEAvGRAVDL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1021 LPSSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEA 1094
Cdd:TIGR03269 153 IEMVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|..
gi 21536376 1095 DVLGDRIAIISHGKLCCVGSSL 1116
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPD 254
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1936-2142 |
4.88e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.48 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILS-NIHEVHQNMGYCPQfdaiTELLTGREHVEFFAL-L 2013
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ----EPVLFSGSVRENIAYgL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2014 RGVPEKEVGKVGEWA-----IRKLGLVKY---GEKyaGNY-SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL- 2083
Cdd:TIGR00958 580 TDTPDEEIMAAAKAAnahdfIMEFPNGYDtevGEK--GSQlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLq 657
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2084 -WNCAlsvvkEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIV 2142
Cdd:TIGR00958 658 eSRSR-----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
895-1064 |
5.39e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 895 LKLGVSIQNLVKVYRDGMKVA----VDGLAlnfYEGQITSFLGHNGAGKTTTMSILTG-----LFPPTSGTAY--ILGKD 963
Cdd:TIGR00956 55 LKILTRGFRKLKKFRDTKTFDilkpMDGLI---KPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITYdgITPEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 964 IRSEMstiRQNLGVCPQHNVLFDMLTVEEHIWFYARLK-------GLSEKHVKAEMEQMALDV-GLPSSKlKSKTSQ--- 1032
Cdd:TIGR00956 132 IKKHY---RGDVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATyGLSHTR-NTKVGNdfv 207
|
170 180 190
....*....|....*....|....*....|....
gi 21536376 1033 --LSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:TIGR00956 208 rgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1014-1089 |
5.80e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1014 QMALDVGLPSSKLKSKTSQLSGG-MQRklsVALAFVGGSKVV----ILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILS 1087
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVV 195
|
..
gi 21536376 1088 TH 1089
Cdd:cd03270 196 EH 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1936-2076 |
6.53e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1936 IPPGECFGLLGVNGAGKsSTF-KMLTGDTTVTRGdaflnknSILSNIhevhqNMGYCPQFdaitelLTGREHVEFFALLR 2014
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGK-TTFaKLLAGVLKPDEG-------EVDPEL-----KISYKPQY------IKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2015 GVPEK--------EVgkvgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK13409 423 SITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2017-2106 |
7.70e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.87 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2017 PEKEVGKVGEWAIRKLGL---VKYG-EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDP----KARRFLWNCAL 2088
Cdd:PRK14258 119 PKLEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRL 198
|
90
....*....|....*...
gi 21536376 2089 svvKEGRSVVLTSHSMEE 2106
Cdd:PRK14258 199 ---RSELTMVIVSHNLHQ 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1939-2076 |
1.52e-03 |
|
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: 43.62 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1939 GECFGLLGVNGAGKsSTF-KMLTGDTTVTRGDafLNKNSILSnihevhqnmgYCPQFdaITELLTGRehVEFFalLRGVP 2017
Cdd:COG1245 366 GEVLGIVGPNGIGK-TTFaKILAGVLKPDEGE--VDEDLKIS----------YKPQY--ISPDYDGT--VEEF--LRSAN 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536376 2018 EKEVGkvGEWA----IRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:COG1245 427 TDDFG--SSYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1908-2081 |
1.89e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.01 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1908 QNDILEIKELTkiYRRKRKPAVDRICVGIPPGEcFGLL-GVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVH- 1985
Cdd:PRK10247 4 NSPLLQLQNVG--YLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1986 QNMGYCPQfdaiTELLTG---REHVEFFALLRGVpekevgKVGEWAIRKlGLVKYG------EKYAGNYSGGNKRKLSTA 2056
Cdd:PRK10247 81 QQVSYCAQ----TPTLFGdtvYDNLIFPWQIRNQ------QPDPAIFLD-DLERFAlpdtilTKNIAELSGGEKQRISLI 149
|
170 180
....*....|....*....|....*
gi 21536376 2057 MALIGGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKH 174
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1928-2134 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1928 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG----DTTVTRGDAFLNKNSIL------------SNIHEVHQNMGYC 1991
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdNWHVTADRFRWNGIDLLklsprerrkiigREIAMIFQEPSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1992 pqFDAITELltGREhveffaLLRGVPEKEVGkvGEW----------AIR---KLGlVKYGEKYAGNY----SGGNKRKLS 2054
Cdd:COG4170 102 --LDPSAKI--GDQ------LIEAIPSWTFK--GKWwqrfkwrkkrAIEllhRVG-IKDHKDIMNSYphelTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2055 TAMALIGGPPVVFLDEPTTGMDPKAR----RFLwnCALSVVKeGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQH 2130
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQaqifRLL--ARLNQLQ-GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 21536376 2131 LKNR 2134
Cdd:COG4170 246 ILKS 249
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1014-1099 |
2.17e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1014 QMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHH 1090
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLSTLSGGeLQRvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHN 148
|
90
....*....|..
gi 21536376 1091 ---MDEADVLGD 1099
Cdd:cd03238 149 ldvLSSADWIID 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
899-1064 |
2.52e-03 |
|
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: 43.40 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTttmSILTGLF---PPTSGTAYILGKDI-RSEMSTIRQN 974
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 975 LGVCPQHNVLF--------DMLT--VEEHIWFyarlkGLSEKHVKAEMEqmaldvGLPsSKLKSKTSQ----LSGGMQRK 1040
Cdd:TIGR00957 1362 ITIIPQDPVLFsgslrmnlDPFSqySDEEVWW-----ALELAHLKTFVS------ALP-DKLDHECAEggenLSVGQRQL 1429
|
170 180
....*....|....*....|....
gi 21536376 1041 LSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD 1453
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
981-1092 |
4.09e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 981 HNVLfDMlTVEEHIWFYARLKGLSEKHvkaemeQMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVAL-AFVGGSKVVILD 1057
Cdd:TIGR00630 786 ADVL-DM-TVEEAYEFFEAVPSISRKL------QTLCDVGLGYIRLGQPATTLSGGeAQRiKLAKELsKRSTGRTLYILD 857
|
90 100 110
....*....|....*....|....*....|....*.
gi 21536376 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMD 1092
Cdd:TIGR00630 858 EPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLD 893
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1019-1108 |
4.89e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1019 VGLPSSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEA 1094
Cdd:PRK15093 143 VGIKDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQML 222
|
90
....*....|....
gi 21536376 1095 DVLGDRIAIISHGK 1108
Cdd:PRK15093 223 SQWADKINVLYCGQ 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2046-2102 |
5.92e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 5.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536376 2046 SGGNKRKLSTAMAL----IGGPPVVFLDEPTTGMDPK-ARRFLWNCALSVVKeGRSVVLTSH 2102
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRdGQALAEAILEHLVK-GAQVIVITH 139
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1911-2008 |
6.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1911 ILEIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNsilsnihevhQNMGY 1990
Cdd:PRK11819 6 IYTMNRVSKVVPPK-KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG----------IKVGY 74
|
90
....*....|....*...
gi 21536376 1991 CPQFDAITELLTGREHVE 2008
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVE 92
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1920-2140 |
7.02e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1920 IYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSST----FKMLTGDTTVTRGDAFL---NKNSIL---SNIHEVHQ- 1986
Cdd:PRK15134 291 ILKRTvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIWFDGQPLhnlNRRQLLpvrHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 1987 -NMGYCPQFDA---ITELLTgrehVEFFALLRGVPEKEVGKVgewaIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK15134 371 pNSSLNPRLNVlqiIEEGLR----VHQPTLSAAQREQQVIAV----MEEVGLdPETRHRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536376 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYT 2140
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2032-2103 |
7.10e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 7.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536376 2032 LGLVKYGEKyAGNYSGGNKRKLSTAMALIGGP-PVVF-LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHS 2103
Cdd:cd03238 76 LGYLTLGQK-LSTLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
902-956 |
9.57e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 9.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 21536376 902 QNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGT 956
Cdd:PRK11819 328 ENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
|
| |
