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Conserved domains on  [gi|1370474228|ref|XP_024307092|]
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ATP-binding cassette sub-family A member 7 isoform X13 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rim_protein super family cl31083
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
29-1333 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]


The actual alignment was detected with superfamily member TIGR01257:

Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 1334.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:TIGR01257  932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQH 1011
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  189 VDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK 268
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRG 1171
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  269 --------ADTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELD 340
Cdd:TIGR01257 1172 gcegtcscTSKGFSTRCPARVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELE 1251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  341 TRLAELRLTGYGISDTSLEEIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA 412
Cdd:TIGR01257 1252 ETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPA 1326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  413 ----GSAPETDQGSGPDAVgrvQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPAL 488
Cdd:TIGR01257 1327 ahpeGQPPPEPEDPGVPLN---TGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPAL 1403
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  489 RLSPTMYGAQVSFFSEDAPGDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPE 558
Cdd:TIGR01257 1404 TLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAA 1482
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  559 SPSPACQCSRPGARRLLPDCPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSL 638
Cdd:TIGR01257 1483 HPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISI 1562
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  639 GGRDPGLP-SGQELGRSVEELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRA 716
Cdd:TIGR01257 1563 GGKLPAIPiTGEALVGFLSDLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRA 1641
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  717 HLPPGPARHAHSITTLNHPLNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPT 796
Cdd:TIGR01257 1642 SLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPT 1721
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  797 LYWLGNFLWDMCNYLVPACIVVLIFLAFQQRAYVAPANLPALLLLLLLYGWSITPLMYPASFFFSVPSTAYVVLTCINLF 876
Cdd:TIGR01257 1722 TYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLF 1801
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  877 IGINGSMATFVLELFSDQK-LQEVSRILKQVFLIFPHFCLGRGLIDMVRNQAMADAFERLGDRQFQSPLRWEVVGKNLLA 955
Cdd:TIGR01257 1802 IGINSSAITFVLELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVA 1881
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  956 MVIQGPLFLLFTLLLQHRSQLLPQYSVPRPRvrslPLLgEEDEDVARERERVVQGATQGDVLVLRNLTKVYRGQRMPAVD 1035
Cdd:TIGR01257 1882 MAVEGVVYFLLTLLIQHHFFLSRWIAEPAKE----PIF-DEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVD 1956
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1036 RLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIFELLTGREHLELL 1115
Cdd:TIGR01257 1957 RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1116 ARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAV 1195
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1196 VREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAAGHTLTLRVPAARSQ------PAAAFVAAEFPGA 1269
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDllpdlnPVEQFFQGNFPGS 2196
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228 1270 ELREAHGGRLRFQLPPGgrcALARVFGELAVHGAEHGVEDFSVSQTMLEEVFLYFSKDQGKDED 1333
Cdd:TIGR01257 2197 VQRERHYNMLQFQVSSS---SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYD 2257
 
Name Accession Description Interval E-value
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
29-1333 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: 1334.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:TIGR01257  932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQH 1011
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  189 VDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK 268
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRG 1171
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  269 --------ADTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELD 340
Cdd:TIGR01257 1172 gcegtcscTSKGFSTRCPARVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELE 1251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  341 TRLAELRLTGYGISDTSLEEIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA 412
Cdd:TIGR01257 1252 ETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPA 1326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  413 ----GSAPETDQGSGPDAVgrvQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPAL 488
Cdd:TIGR01257 1327 ahpeGQPPPEPEDPGVPLN---TGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPAL 1403
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  489 RLSPTMYGAQVSFFSEDAPGDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPE 558
Cdd:TIGR01257 1404 TLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAA 1482
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  559 SPSPACQCSRPGARRLLPDCPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSL 638
Cdd:TIGR01257 1483 HPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISI 1562
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  639 GGRDPGLP-SGQELGRSVEELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRA 716
Cdd:TIGR01257 1563 GGKLPAIPiTGEALVGFLSDLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRA 1641
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  717 HLPPGPARHAHSITTLNHPLNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPT 796
Cdd:TIGR01257 1642 SLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPT 1721
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  797 LYWLGNFLWDMCNYLVPACIVVLIFLAFQQRAYVAPANLPALLLLLLLYGWSITPLMYPASFFFSVPSTAYVVLTCINLF 876
Cdd:TIGR01257 1722 TYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLF 1801
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  877 IGINGSMATFVLELFSDQK-LQEVSRILKQVFLIFPHFCLGRGLIDMVRNQAMADAFERLGDRQFQSPLRWEVVGKNLLA 955
Cdd:TIGR01257 1802 IGINSSAITFVLELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVA 1881
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  956 MVIQGPLFLLFTLLLQHRSQLLPQYSVPRPRvrslPLLgEEDEDVARERERVVQGATQGDVLVLRNLTKVYRGQRMPAVD 1035
Cdd:TIGR01257 1882 MAVEGVVYFLLTLLIQHHFFLSRWIAEPAKE----PIF-DEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVD 1956
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1036 RLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIFELLTGREHLELL 1115
Cdd:TIGR01257 1957 RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1116 ARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAV 1195
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1196 VREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAAGHTLTLRVPAARSQ------PAAAFVAAEFPGA 1269
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDllpdlnPVEQFFQGNFPGS 2196
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228 1270 ELREAHGGRLRFQLPPGgrcALARVFGELAVHGAEHGVEDFSVSQTMLEEVFLYFSKDQGKDED 1333
Cdd:TIGR01257 2197 VQRERHYNMLQFQVSSS---SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYD 2257
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1017-1237 3.59e-108

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: 340.25  E-value: 3.59e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:cd03263      1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03263     81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1177 TTGMDPSARRFLWNSLLAvVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLK 1237
Cdd:cd03263    161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
29-264 1.24e-74

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 249.92  E-value: 1.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:COG1131      8 RNLTKKY-GGDKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGYVPQE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:COG1131     87 PSLYPELTVRENLEFFARLYGLSKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDEPTSG 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474228  189 VDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLT 264
Cdd:COG1131    167 LDPESRREIWELLRELAKegGVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLELA 244
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
1016-1236 1.01e-44

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 164.21  E-value: 1.01e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1016 VLVLRNLTKVYrGQRMpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGY 1095
Cdd:PRK13537     7 PIDFRNVEKRY-GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1096 CPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDE 1175
Cdd:PRK13537    85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1176 PTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHL 1236
Cdd:PRK13537   165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
43-187 3.24e-39

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 as in CFTR, or belong in different polypeptide chains.


Pssm-ID: 333758 [Multi-domain]  Cd Length: 150  Bit Score: 142.78  E-value: 3.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   43 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDEHV 121
Cdd:pfam00005    1 LKNVSLTLNPGEIVALVGPNGAGKSTLLKLISGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  122 WFYGRLKGLSAAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 187
Cdd:pfam00005   81 RLGLRLKGLSKAEKDARAEEALEKLGLGdlldRPVGENPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
52-222 2.91e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.44  E-value: 2.91e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228    52 QGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlghdvrssmaairphlgvcpqynvlfdmltvdehvwfygrlkgls 131
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   132 aaVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL-------LKY 204
Cdd:smart00382   36 --IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKS 113
                           170       180
                    ....*....|....*....|.
gi 1370474228   205 REGRTLILSTHH---LDEAEL 222
Cdd:smart00382  114 EKNLTVILTTNDekdLGPALL 134
 
Name Accession Description Interval E-value
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
29-1333 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: 1334.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:TIGR01257  932 KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQH 1011
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  189 VDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK 268
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRG 1171
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  269 --------ADTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELD 340
Cdd:TIGR01257 1172 gcegtcscTSKGFSTRCPARVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELE 1251
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  341 TRLAELRLTGYGISDTSLEEIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA 412
Cdd:TIGR01257 1252 ETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPA 1326
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  413 ----GSAPETDQGSGPDAVgrvQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPAL 488
Cdd:TIGR01257 1327 ahpeGQPPPEPEDPGVPLN---TGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPAL 1403
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  489 RLSPTMYGAQVSFFSEDAPGDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPE 558
Cdd:TIGR01257 1404 TLHPWMYGQQYTFFSMDEPNSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAA 1482
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  559 SPSPACQCSRPGARRLLPDCPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSL 638
Cdd:TIGR01257 1483 HPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISI 1562
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  639 GGRDPGLP-SGQELGRSVEELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRA 716
Cdd:TIGR01257 1563 GGKLPAIPiTGEALVGFLSDLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRA 1641
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  717 HLPPGPARHAHSITTLNHPLNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPT 796
Cdd:TIGR01257 1642 SLPKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPT 1721
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  797 LYWLGNFLWDMCNYLVPACIVVLIFLAFQQRAYVAPANLPALLLLLLLYGWSITPLMYPASFFFSVPSTAYVVLTCINLF 876
Cdd:TIGR01257 1722 TYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLF 1801
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  877 IGINGSMATFVLELFSDQK-LQEVSRILKQVFLIFPHFCLGRGLIDMVRNQAMADAFERLGDRQFQSPLRWEVVGKNLLA 955
Cdd:TIGR01257 1802 IGINSSAITFVLELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVA 1881
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  956 MVIQGPLFLLFTLLLQHRSQLLPQYSVPRPRvrslPLLgEEDEDVARERERVVQGATQGDVLVLRNLTKVYRGQRMPAVD 1035
Cdd:TIGR01257 1882 MAVEGVVYFLLTLLIQHHFFLSRWIAEPAKE----PIF-DEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVD 1956
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1036 RLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIFELLTGREHLELL 1115
Cdd:TIGR01257 1957 RLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1116 ARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAV 1195
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1196 VREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAAGHTLTLRVPAARSQ------PAAAFVAAEFPGA 1269
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDllpdlnPVEQFFQGNFPGS 2196
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228 1270 ELREAHGGRLRFQLPPGgrcALARVFGELAVHGAEHGVEDFSVSQTMLEEVFLYFSKDQGKDED 1333
Cdd:TIGR01257 2197 VQRERHYNMLQFQVSSS---SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYD 2257
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1017-1237 3.59e-108

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: 340.25  E-value: 3.59e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:cd03263      1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03263     81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1177 TTGMDPSARRFLWNSLLAvVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLK 1237
Cdd:cd03263    161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
29-245 1.43e-104

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: 330.62  E-value: 1.43e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:cd03263      4 RNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03263     84 DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474228  189 VDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLR 245
Cdd:cd03263    164 LDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
29-264 1.24e-74

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 249.92  E-value: 1.24e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:COG1131      8 RNLTKKY-GGDKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGYVPQE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:COG1131     87 PSLYPELTVRENLEFFARLYGLSKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDEPTSG 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474228  189 VDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLT 264
Cdd:COG1131    167 LDPESRREIWELLRELAKegGVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLELA 244
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1016-1323 4.09e-71

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 239.90  E-value: 4.09e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1016 VLVLRNLTKVYRGQRmPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGY 1095
Cdd:COG1131      4 VIEVRNLTKKYGGDK-TALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1096 CPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDE 1175
Cdd:COG1131     83 VPQEPSLYPELTVRENLEFFARLYGLSKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1176 PTTGMDPSARRFLWNSLLAVVREG-RSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAAGHTLTLRVPAAR 1254
Cdd:COG1131    163 PTSGLDPESRREIWELLRELAKEGgVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLE 242
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474228 1255 SQPAAAFVAAEFPGAELREAhggrlrfqlppggrcalarvfgELAVHGAEHGVEDFSVSQTMLEEVFLY 1323
Cdd:COG1131    243 LAELLEGLKLVKGEEELAEI----------------------LEALLEEGVKIESIEVKEPSLEDVFLE 289
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
1024-1324 1.96e-66

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 226.89  E-value: 1.96e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1024 KVYRGqrMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIF 1103
Cdd:TIGR01188    1 KVYGD--FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1104 ELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPS 1183
Cdd:TIGR01188   79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1184 ARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRfAAGHTLTLRVPAARS-QPAAAFV 1262
Cdd:TIGR01188  159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRR-LGKDTLESRPRDIQSlKVEVSML 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474228 1263 AAEFP--GAELREAH--GGRLRFQLPPGGRcALARVFGELAVHGAEhgVEDFSVSQTMLEEVFLYF 1324
Cdd:TIGR01188  238 IAELGetGLGLLAVTvdSDRIKILVPDGDE-TVPEIVEAAIRNGIR--IRSISTERPSLDDVFLKL 300
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1017-1237 3.53e-65

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: 219.93  E-value: 3.53e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:cd03265      1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03265     79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVRE-GRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLK 1237
Cdd:cd03265    159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
29-235 2.82e-62

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: 209.56  E-value: 2.82e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:cd03230      4 RNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03230     82 PSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1370474228  189 VDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 235
Cdd:cd03230    126 LDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1017-1227 1.37e-58

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 199.16  E-value: 1.37e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQrmPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:cd03230      1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLEllarlrgvpeaqvaqtagsglarlglswyadrpagtYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03230     79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRF 1227
Cdd:cd03230    123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
41-250 7.29e-57

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: 199.15  E-value: 7.29e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   41 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEH 120
Cdd:TIGR01188    7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  121 VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 200
Cdd:TIGR01188   87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370474228  201 LLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGS 250
Cdd:TIGR01188  167 IRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK 217
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
29-241 3.27e-56

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: 194.13  E-value: 3.27e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:cd03265      4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03265     82 LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370474228  189 VDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:cd03265    162 LDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1017-1228 1.90e-49

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: 174.30  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGeCFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:cd03264      1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03264     78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370474228 1177 TTGMDPSAR-RFLwnSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFR 1228
Cdd:cd03264    158 TAGLDPEERiRFR--NLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
29-239 3.63e-49

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: 173.53  E-value: 3.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGhITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:cd03264      4 ENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGL--VSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPT 186
Cdd:cd03264     81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgdRAKKKIGS--LSGGMRRRVGIAQALVGDPSILIVDEPT 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370474228  187 AGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 239
Cdd:cd03264    159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1017-1231 5.99e-49

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: 173.32  E-value: 5.99e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRMP--AVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMG 1094
Cdd:cd03266      2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1095 YCPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLD 1174
Cdd:cd03266     82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474228 1175 EPTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLG 1231
Cdd:cd03266    162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
29-234 2.98e-48

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: 171.11  E-value: 2.98e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQ 107
Cdd:cd03225      3 KNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLVFQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  108 Y-NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPT 186
Cdd:cd03225     83 NpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370474228  187 AGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 234
Cdd:cd03225    163 AGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1005-1366 1.29e-47

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: 187.53  E-value: 1.29e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1005 ERVVQGATQGdvLVLRNLTKVYRGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAR 1084
Cdd:TIGR01257  919 ERELPGLVPG--VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1085 EPSAAHLSMGYCPQSDAIFELLTGREHLELLARLRGVP--EAQVAQTAGsgLARLGLSWYADRPAGTYSGGNKRKLATAL 1162
Cdd:TIGR01257  997 NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSweEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAI 1074
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1163 ALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAvVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAA 1242
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGT 1153
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1243 GHTLTL--RVPAARSQ-------------------PAAA------------------FVAAEFPGAELREAHGGRLRFQL 1283
Cdd:TIGR01257 1154 GFYLTLvrKMKNIQSQrggcegtcsctskgfstrcPARVdeitpeqvldgdvnelmdLVYHHVPEAKLVECIGQELIFLL 1233
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1284 PPGG--RCALARVFGELAVHGAEHGVEDFSVSQTMLEEVFLYFSKDQGKDE---DTEEQKEAGVgvdpapGLQHP----- 1353
Cdd:TIGR01257 1234 PNKNfkQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSlfaGGAQQKRENA------NLRHPcsgpt 1307
                          410
                   ....*....|...
gi 1370474228 1354 KRVSQFLDDPSTA 1366
Cdd:TIGR01257 1308 EKAGQTPQASHTC 1320
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1017-1226 9.54e-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: 160.85  E-value: 9.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHlSMGYC 1096
Cdd:cd03268      1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGAL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTagsgLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03268     78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGR 1226
Cdd:cd03268    154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
1016-1236 1.01e-44

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 164.21  E-value: 1.01e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1016 VLVLRNLTKVYrGQRMpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGY 1095
Cdd:PRK13537     7 PIDFRNVEKRY-GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1096 CPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDE 1175
Cdd:PRK13537    85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1176 PTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHL 1236
Cdd:PRK13537   165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
29-235 1.64e-44

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 160.08  E-value: 1.64e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRpHLGVCPQY 108
Cdd:cd03268      4 NDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGALIEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03268     81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1370474228  189 VDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 235
Cdd:cd03268    157 LDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1017-1231 8.43e-44

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: 158.21  E-value: 8.43e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRgqRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAhlsMGYC 1096
Cdd:cd03269      1 LEVENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR---IGYL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03269     76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLG 1231
Cdd:cd03269    156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
29-241 1.89e-43

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 226927 [Multi-domain]  Cd Length: 245  Bit Score: 158.35  E-value: 1.89e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:COG4555      5 TDLTKSY-GSKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFVRRKIGVLFGE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:COG4555     84 RGLYARLTARENLKYFARLNGLSRKEIKARIAELSKRLQLLEYLDRRVGEFSTGMKQKVAIARALVHDPSILVLDEPTSG 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370474228  189 VDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:COG4555    164 LDIRTRRKFHDFIKQLKnEGRAVIFSSHIMQEVEALCDRVIVLHKGEVVLEGSI 217
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1016-1239 2.25e-43

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 226927 [Multi-domain]  Cd Length: 245  Bit Score: 158.35  E-value: 2.25e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1016 VLVLRNLTKVYrGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGY 1095
Cdd:COG4555      1 MLEVTDLTKSY-GSKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFVRRKIGV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1096 CPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDE 1175
Cdd:COG4555     80 LFGERGLYARLTARENLKYFARLNGLSRKEIKARIAELSKRLQLLEYLDRRVGEFSTGMKQKVAIARALVHDPSILVLDE 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228 1176 PTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGR 1239
Cdd:COG4555    160 PTSGLDIRTRRKFHDFIKQLKNEGRAVIFSSHIMQEVEALCDRVIVLHKGEVVLEGSIEALDAR 223
PRK13536 PRK13536
nodulation factor exporter subunit NodI; Provisional
985-1236 4.07e-43

nodulation factor exporter subunit NodI; Provisional


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 160.77  E-value: 4.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  985 PRVRSLPLLGEEDEDVARERERVVqGATQGDVLVLRNLTKVYRGQrmPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMV 1064
Cdd:PRK13536    11 PRRLELSPIERKHQGISEAKASIP-GSMSTVAIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1065 TGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYAD 1144
Cdd:PRK13536    88 LGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKAD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1145 RPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVN 1224
Cdd:PRK13536   168 ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
                          250
                   ....*....|..
gi 1370474228 1225 GRFRCLGSPQHL 1236
Cdd:PRK13536   248 GRKIAEGRPHAL 259
nodI TIGR01288
ATP-binding ABC transporter family nodulation protein NodI; This protein is required for ...
1019-1236 6.41e-42

ATP-binding ABC transporter family nodulation protein NodI; This protein is required for normal nodulation by nitrogen-fixing root nodule bacteria such as Mesorhizobium loti. It is a member of the family of ABC transporter ATP binding proteins and works with NodJ to export a nodulation signal molecule. This model does not recognize the highly divergent NodI from Azorhizobium caulinodans. [Cellular processes, Other, Transport and binding proteins, Other]


Pssm-ID: 130355 [Multi-domain]  Cd Length: 303  Bit Score: 156.24  E-value: 6.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1019 LRNLTKVYRGQRMpaVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQ 1098
Cdd:TIGR01288    7 LVGVSKSYGDKVV--VNDLSFTIARGECFGLLGPNGAGKSTIARMLLGMISPDRGKITVLGEPVPSRARLARVAIGVVPQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1099 SDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTT 1178
Cdd:TIGR01288   85 FDNLDPEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADVRVALLSGGMKRRLTLARALINDPQLLILDEPTT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474228 1179 GMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHL 1236
Cdd:TIGR01288  165 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLESGRKIAEGRPHAL 222
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
30-235 6.65e-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: 152.91  E-value: 6.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   30 GLEKRF--PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQ 107
Cdd:cd03266      6 ALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  108 YNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 187
Cdd:cd03266     86 STGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370474228  188 GVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 235
Cdd:cd03266    166 GLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
29-234 3.08e-40

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: 147.81  E-value: 3.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLGVCPQY 108
Cdd:cd03269      4 ENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03269     79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370474228  189 VDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 234
Cdd:cd03269    159 LDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistant to organic solvents; ABC ...
29-241 2.38e-39

ATP-binding cassette transport system involved in resistant 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: 146.49  E-value: 2.38e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGV 104
Cdd:cd03261      4 RGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  105 CPQYNVLFDMLTVDEHVWFYGRLKG-LSAAVVGpEQDRL-LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 182
Cdd:cd03261     82 LFQSGALFDSLTVFENVAFPLREHTrLSEEEIR-EIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228  183 DEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:cd03261    161 DEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
43-187 3.24e-39

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 as in CFTR, or belong in different polypeptide chains.


Pssm-ID: 333758 [Multi-domain]  Cd Length: 150  Bit Score: 142.78  E-value: 3.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   43 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDEHV 121
Cdd:pfam00005    1 LKNVSLTLNPGEIVALVGPNGAGKSTLLKLISGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  122 WFYGRLKGLSAAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 187
Cdd:pfam00005   81 RLGLRLKGLSKAEKDARAEEALEKLGLGdlldRPVGENPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
41-241 2.08e-38

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 224047 [Multi-domain]  Cd Length: 235  Bit Score: 143.55  E-value: 2.08e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   41 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS--SMAAIRPHLGVCPQY--NVLFdMLT 116
Cdd:COG1122     18 AALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTSSekSLLELRQKVGLVFQNpdDQLF-GPT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  117 VDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRG 196
Cdd:COG1122     97 VEDEVAFGLENLGLPREEIEERVAEALELVGLEELLDRPPFNLSGGQKQRVAIAGVLAMGPEILLLDEPTAGLDPKGRRE 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370474228  197 IWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:COG1122    177 LLELLKKLKEegGKTIIIVTHDLELVLEYADRVVVLDDGKILADGDP 223
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
1017-1322 6.15e-38

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226631 [Multi-domain]  Cd Length: 300  Bit Score: 144.43  E-value: 6.15e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYrgQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAahlSMGYC 1096
Cdd:COG4152      3 LEIEGVTKSF--GDKKAVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLSQEIKN---RIGYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:COG4152     78 PEERGLYPKMTVEDQLKYLAELKGMPKAEIQKKLQAWLERLEIVGKKTKKIKELSKGNQQKIQFISAVIHEPELLILDEP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAaghtltlrvpaarsq 1256
Cdd:COG4152    158 FSGLDPVNVELLKDAIFELKEEGATIIFSSHRMEHVEELCDRLLMLKKGQTVLYGTVEDIRRSFG--------------- 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228 1257 PAAAFVAAEFPGAELrEAHGGRLRFQLPPGG--RCALAR------VFGELAVHGAehgVEDFSVSQTMLEEVFL 1322
Cdd:COG4152    223 KKRLVIESDLSLEEL-ANIPGILKITETKDGswRIQIENetvareIFQEVARDGY---IQRFELQEPSLHDIFI 292
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1017-1235 1.58e-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: 141.04  E-value: 1.58e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSA--AHLSMG 1094
Cdd:cd03219      1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1095 YCPQSDAIFELLTGREHLELLARLRGVP----------EAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALAL 1164
Cdd:cd03219     79 RTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1165 VGDPAVVFLDEPTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQH 1235
Cdd:cd03219    159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
22-241 1.61e-37

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 143.41  E-value: 1.61e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   22 LPHPAGP---KGLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAI 98
Cdd:PRK13537     1 GPMSVAPidfRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   99 RPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQ 178
Cdd:PRK13537    79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474228  179 VVILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:PRK13537   159 VLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
29-234 1.99e-37

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: 137.76  E-value: 1.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVCPQ 107
Cdd:cd00267      3 ENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  108 ynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEPTA 187
Cdd:cd00267     81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1370474228  188 GVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 234
Cdd:cd00267    110 GLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
41-241 2.75e-37

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 224045 [Multi-domain]  Cd Length: 258  Bit Score: 141.16  E-value: 2.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   41 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDE 119
Cdd:COG1120     16 PILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASlSPKELAKKLAYVPQSPSAPFGLTVYE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  120 HVWfYGRLKGLSAAVVGPEQDRL-----LQDVGLV--SKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPA 192
Cdd:COG1120     96 LVL-LGRYPHLGLFGRPSKEDEEiveeaLELLGLEhlADRPVDE--LSGGERQRVLIARALAQETPILLLDEPTSHLDIA 172
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370474228  193 SRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:COG1120    173 HQIEVLELLrdLNREKGLTVVMVLHDLNLAARYADHLILLKDGKIVAQGTP 223
GldA_ABC_ATP TIGR03522
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ...
40-235 7.88e-37

gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 132561 [Multi-domain]  Cd Length: 301  Bit Score: 141.45  E-value: 7.88e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   40 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDE 119
Cdd:TIGR03522   15 QNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYLPEHNPLYLDMYVRE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  120 HVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWE 199
Cdd:TIGR03522   95 YLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPNQLVEIRN 174
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1370474228  200 LLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 235
Cdd:TIGR03522  175 VIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKI 210
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
29-234 8.42e-37

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: 136.74  E-value: 8.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQ 107
Cdd:cd03228      4 KNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  108 YNVLFDMlTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEPTA 187
Cdd:cd03228     84 DPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370474228  188 GVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGR 234
Cdd:cd03228    126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
nodI TIGR01288
ATP-binding ABC transporter family nodulation protein NodI; This protein is required for ...
46-241 9.00e-37

ATP-binding ABC transporter family nodulation protein NodI; This protein is required for normal nodulation by nitrogen-fixing root nodule bacteria such as Mesorhizobium loti. It is a member of the family of ABC transporter ATP binding proteins and works with NodJ to export a nodulation signal molecule. This model does not recognize the highly divergent NodI from Azorhizobium caulinodans. [Cellular processes, Other, Transport and binding proteins, Other]


Pssm-ID: 130355 [Multi-domain]  Cd Length: 303  Bit Score: 141.22  E-value: 9.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   46 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYG 125
Cdd:TIGR01288   23 LSFTIARGECFGLLGPNGAGKSTIARMLLGMISPDRGKITVLGEPVPSRARLARVAIGVVPQFDNLDPEFTVRENLLVFG 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  126 RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLK-Y 204
Cdd:TIGR01288  103 RYFGMSTREIEAVIPSLLEFARLESKADVRVALLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlL 182
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370474228  205 REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:TIGR01288  183 ARGKTILLTTHFMEEAERLCDRLCVLESGRKIAEGRP 219
PRK13536 PRK13536
nodulation factor exporter subunit NodI; Provisional
30-241 5.85e-36

nodulation factor exporter subunit NodI; Provisional


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 139.97  E-value: 5.85e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   30 GLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYN 109
Cdd:PRK13536    46 GVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFD 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  110 VLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 189
Cdd:PRK13536   124 NLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370474228  190 DPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:PRK13536   204 DPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
30-234 2.31e-35

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226631 [Multi-domain]  Cd Length: 300  Bit Score: 137.11  E-value: 2.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   30 GLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLGVCPQYN 109
Cdd:COG4152      7 GVTKSF-GDKK-AVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLS---QEIKNRIGYLPEER 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  110 VLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 189
Cdd:COG4152     82 GLYPKMTVEDQLKYLAELKGMPKAEIQKKLQAWLERLEIVGKKTKKIKELSKGNQQKIQFISAVIHEPELLILDEPFSGL 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1370474228  190 DPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGR 234
Cdd:COG4152    162 DPVNVELLKDAIFELKeEGATIIFSSHRMEHVEELCDRLLMLKKGQ 207
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
29-232 2.96e-35

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: 134.14  E-value: 2.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGhdvrSSMAAIRPHLGVCP 106
Cdd:cd03293      4 RNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRGYVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  107 QYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPT 186
Cdd:cd03293     80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1370474228  187 AGVDPASRRGIWELLLK--YREGRTLILSTHHLDEAELLGDRVAVVAG 232
Cdd:cd03293    160 SALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1017-1226 4.51e-35

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: 133.41  E-value: 4.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPsAAHLSMGYC 1096
Cdd:cd03259      1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-PERRNIGMV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:cd03259     78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVRE-GRSVMLTSHSMEECEALCSRLAIMVNGR 1226
Cdd:cd03259    158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1017-1236 4.91e-35

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 133.82  E-value: 4.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYRGQRmpAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREP--SAAHLSMG 1094
Cdd:cd03218      1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhKRARLGIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1095 YCPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLD 1174
Cdd:cd03218     79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474228 1175 EPTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHL 1236
Cdd:cd03218    159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
PQQ_ABC_ATP TIGR03864
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ...
1017-1242 5.55e-35

ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 274822 [Multi-domain]  Cd Length: 236  Bit Score: 133.96  E-value: 5.55e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1017 LVLRNLTKVYrGQRmPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYC 1096
Cdd:TIGR03864    2 LEVAGLSFRY-GAR-RALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEP 1176
Cdd:TIGR03864   80 FQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474228 1177 TTGMDPSARRFLWNSLLAVVRE-GRSVMLTSHSMEECEAlCSRLAIMVNGRFRCLGSPQHLKGRFAA 1242
Cdd:TIGR03864  160 TVGLDPASRAAITAHVRALARDqGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAELRGATGG 225
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
29-241 5.96e-35

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: 133.72  E-value: 5.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCP-- 106
Cdd:cd03219      4 RGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtf 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  107 QYNVLFDMLTVDEHV------------WFYGRLKGLSAAVvgpEQ-DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAF 173
Cdd:cd03219     82 QIPRLFPELTVLENVmvaaqartgsglLLARARREEREAR---ERaEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474228  174 VGGSQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:cd03219    159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
MlaF COG1127
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ...
29-241 2.13e-34

ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224052 [Multi-domain]  Cd Length: 263  Bit Score: 133.10  E-value: 2.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMA----AIRPHLGV 104
Cdd:COG1127     12 RGVTKSFGD--RVILDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEILIDGEDIPQLSEeelyEIRKRMGV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  105 CPQYNVLFDMLTVDEHVWFYGR-LKGLSAAVVgpeqDRL----LQDVGLvsKQSVQTRH---LSGGMQRKLSVAIAFVGG 176
Cdd:COG1127     90 LFQQGALFSSLTVFENVAFPLReHTKLPESLI----RELvlmkLELVGL--RGAAADLYpseLSGGMRKRVALARAIALD 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474228  177 SQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 241
Cdd:COG1127    164 PELLFLDEPTSGLDPISAGVIDELIRELNDalGLTVIMVTHDLDSLLTIADRVAVLADGKVIAEGTP 230
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
29-235 2.51e-34

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: 131.10  E-value: 2.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVCPQY 108
Cdd:cd03259      4 KGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:cd03259     81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370474228  189 VDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 235
Cdd:cd03259    161 LDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRI 209
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
29-235 3.04e-34

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; 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. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. 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: 131.07  E-value: 3.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFPGS--PQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS----MAAIR-PH 101
Cdd:cd03255      4 KNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFRrRH 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  102 LG-VCPQYNVLfDMLTVDEHVWFYGRLKGlsaavVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVG 175
Cdd:cd03255     84 IGfVFQSFNLL-PDLTALENVELPLLLAG-----VPKKERReraeeLLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474228  176 GSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAElLGDRVAVVAGGRL 235
Cdd:cd03255    158 DPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
PQQ_ABC_ATP TIGR03864
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ...
29-264 4.64e-34

ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 274822 [Multi-domain]  Cd Length: 236  Bit Score: 131.26  E-value: 4.64e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   29 KGLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQY 108
Cdd:TIGR03864    5 AGLSFRY--GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  109 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:TIGR03864   83 PTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474228  189 VDPASRRGIWELL--LKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSPLFLRRHLGSGyylTLVKARLPLT 264
Cdd:TIGR03864  163 LDPASRAAITAHVraLARDQGLSVLWATHLVDEIE-ASDRLVVLHRGRVLADGAAAELRGATGGA---DLEAAFLALT 236
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1018-1226 6.76e-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: 129.89  E-value: 6.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1018 VLRNLTKVYRGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSM-GYC 1096
Cdd:cd03225      1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228 1097 PQ-SDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDE 1175
Cdd:cd03225     81 FQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370474228 1176 PTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGR 1226
Cdd:cd03225    161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
40-241 7.27e-34

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224046 [Multi-domain]  Cd Length: 254  Bit Score: 131.20  E-value: 7.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228   40 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRphLGVCPQY-NVLFDM-LTV 117
Cdd:COG1121     17 RPVLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRKRRKRLR--IGYVPQKsSVDRSFpITV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474228  118 DEHV---------WFYGRLKGLSAAVvgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 188
Cdd:COG1121     95 KDVVllgrygkkgWFRRLNKKDKEKV-----DEALERVGMEDLRDRQIGELSGGQKQRVLLARALAQNPDLLLLDEPFTG 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370474228  189 VDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAgGRLCCCGSP 241
Cdd:COG1121    170 VDVAGQKEIYDLLKELRqEGKTVLMVTHDLGLVMAYFDRVICLN-RHLIASGPP 222
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
40-239 9.48e-34

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 129.58  E-value: 9.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|