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Conserved domains on  [gi|768000599|ref|XP_011525935|]
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ATP-binding cassette sub-family A member 7 isoform X11 [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 ...
1-1610 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: 1432.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599     1 MAFWTQLMLLLWKNFMYRRRQPVQLLVELLWPLFLFFILVAVRHSHPPLEHHECHFPNKPLPSAGTVPWLQGLICNVNNT 80
Cdd:TIGR01257    1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599    81 CFPQLTPGEEPGRLSNFNDSLVSRLLADARTVLGGA--SAH-----RTLAGLGKLIATLR------AAR----------- 136
Cdd:TIGR01257   81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDApeSQHlgqvwAELRTLSQFMDTLRthperiAGRgirirdilkde 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   137 -----------------------STAQPQPTKQSPLEPPMLDVA---ELLTSLL-----------RTESLGLALGQAQ-- 177
Cdd:TIGR01257  161 ealtlflmkniglsdsvvyllvnSQVRPEQFAYGVPDLELKDIAcseALLERFIifsqrrgaqtvRDALCSLSQGTLQwi 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   178 --------------EPLHSLLEAAE-------------DLA---QELLALRSLVEL----RALLQR--PRGTSGPLELLS 221
Cdd:TIGR01257  241 edtlyanvdffklfHVLPTLLDSRSqginlrswggilsDMSpriQEFIHRPSVQDLlwvtRPLLQNggPETFTQLMGILS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   222 EALCSV-RGPSSTVGpSLNWYEASDLMELVGQEPESALP----DSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLL 296
Cdd:TIGR01257  321 DLLCGYpEGGGSRVF-SFNWYEDNNYKAFLGIDSTRKDPiysyDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKIL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   297 FAPDTPFTRKLMAQVNRTFEELTLLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQ---MQDEGRRQPRPGGRDhMEAL 373
Cdd:TIGR01257  400 FTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQnptVKDFINRQLGEEGIT-AEAV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   374 RSFLDPGS--------GGYSWQDAHADVGHLVGTLGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFlgped 445
Cdd:TIGR01257  479 LNFLYNGPrekqaddmTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVF----- 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   446 ssdPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKIRDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRA 525
Cdd:TIGR01257  554 ---PDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPV 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   526 GLYLQQMPYPCYVDDVFLRVLSRSLPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLL 605
Cdd:TIGR01257  631 GIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSM 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   606 SAALLVLVLKLGDILPYSHPGVVFLFLAAFAVATVTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGG 685
Cdd:TIGR01257  711 SIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADL 790
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   686 RVAASLLSPVAFGFGCESLALLEEQGEGAQWHNVGTRPT-ADVFSLAQVSGLLLLDAALYGLATWYLEAVCPGQYGIPEP 764
Cdd:TIGR01257  791 KTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLeGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLP 870
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   765 WNFPFRRSYWCG--------PRPPKSPAPCPTPL-DPK-------VLVEEAPPGLSPGVSVRSLEKRFPGSPQPALRGLS 828
Cdd:TIGR01257  871 WYFLLQESYWLGgegcstreERALEKTEPLTEEMeDPEhpegindSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLN 950
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   829 LDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRL 908
Cdd:TIGR01257  951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQL 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   909 KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREG 988
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   989 RTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK--------ADTDMEGSVDT 1060
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGgcegtcscTSKGFSTRCPA 1190
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1061 RQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELDTRLAELRLTGYGISDTSLE 1140
Cdd:TIGR01257 1191 RVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLE 1270
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1141 EIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA----GSAPETDQGSGPDAv 1208
Cdd:TIGR01257 1271 EIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPAahpeGQPPPEPEDPGVPL- 1344
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1209 grVQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPALRLSPTMYGAQVSFFSEDAP 1288
Cdd:TIGR01257 1345 --NTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEP 1422
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1289 GDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPESPSPACQCSRPGARRLLPD 1358
Cdd:TIGR01257 1423 NSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPE 1501
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1359 CPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSLGGRDPGLP-SGQELGRSVE 1437
Cdd:TIGR01257 1502 CPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPiTGEALVGFLS 1581
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1438 ELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHP 1516
Cdd:TIGR01257 1582 DLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQP 1660
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1517 LNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPAC 1596
Cdd:TIGR01257 1661 LNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAG 1740
                         1770
                   ....*....|....
gi 768000599  1597 IVVLIFLAFQQRAY 1610
Cdd:TIGR01257 1741 LVVGIFIGFQKKAY 1754
 
Name Accession Description Interval E-value
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-1610 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: 1432.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599     1 MAFWTQLMLLLWKNFMYRRRQPVQLLVELLWPLFLFFILVAVRHSHPPLEHHECHFPNKPLPSAGTVPWLQGLICNVNNT 80
Cdd:TIGR01257    1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599    81 CFPQLTPGEEPGRLSNFNDSLVSRLLADARTVLGGA--SAH-----RTLAGLGKLIATLR------AAR----------- 136
Cdd:TIGR01257   81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDApeSQHlgqvwAELRTLSQFMDTLRthperiAGRgirirdilkde 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   137 -----------------------STAQPQPTKQSPLEPPMLDVA---ELLTSLL-----------RTESLGLALGQAQ-- 177
Cdd:TIGR01257  161 ealtlflmkniglsdsvvyllvnSQVRPEQFAYGVPDLELKDIAcseALLERFIifsqrrgaqtvRDALCSLSQGTLQwi 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   178 --------------EPLHSLLEAAE-------------DLA---QELLALRSLVEL----RALLQR--PRGTSGPLELLS 221
Cdd:TIGR01257  241 edtlyanvdffklfHVLPTLLDSRSqginlrswggilsDMSpriQEFIHRPSVQDLlwvtRPLLQNggPETFTQLMGILS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   222 EALCSV-RGPSSTVGpSLNWYEASDLMELVGQEPESALP----DSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLL 296
Cdd:TIGR01257  321 DLLCGYpEGGGSRVF-SFNWYEDNNYKAFLGIDSTRKDPiysyDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKIL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   297 FAPDTPFTRKLMAQVNRTFEELTLLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQ---MQDEGRRQPRPGGRDhMEAL 373
Cdd:TIGR01257  400 FTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQnptVKDFINRQLGEEGIT-AEAV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   374 RSFLDPGS--------GGYSWQDAHADVGHLVGTLGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFlgped 445
Cdd:TIGR01257  479 LNFLYNGPrekqaddmTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVF----- 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   446 ssdPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKIRDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRA 525
Cdd:TIGR01257  554 ---PDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPV 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   526 GLYLQQMPYPCYVDDVFLRVLSRSLPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLL 605
Cdd:TIGR01257  631 GIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSM 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   606 SAALLVLVLKLGDILPYSHPGVVFLFLAAFAVATVTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGG 685
Cdd:TIGR01257  711 SIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADL 790
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   686 RVAASLLSPVAFGFGCESLALLEEQGEGAQWHNVGTRPT-ADVFSLAQVSGLLLLDAALYGLATWYLEAVCPGQYGIPEP 764
Cdd:TIGR01257  791 KTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLeGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLP 870
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   765 WNFPFRRSYWCG--------PRPPKSPAPCPTPL-DPK-------VLVEEAPPGLSPGVSVRSLEKRFPGSPQPALRGLS 828
Cdd:TIGR01257  871 WYFLLQESYWLGgegcstreERALEKTEPLTEEMeDPEhpegindSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLN 950
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   829 LDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRL 908
Cdd:TIGR01257  951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQL 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   909 KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREG 988
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   989 RTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK--------ADTDMEGSVDT 1060
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGgcegtcscTSKGFSTRCPA 1190
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1061 RQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELDTRLAELRLTGYGISDTSLE 1140
Cdd:TIGR01257 1191 RVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLE 1270
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1141 EIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA----GSAPETDQGSGPDAv 1208
Cdd:TIGR01257 1271 EIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPAahpeGQPPPEPEDPGVPL- 1344
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1209 grVQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPALRLSPTMYGAQVSFFSEDAP 1288
Cdd:TIGR01257 1345 --NTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEP 1422
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1289 GDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPESPSPACQCSRPGARRLLPD 1358
Cdd:TIGR01257 1423 NSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPE 1501
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1359 CPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSLGGRDPGLP-SGQELGRSVE 1437
Cdd:TIGR01257 1502 CPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPiTGEALVGFLS 1581
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1438 ELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHP 1516
Cdd:TIGR01257 1582 DLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQP 1660
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1517 LNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPAC 1596
Cdd:TIGR01257 1661 LNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAG 1740
                         1770
                   ....*....|....
gi 768000599  1597 IVVLIFLAFQQRAY 1610
Cdd:TIGR01257 1741 LVVGIFIGFQKKAY 1754
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
807-1026 9.72e-105

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: 332.93  E-value: 9.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03263     1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLR 1026
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
807-1045 5.73e-75

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


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 251.07  E-value: 5.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:COG1131     5 IEVRNLTKKY-GGDKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG1131    84 PQEPSLYPELTVRENLEFFARLYGLSKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDEP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPL 1044
Cdd:COG1131   164 TSGLDPESRREIWELLRELAKegGVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLEL 243

                  .
gi 768000599 1045 T 1045
Cdd:COG1131   244 A 244
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
801-1022 2.45e-39

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 149.19  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  801 PGLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIR 880
Cdd:PRK13537    2 PMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 PHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK13537   80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599  961 VILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
824-968 4.64e-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: 142.40  E-value: 4.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDEHV 902
Cdd:pfam00005    1 LKNVSLTLNPGEIVALVGPNGAGKSTLLKLISGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   903 WFYGRLKGLSAAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 968
Cdd:pfam00005   81 RLGLRLKGLSKAEKDARAEEALEKLGLGdlldRPVGENPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
833-1003 1.90e-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: 46.21  E-value: 1.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599    833 QGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlghdvrssmaairphlgvcpqynvlfdmltvdehvwfygrlkgls 912
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599    913 aaVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL-------LKY 985
Cdd:smart00382   36 --IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKS 113
                           170       180
                    ....*....|....*....|.
gi 768000599    986 REGRTLILSTHH---LDEAEL 1003
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 ...
1-1610 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: 1432.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599     1 MAFWTQLMLLLWKNFMYRRRQPVQLLVELLWPLFLFFILVAVRHSHPPLEHHECHFPNKPLPSAGTVPWLQGLICNVNNT 80
Cdd:TIGR01257    1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599    81 CFPQLTPGEEPGRLSNFNDSLVSRLLADARTVLGGA--SAH-----RTLAGLGKLIATLR------AAR----------- 136
Cdd:TIGR01257   81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDApeSQHlgqvwAELRTLSQFMDTLRthperiAGRgirirdilkde 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   137 -----------------------STAQPQPTKQSPLEPPMLDVA---ELLTSLL-----------RTESLGLALGQAQ-- 177
Cdd:TIGR01257  161 ealtlflmkniglsdsvvyllvnSQVRPEQFAYGVPDLELKDIAcseALLERFIifsqrrgaqtvRDALCSLSQGTLQwi 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   178 --------------EPLHSLLEAAE-------------DLA---QELLALRSLVEL----RALLQR--PRGTSGPLELLS 221
Cdd:TIGR01257  241 edtlyanvdffklfHVLPTLLDSRSqginlrswggilsDMSpriQEFIHRPSVQDLlwvtRPLLQNggPETFTQLMGILS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   222 EALCSV-RGPSSTVGpSLNWYEASDLMELVGQEPESALP----DSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLL 296
Cdd:TIGR01257  321 DLLCGYpEGGGSRVF-SFNWYEDNNYKAFLGIDSTRKDPiysyDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKIL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   297 FAPDTPFTRKLMAQVNRTFEELTLLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQ---MQDEGRRQPRPGGRDhMEAL 373
Cdd:TIGR01257  400 FTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQnptVKDFINRQLGEEGIT-AEAV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   374 RSFLDPGS--------GGYSWQDAHADVGHLVGTLGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFlgped 445
Cdd:TIGR01257  479 LNFLYNGPrekqaddmTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVF----- 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   446 ssdPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKIRDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRA 525
Cdd:TIGR01257  554 ---PDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPV 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   526 GLYLQQMPYPCYVDDVFLRVLSRSLPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLL 605
Cdd:TIGR01257  631 GIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSM 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   606 SAALLVLVLKLGDILPYSHPGVVFLFLAAFAVATVTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGG 685
Cdd:TIGR01257  711 SIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADL 790
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   686 RVAASLLSPVAFGFGCESLALLEEQGEGAQWHNVGTRPT-ADVFSLAQVSGLLLLDAALYGLATWYLEAVCPGQYGIPEP 764
Cdd:TIGR01257  791 KTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLeGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLP 870
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   765 WNFPFRRSYWCG--------PRPPKSPAPCPTPL-DPK-------VLVEEAPPGLSPGVSVRSLEKRFPGSPQPALRGLS 828
Cdd:TIGR01257  871 WYFLLQESYWLGgegcstreERALEKTEPLTEEMeDPEhpegindSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLN 950
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   829 LDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRL 908
Cdd:TIGR01257  951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQL 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   909 KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREG 988
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   989 RTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK--------ADTDMEGSVDT 1060
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGgcegtcscTSKGFSTRCPA 1190
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1061 RQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELDTRLAELRLTGYGISDTSLE 1140
Cdd:TIGR01257 1191 RVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLE 1270
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1141 EIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA----GSAPETDQGSGPDAv 1208
Cdd:TIGR01257 1271 EIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPAahpeGQPPPEPEDPGVPL- 1344
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1209 grVQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPALRLSPTMYGAQVSFFSEDAP 1288
Cdd:TIGR01257 1345 --NTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEP 1422
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1289 GDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPESPSPACQCSRPGARRLLPD 1358
Cdd:TIGR01257 1423 NSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPE 1501
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1359 CPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSLGGRDPGLP-SGQELGRSVE 1437
Cdd:TIGR01257 1502 CPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPiTGEALVGFLS 1581
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1438 ELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHP 1516
Cdd:TIGR01257 1582 DLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQP 1660
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1517 LNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPAC 1596
Cdd:TIGR01257 1661 LNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAG 1740
                         1770
                   ....*....|....
gi 768000599  1597 IVVLIFLAFQQRAY 1610
Cdd:TIGR01257 1741 LVVGIFIGFQKKAY 1754
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
807-1026 9.72e-105

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: 332.93  E-value: 9.72e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03263     1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLR 1026
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
807-1045 5.73e-75

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


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 251.07  E-value: 5.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:COG1131     5 IEVRNLTKKY-GGDKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG1131    84 PQEPSLYPELTVRENLEFFARLYGLSKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDEP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPL 1044
Cdd:COG1131   164 TSGLDPESRREIWELLRELAKegGVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLEL 243

                  .
gi 768000599 1045 T 1045
Cdd:COG1131   244 A 244
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
807-1016 3.44e-63

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: 212.64  E-value: 3.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03230     1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03230    79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768000599  967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03230   123 TSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
822-1031 3.46e-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: 200.31  E-value: 3.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEH 901
Cdd:TIGR01188    7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   902 VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 981
Cdd:TIGR01188   87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768000599   982 LLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGS 1031
Cdd:TIGR01188  167 IRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK 217
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
807-1022 3.82e-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: 3.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03265     1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03265    79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599  967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03265   159 TIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
807-1020 7.35e-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: 173.15  E-value: 7.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGhITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03264     1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGL--VSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03264    78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgdRAKKKIGS--LSGGMRRRVGIAQALVGDPSILIVD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599  965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 1020
Cdd:cd03264   156 EPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
808-1015 1.95e-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: 171.88  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  808 SVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:cd03225     1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQY-NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03225    81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768000599  966 PTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03225   161 PTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
807-1016 4.24e-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: 162.00  E-value: 4.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRpHLGVC 886
Cdd:cd03268     1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03268    78 IEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768000599  967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03268   154 TNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
807-1022 5.94e-44

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: 160.27  E-value: 5.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFpGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:COG4555     2 LEVTDLTKSY-GSKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFVRRKIGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG4555    81 FGERGLYARLTARENLKYFARLNGLSRKEIKARIAELSKRLQLLEYLDRRVGEFSTGMKQKVAIARALVHDPSILVLDEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599  967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG4555   161 TSGLDIRTRRKFHDFIKQLKnEGRAVIFSSHIMQEVEALCDRVIVLHKGEVVLEGSI 217
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
807-1016 1.99e-43

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 157.53  E-value: 1.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRF--PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLG 884
Cdd:cd03266     2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768000599  965 EPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03266   162 EPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
812-1156 1.35e-40

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: 165.19  E-value: 1.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   812 LEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNV 891
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDA 2022
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   892 LFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   972 PASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLvKARLPlttneka 1050
Cdd:TIGR01257 2103 PQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM-KIKSP------- 2174
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  1051 DTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGArlveelphelvlvlpytgahdgSFATLFRELDTRLAELRLT 1130
Cdd:TIGR01257 2175 KDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSS----------------------SLARIFQLLISHKDSLLIE 2232
                          330       340
                   ....*....|....*....|....*.
gi 768000599  1131 GYGISDTSLEEIFLKVVEECAADTDM 1156
Cdd:TIGR01257 2233 EYSVTQTTLDQVFVNFAKQQTETYDL 2258
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
807-1015 1.55e-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: 148.97  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLGVC 886
Cdd:cd03269     1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03269    76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03269   156 FSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistant to organic solvents; ABC ...
807-1022 3.77e-40

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: 148.80  E-value: 3.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPH 882
Cdd:cd03261     1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  883 LGVCPQYNVLFDMLTVDEHVWFYGRLKG-LSAAVVGpEQDRL-LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:cd03261    79 MGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIR-EIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599  961 VILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03261   158 LLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
801-1022 2.45e-39

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 149.19  E-value: 2.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  801 PGLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIR 880
Cdd:PRK13537    2 PMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 PHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK13537   80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599  961 VILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
824-968 4.64e-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: 142.40  E-value: 4.64e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDEHV 902
Cdd:pfam00005    1 LKNVSLTLNPGEIVALVGPNGAGKSTLLKLISGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   903 WFYGRLKGLSAAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 968
Cdd:pfam00005   81 RLGLRLKGLSKAEKDARAEEALEKLGLGdlldRPVGENPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
804-1022 9.29e-39

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: 144.71  E-value: 9.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  804 SPGVSVRSLEKRFPGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS--SMAAIRP 881
Cdd:COG1122     1 LRMIEAENLSFRYPGRK-AALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTSSekSLLELRQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  882 HLGVCPQY--NVLFdMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQ 959
Cdd:COG1122    80 KVGLVFQNpdDQLF-GPTVEDEVAFGLENLGLPREEIEERVAEALELVGLEELLDRPPFNLSGGQKQRVAIAGVLAMGPE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599  960 VVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1122   159 ILLLDEPTAGLDPKGRRELLELLKKLKEegGKTIIIVTHDLELVLEYADRVVVLDDGKILADGDP 223
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
805-1022 8.85e-38

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: 142.70  E-value: 8.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  805 PGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHL 883
Cdd:COG1120     1 MMLEVENLSFGYGG--KPILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASlSPKELAKKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  884 GVCPQYNVLFDMLTVDEHVWfYGRLKGLSAAVVGPEQDRL-----LQDVGLV--SKQSVQTrhLSGGMQRKLSVAIAFVG 956
Cdd:COG1120    79 AYVPQSPSAPFGLTVYELVL-LGRYPHLGLFGRPSKEDEEiveeaLELLGLEhlADRPVDE--LSGGERQRVLIARALAQ 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599  957 GSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1120   156 ETPILLLDEPTSHLDIAHQIEVLELLrdLNREKGLTVVMVLHDLNLAARYADHLILLKDGKIVAQGTP 223
GldA_ABC_ATP TIGR03522
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ...
807-1016 1.15e-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: 144.15  E-value: 1.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:TIGR03522    3 IRVSSLTKLY--GTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:TIGR03522   81 PEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 768000599   967 TAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:TIGR03522  161 TTGLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKI 210
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
808-1015 1.32e-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: 138.53  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVC 886
Cdd:cd00267     1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd00267    79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd00267   108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
807-1015 4.55e-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: 137.51  E-value: 4.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03228     1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  886 CPQYNVLFDMlTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03228    81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 768000599  966 PTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGR 1015
Cdd:cd03228   123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
nodI TIGR01288
ATP-binding ABC transporter family nodulation protein NodI; This protein is required for ...
827-1022 1.12e-36

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: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYG 906
Cdd:TIGR01288   23 LSFTIARGECFGLLGPNGAGKSTIARMLLGMISPDRGKITVLGEPVPSRARLARVAIGVVPQFDNLDPEFTVRENLLVFG 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   907 RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLK-Y 985
Cdd:TIGR01288  103 RYFGMSTREIEAVIPSLLEFARLESKADVRVALLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlL 182
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 768000599   986 REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:TIGR01288  183 ARGKTILLTTHFMEEAERLCDRLCVLESGRKIAEGRP 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
805-1015 2.96e-36

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


Pssm-ID: 226631 [Multi-domain]  Cd Length: 300  Bit Score: 139.80  E-value: 2.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  805 PGVSVRSLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLG 884
Cdd:COG4152     1 MALEIEGVTKSF-GDKK-AVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLS---QEIKNRIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:COG4152    76 YLPEERGLYPKMTVEDQLKYLAELKGMPKAEIQKKLQAWLERLEIVGKKTKKIKELSKGNQQKIQFISAVIHEPELLILD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768000599  965 EPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG4152   156 EPFSGLDPVNVELLKDAIFELKeEGATIIFSSHRMEHVEELCDRLLMLKKGQ 207
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
807-1013 4.70e-36

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: 136.45  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGhdvrSSMAAIRPHLG 884
Cdd:cd03293     1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03293    77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768000599  965 EPTAGVDPASRRGIWELLLK--YREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:cd03293   157 EPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
808-1022 5.35e-36

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: 136.80  E-value: 5.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  808 SVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCP 887
Cdd:cd03219     2 EVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  888 --QYNVLFDMLTVDEHV------------WFYGRLKGLSAAVvgpEQ-DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAI 952
Cdd:cd03219    80 tfQIPRLFPELTVLENVmvaaqartgsglLLARARREEREAR---ERaEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599  953 AFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03219   157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
PRK13536 PRK13536
nodulation factor exporter subunit NodI; Provisional
796-1022 7.36e-36

nodulation factor exporter subunit NodI; Provisional


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 139.97  E-value: 7.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  796 VEEAPPGLSPGVSVR--SLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR 873
Cdd:PRK13536   29 AKASIPGSMSTVAIDlaGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  874 SSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:PRK13536  107 ARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  954 FVGGSQVVILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13536  187 LINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
MlaF COG1127
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ...
804-1022 1.27e-35

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: 136.95  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  804 SPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMA----AI 879
Cdd:COG1127     6 EPLIEVRGVTKSFGD--RVILDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEILIDGEDIPQLSEeelyEI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  880 RPHLGVCPQYNVLFDMLTVDEHVWFYGR-LKGLSAAVVgpeqDRL----LQDVGLvsKQSVQTRH---LSGGMQRKLSVA 951
Cdd:COG1127    84 RKRMGVLFQQGALFSSLTVFENVAFPLReHTKLPESLI----RELvlmkLELVGL--RGAAADLYpseLSGGMRKRVALA 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599  952 IAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1127   158 RAIALDPELLFLDEPTSGLDPISAGVIDELIRELNDalGLTVIMVTHDLDSLLTIADRVAVLADGKVIAEGTP 230
PQQ_ABC_ATP TIGR03864
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ...
806-1045 1.18e-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: 133.19  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   806 GVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV 885
Cdd:TIGR03864    1 ALEVAGLSFRY--GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   886 CPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:TIGR03864   79 VFQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   966 PTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSPLFLRRHLGSGyylTLVKARLP 1043
Cdd:TIGR03864  159 PTVGLDPASRAAITAHVraLARDQGLSVLWATHLVDEIE-ASDRLVVLHRGRVLADGAAAELRGATGGA---DLEAAFLA 234

                   ..
gi 768000599  1044 LT 1045
Cdd:TIGR03864  235 LT 236
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
807-1016 1.35e-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: 132.23  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGS--PQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS----MAAIR 880
Cdd:cd03255     1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 -PHLG-VCPQYNVLfDMLTVDEHVWFYGRLKGlsaavVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:cd03255    81 rRHIGfVFQSFNLL-PDLTALENVELPLLLAG-----VPKKERReraeeLLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599  954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:cd03255   155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
805-1022 3.67e-34

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


Pssm-ID: 224046 [Multi-domain]  Cd Length: 254  Bit Score: 132.35  E-value: 3.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  805 PGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRphLG 884
Cdd:COG1121     3 PMIEVENLTVSYGN--RPVLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRKRRKRLR--IG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQY-NVLFDM-LTVDEHV---------WFYGRLKGLSAAVvgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:COG1121    79 YVPQKsSVDRSFpITVKDVVllgrygkkgWFRRLNKKDKEKV-----DEALERVGMEDLRDRQIGELSGGQKQRVLLARA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAgGRLCCCGSP 1022
Cdd:COG1121   154 LAQNPDLLLLDEPFTGVDVAGQKEIYDLLKELRqEGKTVLMVTHDLGLVMAYFDRVICLN-RHLIASGPP 222
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
807-1014 4.47e-34

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224041 [Multi-domain]  Cd Length: 248  Bit Score: 131.91  E-value: 4.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSsmaaIRPHLGVC 886
Cdd:COG1116     4 LEIEGVSKSFGG--VEVLEDINLSVEKGEFVAILGPSGCGKSTLLRLIAGLEKPTSGEVLLDGRPVTG----PGPDIGYV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG1116    78 FQEDALLPWLTVLDNVALGLELRGKSKAEARERAKELLELVGLAGFEDKYPHQLSGGMRQRVAIARALATRPKLLLLDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 768000599  967 TAGVDPASRRGIWELLLK--YREGRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:COG1116   158 FGALDALTREELQDELLRlwEETRKTVLLVTHDVDEAVYLADRVVVLSNR 207
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
807-1016 7.11e-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: 129.95  E-value: 7.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVC 886
Cdd:cd03259     1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03259    78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768000599  967 TAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03259   158 LSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRI 209
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
821-1020 8.87e-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: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSmaaiRPHLGVCPQ-YNVLFDM-LTV 898
Cdd:cd03235    12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQrRSIDRDFpISV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  899 DE--------HVWFYGRLKGLSAAVVgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:cd03235    88 RDvvlmglygHKGLFRRLSKADKAKV----DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768000599  971 DPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAgGRLCCCG 1020
Cdd:cd03235   164 DPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
807-1028 7.80e-33

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 128.19  E-value: 7.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03295     1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  886 CPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQ--TRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:cd03295    80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLM 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599  964 DEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRH 1028
Cdd:cd03295   160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
817-1022 8.38e-33

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 129.11  E-value: 8.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   817 PGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS----MAAIRPHLGVCPQY- 889
Cdd:TIGR04521   12 PGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkkLKDLRKKVGLVFQFp 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   890 -NVLFDmLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvsKQSVQTR---HLSGGMQRKlsVAIAFVGGSQ--VVIL 963
Cdd:TIGR04521   92 eHQLFE-ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGL--DEEYLERspfELSGGQMRR--VAIAGVLAMEpeVLIL 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599   964 DEPTAGVDPASRRGIWELLLKYR--EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:TIGR04521  167 DEPTAGLDPKGRKEILDLFKRLHkeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
812-1028 2.98e-32

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224050 [Multi-domain]  Cd Length: 309  Bit Score: 128.57  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  812 LEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAA-IRPHLGVCPQYN 890
Cdd:COG1125     7 VSKRY--GNKKAVDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILIDGEDISDLDPVeLRRKIGYVIQQI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  891 VLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQ--TRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 968
Cdd:COG1125    85 GLFPHLTVAENIATVPKLLGWDKERIKKRADELLDLVGLDPSEYADryPHELSGGQQQRVGVARALAADPPILLMDEPFG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599  969 GVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRH 1028
Cdd:COG1125   165 ALDPITRKQLQEEIKELQKelGKTIVFVTHDIDEALKLADRIAVMDAGEIVQYDTPDEILAN 226
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
807-1022 3.01e-32

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 127.16  E-value: 3.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS--SMAAIRPHLG 884
Cdd:TIGR04520    1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeeNLWEIRKKVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   885 ----------VCPqynvlfdmlTVDEHVWFygrlkGLSAAVVGPEQ-----DRLLQDVGLVSKQSVQTRHLSGG-MQRkl 948
Cdd:TIGR04520   81 mvfqnpdnqfVGA---------TVEDDVAF-----GLENLGVPREEmrkrvDEALKLVGMEDFRDREPHLLSGGqKQR-- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   949 sVAIAfvgG-----SQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGS 1021
Cdd:TIGR04520  145 -VAIA---GvlamrPDIIILDEATSMLDPKGRKEVLETIrkLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219

                   .
gi 768000599  1022 P 1022
Cdd:TIGR04520  220 P 220
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
807-1016 9.82e-32

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 124.54  E-value: 9.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:cd03257     2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 PHLGVCPQ--YNVLFDMLTVDEHV----WFYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTR---HLSGGMQRKLSVA 951
Cdd:cd03257    82 KEIQMVFQdpMSSLNPRMTIGEQIaeplRIHGKLSKKEAR----KEAVLLLLVGVGLPEEVLNRyphELSGGQRQRVAIA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599  952 IAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03257   158 RALALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
809-1015 1.72e-31

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 121.91  E-value: 1.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  809 VRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPH---LGV 885
Cdd:cd03229     3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  886 CPQYNVLFDMLTVdehvwfygrlkglsaavvgpeqdrlLQDVGLVskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03229    81 VFQDFALFPHLTV-------------------------LENIALG---------LSGGQQQRVALARALAMDPDVLLLDE 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768000599  966 PTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03229   127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
807-1016 3.42e-31

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 120.61  E-value: 3.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRphLG 884
Cdd:cd03216     1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfASPRDARR--AG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 vcpqynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdVGLVSkQsvqtrhLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03216    77 ------------------------------------------IAMVY-Q------LSVGERQMVEIARALARNARLLILD 107
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768000599  965 EPTAGVDPASRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03216   108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
807-1016 4.05e-31

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 129.55  E-value: 4.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPHLG 884
Cdd:COG1129     9 LELRGISKSFGGVK--ALDGVSLTVRPGEVHALLGENGAGKSTLMKILSGVYPPDSGEILIDGKPVafSSPRDALAAGIA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQYNVLFDMLTVDEHVWFyGRLKGLSAAVVGPEQ-----DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQ 959
Cdd:COG1129    87 TVHQELSLVPNLSVAENIFL-GREPTRRFGLIDRKAmrrraRELLARLGLDIDPDTLVGDLSIAQRQMVEIARALSFDAR 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599  960 VVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG1129   166 VLILDEPTAALTVKETERLFDLIRRLKaQGVAIIYISHRLDEVFEIADRITVLRDGRV 223
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
807-1016 6.92e-31

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224059 [Multi-domain]  Cd Length: 226  Bit Score: 121.85  E-value: 6.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS----SMAAIR 880
Cdd:COG1136     2 IELKNVSKIYGlgGEKVEALKDVNLEIEAGEFVAIVGPSGSGKSTLLNLLGGLDKPTSGEVLINGKDLTKlsekELAKLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 P-HLG-VCPQYNvLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQT-RHLSGGMQRKLSVAIAFVGG 957
Cdd:COG1136    82 RkKIGfVFQNFN-LLPDLTVLENVELPLLIAGKSAGRRKRAAEELLEVLGLEDRLLKKKpSELSGGQQQRVAIARALINN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599  958 SQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:COG1136   161 PKIILADEPTGNLDSKTAKEVLELLRELNKerGKTIIMVTHDPELAK-YADRVIELKDGKI 220
MalK COG3839
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
807-1023 1.31e-30

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 226359 [Multi-domain]  Cd Length: 338  Bit Score: 124.29  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVC 886
Cdd:COG3839     4 LELKNVRKSFGS--FEVLKDVNLDIEDGEFVVLLGPSGCGKSTLLRMIAGLEEPTSGEILIDGRDV-TDLPPEKRGIAMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG3839    81 FQNYALYPHMTVYENIAFGLKLRGVPKAEIDKRVKEVAKLLGLEHLLNRKPLQLSGGQRQRVALARALVRKPKVFLLDEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599  967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPL 1023
Cdd:COG3839   161 LSNLDAKLRVLMRSEIkkLHERLGTTTIYVTHDQVEAMTLADRIVVMNDGRIQQVGTPL 219
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
822-1015 1.51e-30

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 120.62  E-value: 1.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV--CPQYNVLFDMLTVD 899
Cdd:cd03224    14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIgyVPEGRRIFPELTVE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  900 EHVwfygrlkgLSAAVVGPEQD--RLLQDV-----GLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:cd03224    94 ENL--------LLGAYARRRAKrkARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 768000599  973 ASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03224   166 KIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
808-1022 7.40e-30

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223488 [Multi-domain]  Cd Length: 250  Bit Score: 119.60  E-value: 7.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  808 SVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCP 887
Cdd:COG0411     6 EVRGLSKRFGGLT--AVNDVSLEVRPGEIVGLIGPNGAGKTTLFNLITGFYKPSSGTVIFRGRDITGLPPHRIARLGIAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  888 QYNV--LFDMLTVDEHV--------------WFYGRLKGLSAAVVGPEQdrLLQDVGLVSKQSVQTRHLSGGMQRKLSVA 951
Cdd:COG0411    84 TFQItrLFPGLTVLENVavgaharlglsgllGRPRARKEEREARERARE--LLEFVGLGELADRPAGNLSYGQQRRLEIA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599  952 IAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG0411   162 RALATQPKLLLLDEPAAGLNPEETEELAELIRELRDrgGVTILLIEHDMKLVMGLADRIVVLNYGEVIAEGTP 234
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
816-1001 1.26e-29

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 117.14  E-value: 1.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   816 FPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV---RSSMAAIRPHLGVCPQY--N 890
Cdd:TIGR01166    1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   891 VLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:TIGR01166   80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
                          170       180       190
                   ....*....|....*....|....*....|..
gi 768000599   971 DPASRRGIWELLLKYR-EGRTLILSTHHLDEA 1001
Cdd:TIGR01166  159 DPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
809-1015 1.49e-29

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 118.44  E-value: 1.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  809 VRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLG 884
Cdd:cd03256     3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 -VCPQYNvLFDMLTVDEHVWFyGRLKGLSA--AVVG--PEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAF 954
Cdd:cd03256    82 mIFQQFN-LIERLSVLENVLS-GRLGRRSTwrSLFGlfPKEEKqralaALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599  955 VGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
808-1020 2.00e-29

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 116.00  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:cd03214     1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  887 PQynvlfdmltvdehvwfygrlkglsaavvgpeqdrLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03214    79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599  967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 1020
Cdd:cd03214   125 TSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
807-1022 1.07e-28

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224051 [Multi-domain]  Cd Length: 240  Bit Score: 116.07  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPHLG 884
Cdd:COG1126     3 IEIKNLSKSF--GDKEVLKGISLSVEKGEVVVIIGPSGSGKSTLLRCLNGLEEPDSGSITVDGEDVgdKKDILKLRRKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  885 VCPQ-YNvLFDMLTVDEHVwFYG--RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGM-QRklsVAIA--FVGGS 958
Cdd:COG1126    81 MVFQqFN-LFPHLTVLENV-TLApvKVKKLSKAEAREKALELLEKVGLADKADAYPAQLSGGQqQR---VAIAraLAMDP 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599  959 QVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1126   156 KVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMIIVTHEMGFAREVADRVIFMDQGKIIEEGPP 220
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
785-1042 1.30e-28

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227321 [Multi-domain]  Cd Length: 559  Bit Score: 122.76  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  785 PCPTPLDPKVLVEEAPPGLspgVSVRSLEKRFPGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGS 864
Cdd:COG4988   302 VATPGSGEKAEVANEPPIE---ISLENLSFRYPDGK-PALSDLNLTIKAGQLTALVGASGAGKSTLLNLLLGFLAPTQGE 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  865 AFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDEHVWFYGR------------LKGLSAAVVGPEQ-DRLLQDVGlv 930
Cdd:COG4988   378 IRVNGIDLRDlSPEAWRKQISWVSQNPYLFAG-TIRENILLARPdasdeeiiaaldQAGLLEFVPKPDGlDTVIGEGG-- 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  931 skqsvqtRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLdEAELLGDRVAV 1010
Cdd:COG4988   455 -------AGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQALQELAKQKTVLVITHRL-EDAADADRIVV 526
                         250       260       270
                  ....*....|....*....|....*....|..
gi 768000599 1011 VAGGRLCCCGSPLFLRRHlgSGYYLTLVKARL 1042
Cdd:COG4988   527 LDNGRLVEQGTHEELSEK--QGLYANLLKQQE 556
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
807-1016 1.37e-28

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 115.37  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPGSPQ--PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:cd03258     2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  881 PHLG-VCPQYNvLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQ 959
Cdd:cd03258    82 RRIGmIFQHFN-LLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599  960 VVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
822-1015 1.50e-28

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223487 [Multi-domain]  Cd Length: 237  Bit Score: 115.64  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV--CPQYNVLFDMLTVD 899
Cdd:COG0410    17 QALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFDGEDITGLPPHERARLGIayVPEGRRIFPRLTVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  900 EHVwfygrLKGLSAAVVGPEQDRLLQDV-----GLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPAS 974
Cdd:COG0410    97 ENL-----LLGAYARRDKEAQERDLEEVyelfpRLKERRNQRAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 768000599  975 RRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG0410   172 VEEIFEAIkeLRKEGGMTILLVEQNARFALEIADRGYVLENGR 214
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
796-1022 2.13e-28

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 116.20  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  796 VEEAPPGLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--- 872
Cdd:cd03294    14 PQKAFKLLAKGKSKEEILKKT--GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaam 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  873 -RSSMAAIRPH-LGVCPQYNVLFDMLTVDEHVWFygrlkGLSAAVVgPEQDRL------LQDVGLVSKQSVQTRHLSGGM 944
Cdd:cd03294    92 sRKELRELRRKkISMVFQSFALLPHRTVLENVAF-----GLEVQGV-PRAEREeraaeaLELVGLEGWEHKYPDELSGGM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  945 QRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03294   166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
808-1022 4.57e-28

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 114.29  E-value: 4.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV-- 885
Cdd:TIGR04406    3 VAENLIKSYKK--RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIgy 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   886 CPQYNVLFDMLTVDEHVW-FYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:TIGR04406   81 LPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599   965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHlDEAELLG--DRVAVVAGGRLCCCGSP 1022
Cdd:TIGR04406  161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH-NVRETLDicDRAYIISDGKVLAEGTP 219
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
816-1032 4.62e-28

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226905 [Multi-domain]  Cd Length: 259  Bit Score: 114.85  E-value: 4.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  816 FPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAairpHLGVCPQYNVLFDM 895
Cdd:COG4525    13 YEGKPRSALEDVSLTIASGELVVVLGPSGCGKTTLLNLIAGFVTPSRGSIQLNGRRIEGPGA----ERGVVFQNEALLPW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  896 LTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR 975
Cdd:COG4525    89 LNVIDNVAFGLQLRGIEKAQRREIAHQMLALVGLEGAEHKYIWQLSGGMRQRVGIARALAVEPQLLLLDEPFGALDALTR 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599  976 RGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAG--GRLCCCGSPLFLRRHLGSG 1032
Cdd:COG4525   169 EQMQELLLDLwqETGKQVLLITHDIEEALFLATRLVVLSPgpGRVVERLPLDFARRYAAGE 229
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
807-1022 9.94e-28

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 113.10  E-value: 9.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599  807 VSVRSLEKRFPG