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Conserved domains on  [gi|1039750680|ref|XP_017172377|]
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multidrug resistance-associated protein 1 isoform X2 [Mus musculus]

Protein Classification

ABC transporter C family protein( domain architecture ID 1000085)

ATP-binding cassette transporter C (ABCC) family protein similar to human multidrug resistance-associated protein 1 that mediates export of organic anions and drugs from the cytoplasm

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MRP_assoc_pro super family cl33195
multi drug resistance-associated protein (MRP); This model describes multi drug ...
7-773 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


The actual alignment was detected with superfamily member TIGR00957:

Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 1586.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680    7 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICW 86
Cdd:TIGR00957    1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680   87 ADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAH 166
Cdd:TIGR00957   81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  167 VDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNK 246
Cdd:TIGR00957  161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  247 EDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPpKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYF 326
Cdd:TIGR00957  241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGK-KDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYF 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  327 LMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYR 406
Cdd:TIGR00957  320 LMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  407 KALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAM 486
Cdd:TIGR00957  400 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAM 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  487 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTF 566
Cdd:TIGR00957  480 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITF 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  567 AVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITV 646
Cdd:TIGR00957  560 AVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITV 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  647 KNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENI 726
Cdd:TIGR00957  640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 1039750680  727 LFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:TIGR00957  720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKgVNLSGGQKQ 767
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
7-773 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 1586.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680    7 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICW 86
Cdd:TIGR00957    1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680   87 ADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAH 166
Cdd:TIGR00957   81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  167 VDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNK 246
Cdd:TIGR00957  161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  247 EDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPpKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYF 326
Cdd:TIGR00957  241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGK-KDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYF 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  327 LMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYR 406
Cdd:TIGR00957  320 LMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  407 KALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAM 486
Cdd:TIGR00957  400 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAM 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  487 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTF 566
Cdd:TIGR00957  480 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITF 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  567 AVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITV 646
Cdd:TIGR00957  560 AVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITV 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  647 KNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENI 726
Cdd:TIGR00957  640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 1039750680  727 LFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:TIGR00957  720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKgVNLSGGQKQ 767
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
329-617 3.23e-175

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 504.31  E-value: 3.23e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 329 SFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKA 408
Cdd:cd18595     2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 409 LLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKT 488
Cdd:cd18595    82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 489 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAV 568
Cdd:cd18595   162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039750680 569 FVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18595   242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
PLN03130 PLN03130
ABC transporter C family member; Provisional
103-773 1.77e-125

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 411.05  E-value: 1.77e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  103 APVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISaLKkdahvDVFRDSTFYLYFTLV 182
Cdd:PLN03130   108 PPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISEV 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  183 LVQLVLSCF-----------SDCSPLFSETVHD---------RNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLW 242
Cdd:PLN03130   182 AAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  243 SLNKEDTSEEVVPVLVNNWKKECdksrkqpvrivyappkdpSKPKgssqldvneevealivksphkdrePSLFKVLYKTF 322
Cdd:PLN03130   262 KLDTWDQTETLYRSFQKCWDEEL------------------KKPK------------------------PWLLRALNNSL 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  323 GPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREaPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVG 402
Cdd:PLN03130   300 GGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVA 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  403 AVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNA 482
Cdd:PLN03130   379 AVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQT 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVA 562
Cdd:PLN03130   459 FIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVT 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  563 LSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPDSierrSIKSGE 640
Cdd:PLN03130   539 VVSFGVFTLLG--GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNP----PLEPGL 612
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  641 gNSITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQ 718
Cdd:PLN03130   613 -PAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIF 691
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680  719 NDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:PLN03130   692 NATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERgVNISGGQKQ 747
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
313-764 7.74e-42

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 161.49  E-value: 7.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 313 SLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPKILELIINFVNDreAPDWQG-YFYTALLFVSACLQTLALHQYFHI 388
Cdd:COG1132     7 KLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLA--GGDLSAlLLLLLLLLGLALLRALLSYLQRYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 389 CFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYFLwLSLGPSV 467
Cdd:COG1132    85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVL-FVIDWRL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 468 -LAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FQDKVMSIRQEELKVLKK 542
Cdd:COG1132   164 aLIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLRAARL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 543 SA-YLAAVGTFTWVCTPFLVALSTFAVF---VTVDErnildakkaFVS-LALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:COG1132   244 SAlFFPLMELLGNLGLALVLLVGGLLVLsgsLTVGD---------LVAfILYLLRLFGPLRQLANVLNQLQRALASAERI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 618 RIFLSHEELEPDSIERRSIKSGEGnSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 697
Cdd:COG1132   315 FELLDEPPEIPDPPGAVPLPPVRG-EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 698 VEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP---LQEnyykaVMEAC---ALLPDLEILPSGDR 758
Cdd:COG1132   393 TSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdatDEE-----VEEAAkaaQAHEFIEALPDGYD 467

                  ....*.
gi 1039750680 759 TEIGEK 764
Cdd:COG1132   468 TVVGER 473
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
326-597 6.50e-40

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 148.56  E-value: 6.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 326 FLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQ--GYFYTALLFVSACLQTLALHQyFHICFVSGMRIKTAVVGA 403
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQ-SYLLNHTGERLSRRLRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 404 VYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSV-LAGVAVMILMVPLNA 482
Cdd:pfam00664  80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKV-LKKSAYLAAVGTFTWVCTPFLV 561
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSY 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039750680 562 ALSTFAVFVTVDeRNILDAKKAFVSLALFNILRFPL 597
Cdd:pfam00664 240 ALALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
661-734 5.29e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.04  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVT-LKGS-------------VAYVPQqawi---qndSL 722
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIAGARKIqQGRVEvLGGDmadarhrravcprIAYMPQglgknlyptlSV 95
                          90
                  ....*....|....*..
gi 1039750680 723 RENI-----LFGHPLQE 734
Cdd:NF033858   96 FENLdffgrLFGQDAAE 112
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
7-773 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 1586.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680    7 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICW 86
Cdd:TIGR00957    1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680   87 ADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAH 166
Cdd:TIGR00957   81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  167 VDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNK 246
Cdd:TIGR00957  161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  247 EDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPpKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYF 326
Cdd:TIGR00957  241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGK-KDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYF 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  327 LMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYR 406
Cdd:TIGR00957  320 LMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYR 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  407 KALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAM 486
Cdd:TIGR00957  400 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAM 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  487 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTF 566
Cdd:TIGR00957  480 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITF 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  567 AVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITV 646
Cdd:TIGR00957  560 AVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITV 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  647 KNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENI 726
Cdd:TIGR00957  640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*...
gi 1039750680  727 LFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:TIGR00957  720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKgVNLSGGQKQ 767
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
329-617 3.23e-175

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 504.31  E-value: 3.23e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 329 SFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKA 408
Cdd:cd18595     2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 409 LLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKT 488
Cdd:cd18595    82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 489 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAV 568
Cdd:cd18595   162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039750680 569 FVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18595   242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
328-617 7.28e-133

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 395.81  E-value: 7.28e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 328 MSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRK 407
Cdd:cd18559     1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 408 ALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMK 487
Cdd:cd18559    81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18559   161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039750680 568 VFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18559   241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
PLN03130 PLN03130
ABC transporter C family member; Provisional
103-773 1.77e-125

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 411.05  E-value: 1.77e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  103 APVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISaLKkdahvDVFRDSTFYLYFTLV 182
Cdd:PLN03130   108 PPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISEV 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  183 LVQLVLSCF-----------SDCSPLFSETVHD---------RNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLW 242
Cdd:PLN03130   182 AAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  243 SLNKEDTSEEVVPVLVNNWKKECdksrkqpvrivyappkdpSKPKgssqldvneevealivksphkdrePSLFKVLYKTF 322
Cdd:PLN03130   262 KLDTWDQTETLYRSFQKCWDEEL------------------KKPK------------------------PWLLRALNNSL 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  323 GPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREaPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVG 402
Cdd:PLN03130   300 GGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVA 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  403 AVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNA 482
Cdd:PLN03130   379 AVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQT 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVA 562
Cdd:PLN03130   459 FIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVT 538
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  563 LSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPDSierrSIKSGE 640
Cdd:PLN03130   539 VVSFGVFTLLG--GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNP----PLEPGL 612
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  641 gNSITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQ 718
Cdd:PLN03130   613 -PAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIF 691
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680  719 NDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:PLN03130   692 NATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERgVNISGGQKQ 747
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
329-617 2.59e-122

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 368.74  E-value: 2.59e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 329 SFLYKALHDLMMFAGPKILELIINFVNDREAPD-WQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRK 407
Cdd:cd18579     2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 408 ALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMK 487
Cdd:cd18579    82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18579   162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039750680 568 VFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18579   242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
PLN03232 PLN03232
ABC transporter C family member; Provisional
206-778 5.91e-111

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 369.30  E-value: 5.91e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  206 NPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKEcdkSRKqpvrivyappkdpsk 285
Cdd:PLN03232   225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE---SRR--------------- 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  286 PKgssqldvneevealivksphkdrePSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREaPDWQGY 365
Cdd:PLN03232   287 PK------------------------PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGY 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  366 FYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMI 445
Cdd:PLN03232   342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGL 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  446 WSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 525
Cdd:PLN03232   422 WSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSF 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  526 QDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVIS 605
Cdd:PLN03232   502 ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLG--GDLTPARAFTSLSLFAVLRSPLNMLPNLLS 579
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  606 SIVQASVSLKRL-RIFLSHEE-------LEPDSierrsiksgegNSITVKNATFTW-ARGEPPTLNGITFSIPEGALVAV 676
Cdd:PLN03232   580 QVVNANVSLQRIeELLLSEERilaqnppLQPGA-----------PAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAI 648
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  677 VGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPS 755
Cdd:PLN03232   649 VGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPG 728
                          570       580
                   ....*....|....*....|...
gi 1039750680  756 GDRTEIGEKVSVVQGRSQSRWKM 778
Cdd:PLN03232   729 RDLTEIGERGVNISGGQKQRVSM 751
ABC_6TM_VMR1_D1_like cd18596
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
330-617 7.41e-86

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350040 [Multi-domain]  Cd Length: 309  Bit Score: 274.37  E-value: 7.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 330 FLYKALHDLMMFAGPKILELIINFV-NDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKA 408
Cdd:cd18596     3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 409 LLI-------------------TNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLA 469
Cdd:cd18596    83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 470 GVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAV 549
Cdd:cd18596   163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 550 GTFTWVCTPFLVALSTFAVFVTVdERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18596   243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
ABC_6TM_MRP7_D1_like cd18598
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ...
331-617 2.21e-82

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350042 [Multi-domain]  Cd Length: 288  Bit Score: 264.41  E-value: 2.21e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 331 LYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQY-FHICFVSgMRIKTAVVGAVYRKAL 409
Cdd:cd18598     4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYnFQMNKVS-LKVRAALVTAVYRKAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 410 LITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTK 489
Cdd:cd18598    83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 490 TYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVF 569
Cdd:cd18598   163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039750680 570 VTVdeRNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18598   243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
ABC_6TM_YOR1_D1_like cd18597
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ...
328-617 1.22e-79

Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350041 [Multi-domain]  Cd Length: 293  Bit Score: 257.38  E-value: 1.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 328 MSFLYKALHDLMMFAGPKILELIINFVNDREA-----PDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVG 402
Cdd:cd18597     1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 403 AVYRKALLITNAARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLN 481
Cdd:cd18597    81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 482 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLV 561
Cdd:cd18597   160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680 562 ALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18597   240 SMLSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
ABC_6TM_SUR1_D1_like cd18591
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ...
331-617 3.00e-73

Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350035 [Multi-domain]  Cd Length: 309  Bit Score: 240.99  E-value: 3.00e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 331 LYKALHDLMMFAGPKILELIINFVNDREAPDWQ------------------GYFYTALLFVSACLQTLALHQYFHICFVS 392
Cdd:cd18591     4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 393 GMRIKTAVVGAVYRKALLIT--NAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAG 470
Cdd:cd18591    84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 471 VAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVG 550
Cdd:cd18591   164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 551 TFTWVCTPFLVALSTFAVFVTVDERNiLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18591   244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
ABC_6TM_CFTR_D1 cd18594
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
349-617 3.36e-67

Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.


Pssm-ID: 350038 [Multi-domain]  Cd Length: 291  Bit Score: 224.05  E-value: 3.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 349 LIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLM 428
Cdd:cd18594    23 LVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTGHIVNLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 429 SVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNE 508
Cdd:cd18594   103 SNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 509 ILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVdeRNILDAKKAFVSLA 588
Cdd:cd18594   183 IISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLT--GNTLTARKVFTVIS 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039750680 589 LFNILRFPLNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18594   261 LLNALRMTITRfFPESIQTLSESRVSLKRI 290
ABC_6TM_MRP4_D1_like cd18593
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ...
362-617 3.61e-64

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350037 [Multi-domain]  Cd Length: 291  Bit Score: 215.93  E-value: 3.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 362 WQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATY 441
Cdd:cd18593    37 TEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 442 INMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAmktktYQVAHMKSK-----DNRIKLMNEILNGIKVL 516
Cdd:cd18593   117 LHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEIINGIRVI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 517 KLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRFP 596
Cdd:cd18593   192 KMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLG--NILTAERVFVTMALYNAVRLT 269
                         250       260
                  ....*....|....*....|..
gi 1039750680 597 LNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18593   270 MTLfFPFAIQFGSELSVSIRRI 291
PTZ00243 PTZ00243
ABC transporter; Provisional
291-764 2.61e-63

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 231.21  E-value: 2.61e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  291 QLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTAL 370
Cdd:PTZ00243   211 RLYLSSTGSVVRPGPPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLT 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  371 LFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNA--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSA 448
Cdd:PTZ00243   291 LFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSS 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  449 PLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDK 528
Cdd:PTZ00243   371 PMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVAN 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  529 VMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIV 608
Cdd:PTZ00243   451 IEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLG--HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVL 528
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  609 QASVSLKRLRIFLSHE--------ELEPDSIERRSIKSGEGNSITVKNATFT-----------------------W---- 653
Cdd:PTZ00243   529 QFLVSIKRISTFLECDnatcstvqDMEEYWREQREHSTACQLAAVLENVDVTafvpvklprapkvktsllsralrMlcce 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  654 -----ARGEPPT-------------------------------------------------------LNGITFSIPEGAL 673
Cdd:PTZ00243   609 qcrptKRHPSPSvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKL 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  674 VAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEIL 753
Cdd:PTZ00243   689 TVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQL 768
                          570
                   ....*....|.
gi 1039750680  754 PSGDRTEIGEK 764
Cdd:PTZ00243   769 GGGLETEIGEK 779
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
644-764 4.09e-61

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 204.63  E-value: 4.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGE---PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQND 720
Cdd:cd03250     1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039750680 721 SLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEK 764
Cdd:cd03250    81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEK 124
ABC_6TM_MRP5_8_9_D1 cd18592
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ...
341-617 2.21e-52

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350036 [Multi-domain]  Cd Length: 287  Bit Score: 183.92  E-value: 2.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 341 FAGPKIL-ELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSs 419
Cdd:cd18592    14 FIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDKS- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 420 tVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSK 499
Cdd:cd18592    93 -VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 500 DNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTftwVCTPFLVALSTFAVFVT-VDERNIL 578
Cdd:cd18592   172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISI---SLAPIVPVIASVVTFLAhVALGNDL 248
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039750680 579 DAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18592   249 TAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
209-775 8.84e-52

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 196.28  E-value: 8.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  209 PESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKECDKSRKQPvrivyappkdpskpkg 288
Cdd:TIGR01271    5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNP---------------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  289 ssqldvneevealivksphkdrepSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYT 368
Cdd:TIGR01271   69 ------------------------KLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYL 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  369 A----LLFVsacLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINM 444
Cdd:TIGR01271  125 AlglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHF 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  445 IWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 524
Cdd:TIGR01271  202 VWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  525 FQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALST---FAVFVTVDERNIldakkaFVSLALFNILRFPLN-IL 600
Cdd:TIGR01271  282 MEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSvvpYALIKGIILRRI------FTTISYCIVLRMTVTrQF 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  601 PMVISSIVQASVSLKRLRIFLSHEELepdsierrsiKSGEGN----SITVKNATFTW----------------ARGEP-- 658
Cdd:TIGR01271  356 PGAIQTWYDSLGAITKIQDFLCKEEY----------KTLEYNltttEVEMVNVTASWdegigelfekikqnnkARKQPng 425
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  659 --------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRE 724
Cdd:TIGR01271  426 ddglffsnfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKD 505
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039750680  725 NILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:TIGR01271  506 NIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRAR 556
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
313-764 7.74e-42

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 161.49  E-value: 7.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 313 SLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPKILELIINFVNDreAPDWQG-YFYTALLFVSACLQTLALHQYFHI 388
Cdd:COG1132     7 KLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLA--GGDLSAlLLLLLLLLGLALLRALLSYLQRYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 389 CFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYFLwLSLGPSV 467
Cdd:COG1132    85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVL-FVIDWRL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 468 -LAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FQDKVMSIRQEELKVLKK 542
Cdd:COG1132   164 aLIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLRAARL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 543 SA-YLAAVGTFTWVCTPFLVALSTFAVF---VTVDErnildakkaFVS-LALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:COG1132   244 SAlFFPLMELLGNLGLALVLLVGGLLVLsgsLTVGD---------LVAfILYLLRLFGPLRQLANVLNQLQRALASAERI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 618 RIFLSHEELEPDSIERRSIKSGEGnSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 697
Cdd:COG1132   315 FELLDEPPEIPDPPGAVPLPPVRG-EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 698 VEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP---LQEnyykaVMEAC---ALLPDLEILPSGDR 758
Cdd:COG1132   393 TSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdatDEE-----VEEAAkaaQAHEFIEALPDGYD 467

                  ....*.
gi 1039750680 759 TEIGEK 764
Cdd:COG1132   468 TVVGER 473
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
326-597 6.50e-40

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 148.56  E-value: 6.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 326 FLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQ--GYFYTALLFVSACLQTLALHQyFHICFVSGMRIKTAVVGA 403
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQ-SYLLNHTGERLSRRLRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 404 VYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSV-LAGVAVMILMVPLNA 482
Cdd:pfam00664  80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKV-LKKSAYLAAVGTFTWVCTPFLV 561
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSY 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039750680 562 ALSTFAVFVTVDeRNILDAKKAFVSLALFNILRFPL 597
Cdd:pfam00664 240 ALALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
644-775 2.59e-36

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 136.31  E-value: 2.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGePPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL-----------------KG 706
Cdd:cd03290     1 VQVTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsfeatrsrnRY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039750680 707 SVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:cd03290    80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQR 148
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
308-763 9.40e-34

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 138.43  E-value: 9.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 308 KDREPSLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWqGYFYTALLFVSACLQTL--AL 382
Cdd:COG2274   137 RGEKPFGLRWFLRLLRRYrrlLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLST-LWVLAIGLLLALLFEGLlrLL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 383 HQYF--HIcfvsGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNlmsvdaqRFMDLATYINMIWSAPLQVILALYFLW 460
Cdd:COG2274   216 RSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVL 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 461 LSL-------GPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIR 533
Cdd:COG2274   285 IFLivlffysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLL 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 534 QEELKVLKKSAYLAAVGTFTwvcTPFLVALSTFAVFVT----VDERNI-LDAKKAFVSLalfnILRF--PLNILPMVISS 606
Cdd:COG2274   365 AKYLNARFKLRRLSNLLSTL---SGLLQQLATVALLWLgaylVIDGQLtLGQLIAFNIL----SGRFlaPVAQLIGLLQR 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 607 IVQASVSLKRLRIFLSHEeLEPDSIERRSIKSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSS 686
Cdd:COG2274   438 FQDAKIALERLDDILDLP-PEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 687 LLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHPLQEnyYKAVMEAC---ALLPDL 750
Cdd:COG2274   517 LLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDAT--DEEIIEAArlaGLHDFI 594
                         490
                  ....*....|...
gi 1039750680 751 EILPSGDRTEIGE 763
Cdd:COG2274   595 EALPMGYDTVVGE 607
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
620-763 5.02e-22

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 100.99  E-value: 5.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 620 FLSHEELEPDSIERrSIKSGEGNSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 699
Cdd:COG4988   314 LLDAPEPAAPAGTA-PLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 700 GHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP------LQenyykAVMEACALLPDLEILPSGDRTE 760
Cdd:COG4988   392 GSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdasdeeLE-----AALEAAGLDEFVAALPDGLDTP 466

                  ...
gi 1039750680 761 IGE 763
Cdd:COG4988   467 LGE 469
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
338-617 7.38e-22

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 96.47  E-value: 7.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 338 LMMFAGPKILELIINFVndREAPDWQGYFYTALLFVSAC-LQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAAR 416
Cdd:cd07346    13 ALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 417 KSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYFLwLSLGPSV-LAGVAVMILMVPLNAVMAMKTKTYQVA 494
Cdd:cd07346    91 DRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVIL-FYLNWKLtLVALLLLPLYVLILRYFRRRIRKASRE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 495 HMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAvgtFTWVCTPFLVALSTFAVFV---- 570
Cdd:cd07346   170 VRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA---LFSPLIGLLTALGTALVLLyggy 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039750680 571 -TVDERniLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd07346   247 lVLQGS--LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
644-727 3.44e-21

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: 91.29  E-value: 3.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03228     1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
                          90
                  ....*....|....*..
gi 1039750680 711 VPQQAWIQNDSLRENIL 727
Cdd:cd03228    81 VPQDPFLFSGTIRENIL 97
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
659-775 5.21e-21

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 93.77  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYK 738
Cdd:cd03291    51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039750680 739 AVMEACALLPDLEILPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:cd03291   131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRAR 167
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
450-763 1.06e-18

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 90.42  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 450 LQVILALYFLWLSLGPSVLAGVaVMILMVPLNAV-MA---MKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 525
Cdd:TIGR02857 127 LAVIVPLAILAAVFPQDWISGL-ILLLTAPLIPIfMIligWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQ 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 526 QDKVMSI----RQEELKVLKKSAYLAAVgtftwvcTPFLVALSTFAVFVTVDERNI---LDAKKAFVSLALFNILRFPLN 598
Cdd:TIGR02857 206 AAAIRRSseeyRERTMRVLRIAFLSSAV-------LELFATLSVALVAVYIGFRLLagdLDLATGLFVLLLAPEFYLPLR 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 599 ILPMVISSIVQASVSLKRLRIFLSHEELEpdSIERRSIKSGEGNSITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVG 678
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVG 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 679 QVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHPLQ-ENYYKAVMEAC 744
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPDAsDAEIREALERA 435
                         330
                  ....*....|....*....
gi 1039750680 745 ALLPDLEILPSGDRTEIGE 763
Cdd:TIGR02857 436 GLDEFVAALPQGLDTPIGE 454
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
644-764 2.68e-16

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 78.81  E-value: 2.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03254     3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 711 VPQQAWIQNDSLRENILFGHPlqENYYKAVMEACALL-PDLEI--LPSGDRTEIGEK 764
Cdd:cd03254    82 VLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAgAHDFImkLPNGYDTVLGEN 136
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
644-729 1.49e-15

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 74.95  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAY 710
Cdd:cd03246     1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
                          90
                  ....*....|....*....
gi 1039750680 711 VPQQAWIQNDSLRENILFG 729
Cdd:cd03246    81 LPQDDELFSGSIAENILSG 99
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
644-764 2.14e-15

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 76.12  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03251     1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 711 VPQQAWIQNDSLRENILFGHPlqENYYKAVMEAC--ALLPDL-EILPSGDRTEIGEK 764
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRP--GATREEVEEAAraANAHEFiMELPEGYDTVIGER 135
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
644-764 1.09e-14

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 74.11  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VA 709
Cdd:cd03249     1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 710 YVPQQAWIQNDSLRENILFGHPLQENyyKAVMEAC--ALLPD-LEILPSGDRTEIGEK 764
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAkkANIHDfIMSLPDGYDTLVGER 136
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
661-739 2.17e-14

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 71.14  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQND-SLRENI 726
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
                          90
                  ....*....|...
gi 1039750680 727 LFGHPLQENYYKA 739
Cdd:pfam00005  81 RLGLLLKGLSKRE 93
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
644-715 2.89e-14

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 73.20  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQA 715
Cdd:COG1121     7 IELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRA 84
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
643-764 7.37e-14

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 71.47  E-value: 7.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:cd03245     2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 710 YVPQQAWIQNDSLRENILFGHPLQENyyKAVMEACALL---PDLEILPSGDRTEIGEK 764
Cdd:cd03245    82 YVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELAgvtDFVNKHPNGLDLQIGER 137
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
643-769 1.53e-13

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 70.60  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVA 709
Cdd:cd03244     2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglhdLRSRIS 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680 710 YVPQQAWIQNDSLRENIlfgHPLQENYYKAVMEA---CALLPDLEILPSGDRTEI---GEKVSVVQ 769
Cdd:cd03244    82 IIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVeegGENLSVGQ 144
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
643-731 2.94e-13

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 73.32  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:PRK11160  338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
                          90       100
                  ....*....|....*....|..
gi 1039750680 710 YVPQQAWIQNDSLRENILFGHP 731
Cdd:PRK11160  418 VVSQRVHLFSATLRDNLLLAAP 439
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
644-729 5.90e-12

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: 65.96  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG--------SVAYVP 712
Cdd:cd03293     1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERPtSGEVLVDGepvtgpgpDRGYVF 79
                          90       100
                  ....*....|....*....|.
gi 1039750680 713 QQA----WIqndSLRENILFG 729
Cdd:cd03293    80 QQDallpWL---TVLDNVALG 97
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
646-729 8.60e-12

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: 65.18  E-value: 8.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 646 VKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVP 712
Cdd:cd03225     2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
                          90
                  ....*....|....*....
gi 1039750680 713 QQAWIQ--NDSLRENILFG 729
Cdd:cd03225    82 QNPDDQffGPTVEEEVAFG 100
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
634-773 1.10e-11

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 68.12  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 634 RSIKSGEGNsITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------- 706
Cdd:PRK11176  333 RVIERAKGD-IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyt 411
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 707 ------SVAYVPQQAWIQNDSLRENIlfGHPLQENYYKAVMEACALLPD----LEILPSGDRTEIGEK-VSVVQGRSQ 773
Cdd:PRK11176  412 laslrnQVALVSQNVHLFNDTIANNI--AYARTEQYSREQIEEAARMAYamdfINKMDNGLDTVIGENgVLLSGGQRQ 487
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
620-769 2.06e-11

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 67.18  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 620 FLSHEELEPDSiERRSIKSGEGNSITVKNATFTWARGEPptLNG-ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdKV 698
Cdd:PRK11174  327 FLETPLAHPQQ-GEKELASNDPVTIEAEDLEILSPDGKT--LAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 699 EGHVTLKG------SVAYVPQQ-AWI-QN-----DSLRENILFGHP-LQENYYKAVMEACALLPDLEILPSGDRTEIGEK 764
Cdd:PRK11174  403 QGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQ 482

                  ....*...
gi 1039750680 765 ---VSVVQ 769
Cdd:PRK11174  483 aagLSVGQ 490
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
646-743 4.32e-11

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: 63.32  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 646 VKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQAWI 717
Cdd:cd03235     2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSI 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039750680 718 QND---SLRENIL--------FGHPLQENYYKAVMEA 743
Cdd:cd03235    80 DRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEA 116
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
644-728 5.67e-11

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 62.89  E-value: 5.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 706
Cdd:cd03255     1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaaf 79
                          90       100
                  ....*....|....*....|....*.
gi 1039750680 707 ---SVAYVPQQ-AWIQNDSLRENILF 728
Cdd:cd03255    80 rrrHIGFVFQSfNLLPDLTALENVEL 105
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
634-774 6.73e-11

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 65.51  E-value: 6.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 634 RSIKSGegnSITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------- 706
Cdd:PRK10790  334 RPLQSG---RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplssls 409
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 707 ------SVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEkvsvvQGRSQS 774
Cdd:PRK10790  410 hsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE-----QGNNLS 478
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
596-766 8.40e-11

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 65.23  E-value: 8.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 596 PLNILPMVISSIVQASVSLKRLriF-LSHEELEP-DSIERRSIKSGEGnSITVKNATFTWaRGEPPTLNGITFSIPEGAL 673
Cdd:COG5265   311 PLNFLGFVYREIRQALADMERM--FdLLDQPPEVaDAPDAPPLVVGGG-EVRFENVSFGY-DPERPILKGVSFEVPAGKT 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 674 VAVVGQVGCGKSSLLSALLAEMDKVEG----------HVT---LKGSVAYVPQQAWIQNDSLRENILFGHP--LQENYYK 738
Cdd:COG5265   387 VAIVGPSGAGKSTLARLLFRFYDVTSGrilidgqdirDVTqasLRAAIGIVPQDTVLFNDTIAYNIAYGRPdaSEEEVEA 466
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039750680 739 AVmEACALLPDLEILPSGDRTEIGE---KVS 766
Cdd:COG5265   467 AA-RAAQIHDFIESLPDGYDTRVGErglKLS 496
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
645-713 5.83e-10

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: 58.41  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 645 TVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYV 711
Cdd:cd00267     1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklpleelrrrIGYV 78

                  ..
gi 1039750680 712 PQ 713
Cdd:cd00267    79 PQ 80
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
643-772 1.99e-09

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 58.19  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:cd03369     6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 710 YVPQQAWIQNDSLRENI-LFGHPLQENYYKAvmeacallpdLEILPSGDRTEIGEKVSVVQGRS 772
Cdd:cd03369    86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIYGA----------LRVSEGGLNLSQGQRQLLCLARA 139
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
583-774 2.29e-09

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 60.75  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 583 AFVSLALFNILRfplniLPMVISSIVQASVSLKRLRIFLSHEELEPDSIER---RSIKSGEGnSITVKNATFTWArGEPP 659
Cdd:PRK13657  277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPpgaIDLGRVKG-AVEFDDVSFSYD-NSRQ 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 660 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI 726
Cdd:PRK13657  350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNI 429
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039750680 727 LFGHP--LQENYYKAvMEACALLPDLEILPSGDRTEIGEKvsvvqGRSQS 774
Cdd:PRK13657  430 RVGRPdaTDEEMRAA-AERAQAHDFIERKPDGYDTVVGER-----GRQLS 473
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
590-750 3.01e-09

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 60.21  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 590 FNILRFPLNILPMVISSIVQASVSLKRLRIFLSH-EELEPDSIERRSIKSGEGNSITVKNATFTWARGEPpTLNGITFSI 668
Cdd:COG4178   308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEAlEAADALPEAASRIETSEDGALALEDLTLRTPDGRP-LLEDLSLSL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 669 PEGALVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVTL--KGSVAYVPQQAWIQNDSLRENILFGHPlQENY----YKAVM 741
Cdd:COG4178   387 KPGERLLITGPSGSGKSTLLRA-IAGLwPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPAT-AEAFsdaeLREAL 464

                  ....*....
gi 1039750680 742 EACAlLPDL 750
Cdd:COG4178   465 EAVG-LGHL 472
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
644-729 3.18e-09

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 60.30  E-value: 3.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVTLKG-------------S 707
Cdd:COG1123     5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGrdllelsealrgrR 84
                          90       100
                  ....*....|....*....|....
gi 1039750680 708 VAYVPQQAWIQNDSLR--ENILFG 729
Cdd:COG1123    85 IGMVFQDPMTQLNPVTvgDQIAEA 108
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
597-775 5.62e-09

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 59.34  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 597 LNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErrSIKSGEGnSITVKNATFTWARGEPPTLNGITFSIPEG 671
Cdd:PRK10789  265 LMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVKDGSE--PVPEGRG-ELDVNIRQFTYPQTDHPALENVNFTLKPG 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 672 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVAYVPQQAWIQNDSLRENILFGHPlqeNYYK 738
Cdd:PRK10789  342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipltklqldsWRSRLAVVSQTPFLFSDTVANNIALGRP---DATQ 418
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039750680 739 AVMEACALLP----DLEILPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:PRK10789  419 QEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQR 459
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
652-751 1.66e-08

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 57.77  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQQAWIQND-SLRENILF 728
Cdd:COG0488     5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLD 84
                          90       100
                  ....*....|....*....|....*..
gi 1039750680 729 GHP----LQENYYKAVMEACALLPDLE 751
Cdd:COG0488    85 GDAelraLEAELEELEAKLAEPDEDLE 111
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
644-775 3.01e-08

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 57.42  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVA 558
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 710 YVPQQAWIQNDSLRENILFG--HPLQENYYKAVMEACALLPDLEiLPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIME-FPNGYDTEVGEKGSQLSGGQKQR 625
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
644-713 3.31e-08

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: 54.82  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------- 706
Cdd:cd03257     2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirr 81

                  ....*...
gi 1039750680 707 -SVAYVPQ 713
Cdd:cd03257    82 kEIQMVFQ 89
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
644-728 7.53e-08

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 53.64  E-value: 7.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 711
Cdd:COG4133     3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYL 80
                          90
                  ....*....|....*...
gi 1039750680 712 PQQ-AWIQNDSLRENILF 728
Cdd:COG4133    81 GHAdGLKPELTVRENLRF 98
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
644-731 1.38e-07

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 52.95  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVPQQAWIq 718
Cdd:cd03260     1 IELRDLNV--YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVL- 77
                          90
                  ....*....|....*
gi 1039750680 719 ndSLRENI--LFGHP 731
Cdd:cd03260    78 --ELRRRVgmVFQKP 90
PLN03232 PLN03232
ABC transporter C family member; Provisional
395-726 2.59e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 54.60  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  395 RIKTAVVGAVYRKALLITNaarkSSTVGEIVNLMSVDAQRF-MDLATYINMIwsaplqvilaLYFLWLSLGPSVLAGVAV 473
Cdd:PLN03232   984 RLHDAMLNSILRAPMLFFH----TNPTGRVINRFSKDIGDIdRNVANLMNMF----------MNQLWQLLSTFALIGTVS 1049
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  474 MILMVPLNAVMAMKTKTYQVAHMKSKDNR----------IKLMNEILNG---IKVLKLYAWELAFQDKVM--SIRQEeLK 538
Cdd:PLN03232  1050 TISLWAIMPLLILFYAAYLYYQSTSREVRrldsvtrspiYAQFGEALNGlssIRAYKAYDRMAKINGKSMdnNIRFT-LA 1128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  539 VLKKSAYLAAV-----GTFTWVctpflvaLSTFAVFVTVDERNildaKKAFVSLALFnILRFPLNILPMVISSIVQASV- 612
Cdd:PLN03232  1129 NTSSNRWLTIRletlgGVMIWL-------TATFAVLRNGNAEN----QAGFASTMGL-LLSYTLNITTLLSGVLRQASKa 1196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  613 -----SLKRLRIFLSHEELEPDSIERRSIKSG--EGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKS 685
Cdd:PLN03232  1197 enslnSVERVGNYIDLPSEATAIIENNRPVSGwpSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039750680  686 SLLSAL--LAEMDKVE-----------GHVTLKGSVAYVPQQAWIQNDSLRENI 726
Cdd:PLN03232  1277 SMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
644-706 2.95e-07

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 53.75  E-value: 2.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680 644 ITVKNATFTW---ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:COG1123   261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
644-706 4.19e-07

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 51.73  E-value: 4.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039750680 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:cd03261     1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG 61
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
643-728 4.61e-07

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 51.01  E-value: 4.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFT----WARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVTLKG---------- 706
Cdd:cd03213     3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGrpldkrsfrk 82
                          90       100
                  ....*....|....*....|...
gi 1039750680 707 SVAYVPQQ-AWIQNDSLRENILF 728
Cdd:cd03213    83 IIGYVPQDdILHPTLTVRETLMF 105
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
614-725 4.83e-07

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 53.14  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 614 LKRLriflshEELEPDSIERRS------IKSGE--GNS-ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGK 684
Cdd:COG0488   283 IKAL------EKLEREEPPRRDktveirFPPPErlGKKvLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039750680 685 SSLLSALLAEMDKVEGHVTLkGS---VAYVPQqawiQNDSLREN 725
Cdd:COG0488   355 STLLKLLAGELEPDSGTVKL-GEtvkIGYFDQ----HQEELDPD 393
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
656-707 5.29e-07

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 51.60  E-value: 5.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLKGS 707
Cdd:PRK11247   23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLAGT 73
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
644-775 8.23e-07

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 50.95  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL----LAEMDKV--EGH-------VTLKGSVAY 710
Cdd:cd03252     1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyVPENGRVlvDGHdlaladpAWLRRQVGV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 711 VPQQAWIQNDSLRENILFGHPLQEnyYKAVMEACALLPDLEI---LPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMS--MERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQR 146
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
644-729 1.03e-06

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: 49.49  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------------SV 708
Cdd:cd03229     1 LELKNVSKR--YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRI 78
                          90       100
                  ....*....|....*....|..
gi 1039750680 709 AYVPQQ-AWIQNDSLRENILFG 729
Cdd:cd03229    79 GMVFQDfALFPHLTVLENIALG 100
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
643-713 1.09e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 51.04  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS----------VAYVP 712
Cdd:PRK15056    6 GIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84

                  .
gi 1039750680 713 Q 713
Cdd:PRK15056   85 Q 85
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
647-775 1.73e-06

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 49.78  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 647 KNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVP 712
Cdd:cd03248    15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680 713 QQAWIQNDSLRENILFGhpLQENYYKAVMEACALL---PDLEILPSGDRTEIGEKVSVVQGRSQSR 775
Cdd:cd03248    95 QEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAhahSFISELASGYDTEVGEKGSQLSGGQKQR 158
cbiO PRK13640
energy-coupling factor transporter ATPase;
642-706 1.75e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.57  E-value: 1.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 642 NSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLAEMDKVEGHVTLKG 706
Cdd:PRK13640    4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG 71
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
644-726 1.89e-06

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 50.24  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03289     3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
                          90
                  ....*....|....*.
gi 1039750680 711 VPQQAWIQNDSLRENI 726
Cdd:cd03289    82 IPQKVFIFSGTFRKNL 97
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
643-729 2.01e-06

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 49.65  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAY 710
Cdd:cd03296     2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqerNVGF 78
                          90       100
                  ....*....|....*....|
gi 1039750680 711 VPQQ-AWIQNDSLRENILFG 729
Cdd:cd03296    79 VFQHyALFRHMTVFDNVAFG 98
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
644-692 3.15e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 49.60  E-value: 3.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALL 692
Cdd:PRK13632    8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLL 59
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
644-715 5.86e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 49.45  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:PRK09536    4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVAS 81

                  ....*
gi 1039750680 711 VPQQA 715
Cdd:PRK09536   82 VPQDT 86
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
655-706 6.80e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 48.44  E-value: 6.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 655 RGEPPTL--------NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK10253    9 RGEQLTLgygkytvaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG 68
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
643-731 8.00e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 48.11  E-value: 8.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 643 SITVKNATFTWARGEppTLNGITFSIPEGALVAVVGQVGCGKSSLLSAlLAEMDKVEGHVTLKGSVAYVPQQAW---IQN 719
Cdd:PRK14258    7 AIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrVNL 83
                          90
                  ....*....|..
gi 1039750680 720 DSLRENILFGHP 731
Cdd:PRK14258   84 NRLRRQVSMVHP 95
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
641-726 1.13e-05

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 49.14  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  641 GNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKG-------------S 707
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkA 1293
                           90
                   ....*....|....*....
gi 1039750680  708 VAYVPQQAWIQNDSLRENI 726
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNL 1312
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
634-728 1.14e-05

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 47.14  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 634 RSIKSGEGNSITVKNATFTWARGEPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKGSVA 709
Cdd:cd03220     8 KSYPTYKGGSSSLKKLGILGRKGEVGEfwaLKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPdSGTVTVRGRVS 86
                          90       100
                  ....*....|....*....|.
gi 1039750680 710 YVPQ-QAWIQND-SLRENILF 728
Cdd:cd03220    87 SLLGlGGGFNPElTGRENIYL 107
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
639-702 1.62e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 47.44  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 639 GEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 702
Cdd:PRK13648    3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI 66
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
507-769 1.65e-05

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 48.79  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  507 NEILNGIKVLKlyawelAFQDKVMSIRQEELKV-LKKSAYLAAVGTFTWV-----CTPFLVALstFAVFVTVDERNILDA 580
Cdd:TIGR00957 1148 NETLLGVSVIR------AFEEQERFIHQSDLKVdENQKAYYPSIVANRWLavrleCVGNCIVL--FAALFAVISRHSLSA 1219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  581 KKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSG--EGNSITVKNATFTWARGEP 658
Cdd:TIGR00957 1220 GLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGwpPRGRVEFRNYCLRYREDLD 1299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLREN 725
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMN 1379
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039750680  726 I-LFGHPLQENYYKAvMEACALLPDLEILPSG---DRTEIGEKVSVVQ 769
Cdd:TIGR00957 1380 LdPFSQYSDEEVWWA-LELAHLKTFVSALPDKldhECAEGGENLSVGQ 1426
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
640-706 1.80e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 47.32  E-value: 1.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 640 EGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK13635    2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG 68
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
642-719 2.07e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 47.04  E-value: 2.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039750680 642 NSITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQN 719
Cdd:PRK13647    3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
656-714 2.34e-05

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 46.55  E-value: 2.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQ 714
Cdd:PRK11231   13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQH 84
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
661-734 5.29e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.04  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVT-LKGS-------------VAYVPQqawi---qndSL 722
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIAGARKIqQGRVEvLGGDmadarhrravcprIAYMPQglgknlyptlSV 95
                          90
                  ....*....|....*..
gi 1039750680 723 RENI-----LFGHPLQE 734
Cdd:NF033858   96 FENLdffgrLFGQDAAE 112
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
661-728 5.79e-05

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 46.67  E-value: 5.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLK---GSVAYVPQQAWIQNDSLRENILF 728
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIY 537
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
661-758 7.56e-05

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 44.95  E-value: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG----------SVAYVPQQ-AWIQNDSLRENI 726
Cdd:cd03234    23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039750680 727 LF-----GHPLQENYYKAVMEACALLPDLEILPSGDR 758
Cdd:cd03234   103 TYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGN 139
PLN03130 PLN03130
ABC transporter C family member; Provisional
564-706 7.75e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 46.65  E-value: 7.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680  564 STFAVFVTVDERNildaKKAFVS-LALfnILRFPLNILPMVISSIVQASV------SLKRLRIFLSHEELEPDSIERRSI 636
Cdd:PLN03130  1155 ASFAVMQNGRAEN----QAAFAStMGL--LLSYALNITSLLTAVLRLASLaenslnAVERVGTYIDLPSEAPLVIENNRP 1228
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039750680  637 KSG--EGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PLN03130  1229 PPGwpSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG 1300
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
647-714 1.33e-04

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 43.79  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 647 KNATFTWARGEP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG------------SVA 709
Cdd:cd03233     7 RNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEII 86

                  ....*
gi 1039750680 710 YVPQQ 714
Cdd:cd03233    87 YVSEE 91
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
659-706 1.39e-04

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 43.94  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039750680 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:cd03292    15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG 62
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
644-692 1.90e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 44.31  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039750680 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL 692
Cdd:PRK13651    3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL 57
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
656-713 2.51e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 43.68  E-value: 2.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039750680 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVPQ 713
Cdd:PRK14267   15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPD 77
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
643-706 3.60e-04

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 43.54  E-value: 3.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 643 SITVKNATFtWARgePPTL---NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK15079   19 DIKDGKQWF-WQP--PKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
655-726 4.24e-04

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 42.64  E-value: 4.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhvtlKGSVAyVPQQAWIQNDSLRENI 726
Cdd:COG2401    40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVD-VPDNQFGREASLIDAI 106
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
652-732 4.64e-04

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 42.09  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQN 719
Cdd:cd03231     7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKT 86
                          90
                  ....*....|....
gi 1039750680 720 D-SLRENILFGHPL 732
Cdd:cd03231    87 TlSVLENLRFWHAD 100
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
654-757 5.08e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 42.17  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 654 ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---SALLAemdKVEGHVTLKG----------SVAYV-PQQAWIQN 719
Cdd:PRK13539   11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLrliAGLLP---PAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPA 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039750680 720 DSLRENILF------GHPLqenyykAVMEA-CAL-LPDLEILPSGD 757
Cdd:PRK13539   88 LTVAENLEFwaaflgGEEL------DIAAAlEAVgLAPLAHLPFGY 127
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
644-704 7.53e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 42.31  E-value: 7.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL 704
Cdd:PRK13634    3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI 66
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
655-714 8.65e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 42.85  E-value: 8.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQQ 714
Cdd:PRK10636   11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQE 72
cbiO PRK13641
energy-coupling factor transporter ATPase;
643-706 9.27e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 42.12  E-value: 9.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 643 SITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK13641    2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG 68
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
644-704 9.40e-04

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 41.61  E-value: 9.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 644 ITVKNATftWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-HVTL 704
Cdd:COG1119     4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRL 63
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
643-688 1.01e-03

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 42.14  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039750680 643 SITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLL 688
Cdd:PRK11650    3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL 47
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
661-706 1.18e-03

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 42.36  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVTLKG 706
Cdd:COG4172   302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDG 346
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
644-688 1.28e-03

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 41.60  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039750680 644 ITVKNA--TFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLL 688
Cdd:COG1135     2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI 48
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
661-687 1.29e-03

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 41.87  E-value: 1.29e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSL 687
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTL 57
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
609-713 1.81e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.80  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 609 QASVSLKRL-RIFLshEELEPDSIERRSIKSGEG-----NSITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGC 682
Cdd:PRK15064  281 QATSRAKQIdKIKL--EEVKPSSRQNPFIRFEQDkklhrNALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGV 356
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039750680 683 GKSSLLSALLAEMDKVEGHV--TLKGSVAYVPQ 713
Cdd:PRK15064  357 GKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ 389
cbiO PRK13650
energy-coupling factor transporter ATPase;
642-693 1.90e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 40.87  E-value: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039750680 642 NSITVKNATFTWARG-EPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLA 693
Cdd:PRK13650    3 NIIEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLE 58
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
661-694 1.96e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 40.00  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE 694
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA 44
cbiO PRK13642
energy-coupling factor transporter ATPase;
644-706 2.54e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 40.46  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 644 ITVKNATFTWAR-GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK13642    5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG 68
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
661-711 2.66e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 41.03  E-value: 2.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMD-KVEGHVTLKGSVAYV 711
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKST-LSNLIAGVTmPNKGTVDIKGSAALI 90
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
659-747 2.80e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.19  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMD----KVEGHVTLKGSVA-------Y-VPQQAWI-QNDSLR 723
Cdd:PRK15439   25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKiiAGIVPPDsgtlEIGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVK 104
                          90       100
                  ....*....|....*....|....
gi 1039750680 724 ENILFGHPLQENYYKAVMEACALL 747
Cdd:PRK15439  105 ENILFGLPKRQASMQKMKQLLAAL 128
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
656-728 3.53e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 39.70  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQQAWIQNDSL 722
Cdd:PRK10247   18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTV 97

                  ....*.
gi 1039750680 723 RENILF 728
Cdd:PRK10247   98 YDNLIF 103
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
642-706 4.20e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 39.90  E-value: 4.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 642 NSITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEM---DKVEGHVTLKG 706
Cdd:PRK14247    2 NKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDG 69
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
661-706 4.61e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 39.05  E-value: 4.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-KV-EGHVTLKG 706
Cdd:cd03217    16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVtEGEILFKG 63
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
644-728 6.22e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 38.29  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVTL--KGSVAYVPQQAWIQND 720
Cdd:cd03223     1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRA-LAGLwPWGSGRIGMpeGEDLLFLPQRPYLPLG 78

                  ....*...
gi 1039750680 721 SLRENILF 728
Cdd:cd03223    79 TLREQLIY 86
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
655-730 6.25e-03

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 38.63  E-value: 6.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvPQQAwiQNDSLRENILF-GH 730
Cdd:PRK13538   11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE----PIRR--QRDEYHQDLLYlGH 81
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
344-617 7.75e-03

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 38.93  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 344 PKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGE 423
Cdd:cd18541    19 PRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 424 IVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYF-LWLSLGPSVLAgVAVMILMVPLNAVMAMKTktyqvaHMKSKDN 501
Cdd:cd18541    99 LMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMmFTISPKLTLIA-LLPLPLLALLVYRLGKKI------HKRFRKV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039750680 502 RIKL--MN----EILNGIKVLKLYAWELAFQDKVMSIRQEelkVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFV----- 570
Cdd:cd18541   172 QEAFsdLSdrvqESFSGIRVIKAFVQEEAEIERFDKLNEE---YVEKNLRLARVDALFFPLIGLLIGLSFLIVLWyggrl 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039750680 571 ------TVDErnildakkaFVS-LALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18541   249 virgtiTLGD---------LVAfNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
661-706 8.53e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 38.64  E-value: 8.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039750680 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKG 706
Cdd:PRK11629   25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNG 70
uvrA PRK00349
excinuclease ABC subunit UvrA;
632-688 9.89e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 39.29  E-value: 9.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039750680 632 ERRSiksGEGNSITVKNAtftwaRGEppTLNGITFSIPEGALVAVVGQVGCGKSSLL 688
Cdd:PRK00349  606 ERRK---GNGKFLKLKGA-----REN--NLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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