ID Q96WN4_VENIN Unreviewed; 1551 AA. AC Q96WN4; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 2. DT 17-JUN-2020, entry version 93. DE SubName: Full=ATP-binding cassette transporter ABC1 {ECO:0000313|EMBL:AAK62810.2}; OS Venturia inaequalis (Apple scab fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Venturiales; Venturiaceae; Venturia. OX NCBI_TaxID=5025 {ECO:0000313|EMBL:AAK62810.2}; RN [1] {ECO:0000313|EMBL:AAK62810.2} RP NUCLEOTIDE SEQUENCE. RA Schnabel G., Schnabel E., Jones A.L.; RT "Genes encoding multidrug resistance like proteins in Venturia RT inaequalis."; RL (In) Unknown A. (eds.); RL MODERN FUNGICIDES AND ANTIFUNGAL COMPOUNDS III, pp.297-305, Unknown RL publisher (2001). RN [2] {ECO:0000313|EMBL:AAK62810.2} RP NUCLEOTIDE SEQUENCE. RA Schnabel G., Schnabel E.L., Jones A.L.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. CC PDR (TC 3.A.1.205) subfamily. {ECO:0000256|SAAS:SAAS00709344}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00434}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF227914; AAK62810.2; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro. DR CDD; cd03233; ABCG_PDR_domain1; 1. DR CDD; cd03232; ABCG_PDR_domain2; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR029481; ABC_trans_N. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR034001; ABCG_PDR_1. DR InterPro; IPR034003; ABCG_PDR_2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010929; PDR_CDR_ABC. DR Pfam; PF01061; ABC2_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF14510; ABC_trans_N; 1. DR Pfam; PF06422; PDR_CDR; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434, KW ECO:0000256|SAAS:SAAS00555301, ECO:0000313|EMBL:AAK62810.2}; KW Membrane {ECO:0000256|SAAS:SAAS01257648, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434, KW ECO:0000256|SAAS:SAAS00555311}; Repeat {ECO:0000256|SAAS:SAAS00709352}; KW Transmembrane {ECO:0000256|SAAS:SAAS01257645, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS01257639, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS01257646}. FT TRANSMEM 551..571 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 583..604 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 633..653 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 660..682 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 694..714 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 793..813 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1216..1234 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1246..1269 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1289..1315 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1327..1351 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1357..1375 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1387..1406 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1481..1500 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 188..438 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT DOMAIN 877..1119 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT NP_BIND 913..920 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" FT REGION 1..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 445..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 844..865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1530..1551 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 29..43 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 61..75 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..862 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1551 AA; 173100 MW; 954CDFDEEB256A0A CRC64; MAYAGTKGDG IIRTASGHET YAPDGLGTPQ REYEEEIAPS EDPSRATSER YAPITGHLYR RNSSDTEKGS DEDFTMATRS KSFTENMDTD DKDKLNRILT SLSQHQTRSS TLRRNDTISG LKEDDPVFDP SHKDFDLYKY LRLFMRDLQA DGRETKKAGI VFRNLSVSGS GAALQLQSTV SDFVLAPFRL RELFSSSKSH KQIIDKFDGV LKSGELLIVL GRPGSGCSTF LKTLCGELTG LTVDKGSVIH YNGIPQKKMI KEFKGEVVYN QEVDKHFPHL TVGQTLEFAA AVRTPSNRLH GESRTEFSSQ VAKVVMAVFG LSHTYNTKVG NDFVRGVSGG ERKRVSIAEM AVAGAPLAAW DNSTRGLDSA TALKFVEATR ISADLTGSSH AIAIYQASQA IYDRFDKAVV LYSGRQIYFG PASKAKQFFE EQGWYCPKRQ TTGDFLTSIT NPSERRPREG MEKQVPRTPE DFEKYWRNSE MYQSLQKEIE DHETEFPIGG ETLGKLQQQK RNAQASHTRP KSPYMISVPM QIKLCTKRAY QRIWNDMSST LTMFISQIIM SLIIGSVFYG TPNATAGFFS KGAVLFFAVL LNALVAMTEI NSLYDQRPIV EKHNSYAFYH PATEAIAGIV SDIPVKFLLA VGFNVIFYFL AGLRREPSQF FLYFLVSYVI MFVMAAVFRT MAAVTKTISQ AMSLAGVLVL ALVIYTGFVI PVSYMKPWFG WIHYINPIYY AFEILIANEF HGRDFTCSAI IPAYTPLQGD SWICSIVGAV PGRRTVSGDD FIMQMYQYSY SHVWRNFGIL LGFLCGFMCI YFVGVEVNSS TSSAAEFLIF RRGYVPAYMQ DDPKHAGNDE EKMADGTTDA KEDGGDVSAI PPQKDIFTWR DIVYDIQIKG EDRRLLDHVT GWVRPGTLTA LMGVSGAGKT TLLDVLAQRT TMGVITGDML VNGKPLDASF QRKTGYVQQQ DLHLETATVR ESLRFSAELR QPKTVTLQEK FDYVEDVIKM LNMEDFAEAI VGSPGEGLNV EQRKLLTIGV ELAAKPKLLL FLDEPTSGLD SQSAWAICAF LRKLADAGQA VLCTIHQPSA ILFQEFDRLL FLAKGGKTVY FGPVGKNSET LIDYYESNGA RKCGEEENPA EYMLEIVNKG SSGQGQDWHE VWKGSKEREA VNEELKQIHK EKEGEAIAGA NEEGAQDEFA MPFTAQVKAV TVRVFQQYWR MPSYVFAKWA LGIASGLFIG FSFFQANTTQ QGVQNVLFSA FMIATIFSSL VQQIMPLFVN QRSLYEVRER PSKAYSWKAF MIANIVVEIP YNIFLGVPVF ACYLYAIAGI ISSVRQVLIL LLMIQFFVYA GTFAAMCIAA LPDAETAAAV VTLLFATSLT FNGVMQSPQA LPGFWIFMYR ISPFTYWISS LVSTMLHGRR IECSSSETSR FSPPAGQTCQ QYLADYLQTA PGTLQNPNDT TNCRYCSLST ADQLLAGSNV KYDTRWRDFG IVWSYVIFNI FVAVLTYYLF RVKKWNKGTG KSDGAKKAGF LGKILKKGAN KGNDAKTEKG EQQANQHQRA I //