ID W9CI94_SCLBF Unreviewed; 1559 AA.
AC W9CI94;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Putative ABC bile acid transporter {ECO:0000313|EMBL:ESZ94394.1};
GN ORFNames=SBOR_5222 {ECO:0000313|EMBL:ESZ94394.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ94394.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ94394.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESZ94394.1}.
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DR EMBL; AYSA01000247; ESZ94394.1; -; Genomic_DNA.
DR STRING; 1432307.W9CI94; -.
DR HOGENOM; CLU_000604_27_6_1; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000019487; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18596; ABC_6TM_VMR1_D1_like; 1.
DR CDD; cd18604; ABC_6TM_VMR1_D2_like; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF335; ABC TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019487};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1017..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1119..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1206..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 274..589
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 616..870
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 952..1258
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1292..1544
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 364..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1559 AA; 173396 MW; CFE28B10FCAFEF2A CRC64;
MLDYNSGSLA AAICCLLVVT VLTFPSVFSI LSHFREKGKQ DPNNYKDKDG VSTEETIAAF
STKVPKTLLV LSTLLGLGTS LALAILDIFH HDGLKLEDWI NVALWSFILI QAVSTILSRS
PTKSFANGAR ATISSICLFA LCLFEDSLIV ENQTAQDDFS SSATFWLRIS QLILALFAAI
SGIYFPRRPH VTHNKRPVDG MLSVSAFGRF TFSWVGDILA LASDKKRLEL QDLPTMDHYT
RAKDLSEAWE ERKHTKALWI EIFLAHKSPF VFQWILTVFQ AFGNFAPQFV TYQILKMLEV
RQPGDKVPFT AWIWVTTLFL VTLAAAWIES WMFWISWSEL AIPIRSQLSS QIFQKAMRRK
DVKGAARSGK KSMAVTSEVA QGSIAQDKPE DNEEEDSDPK GRQSTVNLIG VDAKRLSDFC
SFNNYFPGAV FKLIVSFSFL ISIIGWQSLV AGMLAMSLTI PLNIYFSKRY SAAQDRLMKV
RDVKMAVVTE ALQGIRQIKF SALESNWGNK IGLVRKKELD EQWSVYLNDT MLLFCWITSP
IALAAVALAV YAYLHGVLLP SVAFTAIGVF VNLEVTLSVI PELTTDLIDA YISIKRIQRY
LDGPEISENT SDAPNVSFEK ASIAWPCAEG EDEMDGNERY VLRNVDVSFP KGELSVISGK
TGTGKSLMLA SILGEVDILA GKVHVPRGPR AADRHDHLAN KDNWIIPTSI AFVAQIPWIE
NASIKDNILF GLPLDEGRYQ KVIEYCALRK DLEMLGDGEH TEIGANGINL SGGQRWRVTF
ARALYSRAGI LVLDDIFSAV DAHVGRFIYE KGLTGELGVG RTRILVTHHV ALCKAKAKYL
VELGDGTVES AGFLSDLEEA GTLERIISHE ETSEQIAEDE APITESESST VINASESSDD
ENTNGNSLTK VQSRKEEPKK FVEEETREQG RVKGKVYGHY IKASGGWSFW SLAVIAFIGQ
QFLITGRSWW LRLWTASYEE SSIPTSMFKV QIDNFPLYGS THNSSFQAES IKHNTSYYLI
VYVCLSAVSA IVGTLRYFWI YTGSIRASKI LFDRLCFTVL RTPLRWMDTV PLGRILNRFT
TDFNVVDGRL ANDIGFGANN LFALIGIICT GIFVSPWILL MSSILLALCV YIAILYLPGA
REVKRIESIS KSPIFEQFGS ALTGVGTIRA FDKTDVYIKS MWAKIDNHST SFWHLWAFNR
WMGWRMSFIG AFFATIVAIV IILIPSIDAA LAGFALSFAL SYGQTVIWTI RHYTNLELNM
NAAERIIEYS NLKTESLDGP DPPAAWPTEG RLEVNDLVVS YADDLPPILK GLTFRVERSE
RIGVVGRTGA GKSSLTLALF RFLEAREGTI HIDGLDISKI NLHSLRSRLA IIPQDPVLFS
GTVRSNLDAF DDHTDSELRD ALERVQLIPP SGQNTPSTSG TSTPSLQRNK NPFTSLTSPI
TEGGLNLSQG QRQLLCLARA IVSHPKIMVL DEATSAVDME TDALIQRSIR QEFTDSTLIV
IAHRLSTIAD FDKILVLGEG KVVEFGTPKE LWELSEGVFK GMVKESGERS KLEDMILMS
//
