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Database: UniProt
Entry: A0A1B8AR38_FUSPO
LinkDB: A0A1B8AR38_FUSPO
Original site: A0A1B8AR38_FUSPO 
ID   A0A1B8AR38_FUSPO        Unreviewed;      1461 AA.
AC   A0A1B8AR38;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN   ORFNames=FPOA_09314 {ECO:0000313|EMBL:OBS22995.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS22995.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS22995.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS22995.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       PDR (TC 3.A.1.205) subfamily. {ECO:0000256|ARBA:ARBA00006012}.
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:OBS22995.1}.
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DR   EMBL; LYXU01000003; OBS22995.1; -; Genomic_DNA.
DR   STRING; 36050.A0A1B8AR38; -.
DR   OMA; YTINLWR; -.
DR   OrthoDB; 5473955at2759; -.
DR   Proteomes; UP000091967; 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; cd03233; ABCG_PDR_domain1; 1.
DR   CDD; cd03232; ABCG_PDR_domain2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR029481; ABC_trans_N.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_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   PANTHER; PTHR19241:SF253; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR   PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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|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:UP000091967};
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        486..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        520..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        597..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        734..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1156..1175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1187..1210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1231..1257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1277..1299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1311..1334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1432..1450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..377
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          816..1058
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1461 AA;  163648 MW;  51DD7B9060383C40 CRC64;
     MAQHKEHNPS SSSTTLQDTQ NTDNTSDHDY DADIHQLARR ITSQSTTSGH GPLFPLGENT
     SLDPESPHFN PKKWAKAYLK TRTAAADGNT PRTAGIAFKN LDAFGFGQAT DFQNTLVNIF
     LNATSLVRNI GGYKGQRVDI LRNLDGLVEA GEMLCVLGPP GSGCSTLLRS ISGETHGFHL
     GDDTVLNYQG IRPEQMKKAY RGEAIYTAEV DHHFPHLTVG DTLYFAARCR CPPKDKLPHG
     VTAREYAEHL RDVIMAMFGI SHTKNTRVGN DFVRGVSGGE RKRVTIAEAA LGYSPLQCWD
     NSTRGLDSAN AVEFCRVLRT QADVLGISSC VAIYQAPQSA YDLFDKVVVL YEGRQIFFGR
     TGDAQAYFED LGFVCPEQQT TADFLTSMTN PVERIVRPGA NPPRTSDEFA LAWQNSQARS
     RLLDEIDYYM EQHPFDGPDL QRFSQSRRLD QARVQREKSP FNLSFWQQYT INLWRSVKML
     VGDPSITLTM LVTNVFQALI VSSIFYNLPH NTTSFFRRTT LLFFIVLMNA FSSVLEIMTL
     YEKRKVVEKQ SRYAFYHPSA ESLAAMVTDL PYKVTNAILM NTTLYFMCNL RREPGPYFSF
     LLFSFALTMC MSMMFRFIGS ATKSISQALA PACIILLGLV LYSGYAIPSD YMHDWLAWIR
     WINPVFYGLE SVFLIEFHGQ EYSCSSFVPS GAGYENLNSG ERVCNIAGSV PGQSFVRGED
     YLRTSFGFVD SHRWRNLGIL IVWALFYMAL HLVTTEYVAS ERSKGEVLVF LRESMHKVSG
     KRVSDEESGS SLPVGKQEAP GNSSEKVEVE RQTSVFHWND VCYDIKIKGE DRRILDHVDG
     WVKPGTLTAL MGVSGAGKTT LLDVLASRVT MGVVSGEMLV NGHQRDSSFQ RKTGYVTQQD
     LHQASATVRE ALRFSAILRQ PAKYSKQERI DYVETVISLL GMDAYADAII GVPGEGLNVE
     QRKRLTIGVE LVARPQLLLF LDEPTSGLDS QTSWSICDLM ETLTKSGQAI LCTIHQPSAM
     LFQRFDRLLL LAKGGKTVYF GEVGQNSQVL MDYFTRNGGP ALPPKANPAE HMLHVIGAAP
     GAHSDIDWPA IWRGSPEYQS VQRELQSLKS ESLSSQVQAS SGDASEYKEF ASSYPTQLWE
     VTKRLFQGYW RNPQYMYSKV LLSVGAALFI GLSVMDSSNT IRGLQNQMFG VFLFLTIFSQ
     VAEQMMPVFV EQRTLFEARE RPSKTYSWQS FMFANITVEL AWNSFIGIFS FIVWYYPIGL
     YRNAEWTNQV DSRGITIFLH VLMFFLLAST FTHMIIAGLP DSDTAAGILN LLFIMMFAFC
     GVLAGPDVLS RFWIFMYRVN PFTYVVEGFL GTTLANAPVT CAANEILDFK PTNGSNCSDF
     LSAYISEHGG YLEGESGSST TECHYCPMAN TNSFLKMINI NFDNRWRDFG LLWAYVLFNC
     AAAVAIYLLV RVPKKSKSKT A
//
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