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Database: UniProt
Entry: B0Y7B6_ASPFC
LinkDB: B0Y7B6_ASPFC
Original site: B0Y7B6_ASPFC 
ID   B0Y7B6_ASPFC            Unreviewed;      1088 AA.
AC   B0Y7B6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   13-SEP-2023, entry version 76.
DE   SubName: Full=ABC transporter (Adp1), putative {ECO:0000313|EMBL:EDP49297.1};
GN   ORFNames=AFUB_073240 {ECO:0000313|EMBL:EDP49297.1};
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP49297.1, ECO:0000313|Proteomes:UP000001699};
RN   [1] {ECO:0000313|EMBL:EDP49297.1, ECO:0000313|Proteomes:UP000001699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC   {ECO:0000313|Proteomes:UP000001699};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; DS499599; EDP49297.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y7B6; -.
DR   EnsemblFungi; EDP49297; EDP49297; AFUB_073240.
DR   VEuPathDB; FungiDB:AFUB_073240; -.
DR   HOGENOM; CLU_000604_57_1_1; -.
DR   PhylomeDB; B0Y7B6; -.
DR   Proteomes; UP000001699; 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; cd03213; ABCG_EPDR; 1.
DR   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF2; ATP-DEPENDENT PERMEASE-RELATED; 1.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1088
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002758701"
FT   TRANSMEM        318..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        866..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        909..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        946..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        976..996
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1062..1085
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..120
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          373..615
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          634..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        91..108
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        110..119
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1088 AA;  119927 MW;  5A6318FC5D08A7CF CRC64;
     MMRLRSTVRL SLAALLSLSA STISARSNYS QSELLPPLFS VLDDRPPECP PCFNCQLDAF
     QCAQFAPCNK FNGKCVCPPG FGGDDCSEPV CGSLADGVNR APRKGGSCDC KEGWSGINCN
     VCQTNHACNA MMPEGEGGVC YKQGVTVKEN YQMCDVTNRK ILDQLQGRKP QVTFSCEADD
     HTCNFQFWVD QKESFYCALD TCDWNLETGY NQNKTTYNCK NINCKCIPGR MLCGEEGSID
     IGEFLAQEIK GPASFRTVTT EGGSPEDGSK FQEPAMDDLI KSVFGDPSIF LNCDAGECLY
     HTDVPGYVRP IKQINTPLIA GVIAGCALFV VAVILGVWYL SRRSYHGRIY LPLSDDSDDE
     AARLLADHKP AALYWDNVSY YLNGKEILSG IQGAAHPGEI TAIMGASGAG KTTFLDILAR
     KNKRGTVQGD FYINGEKLSD HDFKSMVGFV DQEDTMLPTL TVHETILTSA LLRLPRDMSR
     AAKEQRVFEV EKQLGIHHIK DQLIGSEEGK GRGISGGEKR RVGIACELVT SPSILFLDEP
     TSGLDAFNAF NVVECLVTLA KTYNRTVIFT IHQPRSNIVA LFDRLILLAH GKTVYSGPFS
     TCQQYFDDSG YSCPPGFNIA DYLVDLTMHA SVTRSHENGH ERPFLDMQPP RTASSSLRAV
     KSVASASNAS IEDSVESSRR PKSKRRISLK QRQDKQLYSR KKDHQTPPTP KTDEEDGGEI
     SDSTQQWLRL SRQQGHVPPQ VLDDPDHLPP AAPGPTDLDI LIANYASSDV ARSVHDEIVA
     AVQKAHVANG STNAEIMSGA ATGHAKSYPR VSLLRQFVIL SQRTWRNLYR NPMLMLTHYA
     ISILLAVLCG YLFYGLTDDI KGFQNRLGLF FFILALFGFS TLTSLTVFST ERLLFVRERA
     NGYYHPITYF AAKVVFDVVP LRLIPPIIMG IIVYPMTGLI PAWGEFFRFI LVLVLFNLAA
     ANICLFIGIV FRDGGVANLI GSLVMLFSLL FAGLLLNHDA IPKSALWLQT LSIFHYGFEA
     LIVNEVTFLT LIDHKYGLDI EVPGASILSA FGFDTLAFWP DVIGLAIISG AFIVIAYAAM
     HFLLVEKR
//
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