ID A0A317VEV9_9EURO Unreviewed; 1540 AA.
AC A0A317VEV9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ABC metal ion transporter {ECO:0000313|EMBL:PWY72896.1};
GN ORFNames=BO70DRAFT_297348 {ECO:0000313|EMBL:PWY72896.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY72896.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY72896.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY72896.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
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:PWY72896.1}.
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DR EMBL; MSFL01000025; PWY72896.1; -; Genomic_DNA.
DR STRING; 1448321.A0A317VEV9; -.
DR VEuPathDB; FungiDB:BO70DRAFT_297348; -.
DR OrthoDB; 3295317at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProt.
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; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_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; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF456; BILE PIGMENT TRANSPORTER 1-RELATED; 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; 2.
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:UP000247233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1198..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..590
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 628..851
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 972..1252
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1289..1524
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 852..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 171074 MW; 28E0FCD864552748 CRC64;
MLDDGAQTVL GGSNPGSLLS SNPISAFHSP NLQPFCGDVE GWGPISKIRF DLTPCFLDAG
VAVVAAWGLL MGAGALWYLL KKRIPQPVSK NWHFYTKLVV LAALIFTTAL QAAIQAETSP
HIFFGDFRFW SSVLVLASLC VISAVQYYEH WRSRQPNGVV LFYWVFFAIA YGVKLRSLVA
QHAWEDQLPY FVCFNVSLGL ALLEFVLEYF VPKKQSDYDA LGDEDECPYE YADIFSVLTF
SWMTPMMKFG YSNYLTQDDL WNLRHRDSTA VTGNTLRGHW EKELQKKKPS LSWALIKSFG
GSFLRGGIIK CGSDSLAFVQ PQLLRLLITF INSQASDEPQ PIIRGVAIAL GMFLVSISQT
MCLHQYFQRA FDTGMRVKSA LTGMIYAKSL KLSSEGRAAK TTGDIVNHMA VDQQRLSDLT
QFGIQLWSAP FQITLCMLSL YQLVGYSMFA GIGVMILMIP LNGVIARMMK KLQLIQMKNK
DSRSRLMTEI LNNIKSIKLY AWNTAFMNKL SHIRNDLELN TLRKIGATQS VANFTWQSTP
FLVSCSTFTV YALTQDKPLT TDIVFPALTL FNLLTFPLSI LPMVITAVIE ASVAVRRLTE
YFTAEELQTD AVKFEETVAH VGDESVCIRD ASFTWNRYNG THVIEDINFS ARKGELSCIL
GRVGAGKSSL LQALLGDLWR TQGDVVVRGR IAYVAQAPWV MNASVRENIV FGHRWDPQFY
DLTVEACALI DDFKNLPDGD QTEVGERGIS LSGGQKARLT LARAVYARAD IYLLDDVLSA
VDQHVGRHLI NRVLGPNGIL GSKTRILATN AIPVLKEADF IGLLRNKTII EKGTYEQLLA
MKGEVANLIR TNLNDSDDDD SGSESRDLAS PESSESATVI DNASDASDPE DAENEIGALA
PIRASGERRK STVTLRRAST ATWKGPRRKL GDEENVLKSK QTQETSEQGK VKWSVYGEYA
KNSNIIAVCF YLAALLGAQT AQVAGSFWLK HWSEVSEKQP NLGVGKYIGV YLAFGLGSSL
LVIVQNLILW IFCSIEASRK LHERMAFAIF RSPMSFFETT PSGRILNRFS SDIYRIDEVL
ARTFNMLFGN SAKAMFTMIV IASSTPAFLI LVIPLSYVYF SYQKYYLRTS RELKRLDSVT
RSPIFAHFQE SLGGISTIRA YKQEDRFTME NEWRMDANIR AYFPSISANR WLAVRLEFIG
SIIILASAVL SIASVATGSG LSAGMVGLAM SYALQITQSL NWIVRQTVEV ETNIVSVERV
LEYANLPSEA PEVIFKQRPA IGWPAQGAVS FENYSTRYRA GLDLVLKDIN LDIKPHEKIG
VVGRTGAGKS SLTLALFRII EPDGGNISID GLNVSKIGLF DLRGRLAIIP QDPAMFEGTV
RDNLDPRHVH DDTELWSVLE HARLKEHISQ MDGQLDAQIM EGGSNLSQGQ RQLVSLARAL
LTPSNILVLD EATAAVDVET DALLQRTLRS SIFQDRTIIT IAHRINTIID SDRIVVLDKG
RVAEFDTPAE LIKSQGKFYE LVKESGLLDS SDGPGLTQAS
//
