ID A2QVP0_ASPNC Unreviewed; 1491 AA.
AC A2QVP0;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Contig An11c0070, genomic contig {ECO:0000313|EMBL:CAK40572.1};
GN ORFNames=An11g02110 {ECO:0000313|EMBL:CAK40572.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK40572.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK40572.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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}.
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DR EMBL; AM270224; CAK40572.1; -; Genomic_DNA.
DR EnsemblFungi; CAK40572; CAK40572; An11g02110.
DR HOGENOM; CLU_000604_35_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0005886; C:plasma 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; IPR043926; ABCG_dom.
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:SF682; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 2.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
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}.
FT TRANSMEM 510..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1186..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1251..1283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1295..1317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1323..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1450..1470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..403
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 845..1087
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..474
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 167785 MW; B92B5BC7527895F5 CRC64;
MDSGRSPPHE QSSVLEEEKK TSLDSSSGSS SSASPSSGLS RKQSAIPVEH QVSNENLIRQ
ESSLQRQLTQ QDIARALSQR RSTGAAGADD TDQIARLVSR MFGQERKANS EEEKTRHLGV
VWKDLTVKGV GLGAALQPTN TDILLGLPRL IKGLLTGGRK SAPLRTILDD FNGCVRPGEM
LLVLGRPGSG CSTFLKVIGN QRSGYKSVEG DVRYGGADAE TMAKNYRSEV LYNPEDDLHY
PTLTVRDTLM FALKSRTPDK SSRLPGESRK HYQETFLSTI AKLFWIEHAL GTKVGNELIR
GVSGGEKKRV SIGEALITKA STQCWDNSTK GLDASTALEY VESLRSSTDM AHASTLVALY
QASENLYNLF DKVMLIEEGK CAYYGRTENA KAYFERLGFV CPPRWTTPDF LTSVSDPYAR
RIKEGWEDRV PRSGEDFQRA YQKSEICKEA KADIEDFEKE IESEQRACEQ ARERKRKQNY
TVSFYKQVII LTQRQFLVMY GDKQTLIGKW VMLTFQALII GSLFYDLPPT SAGVFTRGGV
MFYVLLFNSL LAMAELTALY GSRPVILKHK SFSFYRPAAY ALAQVVVDVP IVFVQVTIFE
LIVYFMSNLS RTASQFFINF LFVFILTMTM YSFFRTIGAL SASLDVATRV TGVSVQALIV
YTGYLIPPWK MHPWLKWLIW INPLQYAFEA IMSNEFYDLD LQCVSPSIFP DGPSAQPGNQ
VCAIQGSTPN QLVVQGSNYI EAAFTYSRSH LWRNFGIVIA WFVLFVCLTM VGMELQKPNK
GGSTVTIFKK GEAPEAVQEA VKNKELPGDV ETGSDGAGAT SGFQEKGTDD SSDEVHGIAQ
STSIFTWQGV NYTIPYKDGQ RKLLQDVQGY VKPGRLTALM GASGAGKTTL LNTLAQRINF
GVVTGTFLVD GKPLPKSFQR ATGFAEQMDI HEPTATVRES LQFSALLRQP KEVPIKEKYE
YCEKIIDLLE MRPIAGAIVG EGGAGLNAEQ RKRLTIAVEL ASKPQLLLFL DEPTSGLDSL
AAYNIVRFLR RLADAGQAIL CTIHQPSAVL FEQFDELLLL QSGGRVVYNN ELGTDSKKLI
EYFEQNGARK CSPHENPAEY MLDVIGAGNP DYKGQDWGDV WARSTQHKQV SQEIENIIQE
RRNREVEGEK DDNREYAMPI WVQILTVSKR SFVAYWRTPQ YALGKFLLHI FTGLFNTFTF
WHLGNSYIDM QSRMFSIFMT LTIAPPLIQQ LQPRFLHFRN LYESREAGSK IYSWTAFVTS
AILPELPYSV VAGSIYFNCW YWGVWFPRNS FTSGFIWMFL MLFELFYVGL GQFIAAFSPN
PLFASLLVPT FFTFVLSFCG VVVPYSSLNV FWRSWMYWLT PFHYLLEGFL AVVVHGVPVR
CVPREASEFS PPSGMTCQEY AGSYASQIGG YVQDAGNGLC AFWRPQTLMP YSQARNYNVY
YSHKWRNYGI FWAFVIFNFM AVFFFSWLYL HGVRNMKKSI SARKSKKAVK Q
//
