AUNC_ASPNC
ID AUNC_ASPNC Reviewed; 565 AA.
AC A2QBE9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Efflux pump aunC {ECO:0000303|PubMed:31067027};
DE AltName: Full=Aurasperone B biosynthesis cluster protein C {ECO:0000303|PubMed:31067027};
GN Name=aunc {ECO:0000303|PubMed:31067027}; ORFNames=An01g15000;
OS Aspergillus niger (strain 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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).
RN [2]
RP FUNCTION.
RX PubMed=31067027; DOI=10.1021/acs.biochem.9b00291;
RA Obermaier S., Mueller M.;
RT "Biaryl-forming enzymes from Aspergilli exhibit substrate-dependent
RT stereoselectivity.";
RL Biochemistry 58:2589-2593(2019).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of aurasperone B, a dimeric gamma-naphthopyrone.
CC {ECO:0000305|PubMed:31067027}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; AM269994; CAK37454.1; -; Genomic_DNA.
DR RefSeq; XP_001389888.1; XM_001389851.2.
DR AlphaFoldDB; A2QBE9; -.
DR SMR; A2QBE9; -.
DR PaxDb; A2QBE9; -.
DR EnsemblFungi; CAK37454; CAK37454; An01g15000.
DR GeneID; 4977901; -.
DR KEGG; ang:ANI_1_2034014; -.
DR VEuPathDB; FungiDB:An01g15000; -.
DR HOGENOM; CLU_000960_22_1_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..565
FT /note="Efflux pump aunC"
FT /id="PRO_0000449888"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 60824 MW; 02D1DB363DB0D22B CRC64;
MSDTARISGG SFTSPPGRDV ELNSFKEASQ TRLYPYSSRK EEEGREDEQQ RPEREEDTGA
LTGYKLVLVT VGLCFCIFCT SLDNTIVATA VPRITQQFHS LDDVGWYASA YLLTTCAVTL
PFGRLYTFFP IKWVYLSALF VFELGSFICG ITPSSLGLIL GRAVAGLGGG GLFSGSLLII
TQCVPLRRRP AFSGFIMSIF AVASVIAPLM GGAFTDHISW RWCFYINLPF GLVSAVVIFF
TFQTTKPVVQ ASLREKAAGL DPLGTATFLP AIVCLLLATQ WGGAQYPWGD GRIIALFTLF
GVLLACFVGL QLWARERATL PPRLLRGRNI WGSALYGFCL NGAMFTFVYY LPIWFQAVQG
TSATESGIRN LPLVISNVIF AIISGVLVSA TGYFGPFMLL SAAMASIAAG LLSMLHPSSG
AGEWIGYQVL LGSSIGMGFQ LPVFVVQTTL ASTDIPTATA LMTFIQLLGG AIFVSVAQNV
FRNQLAADIR AALPMLDPKA VINAGPTSLR AMYSGETLTT LVAMYNDAVV HTFYLAIGLA
AASFLAATVI QWRPSPKSIS HPDSS
