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AZAK_ASPNA
ID   AZAK_ASPNA              Reviewed;         468 AA.
AC   G3XMC9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Efflux pump azaK {ECO:0000303|PubMed:22921072};
DE   AltName: Full=Azaphilone biosynthesis cluster protein azaK {ECO:0000303|PubMed:22921072};
GN   Name=azaK {ECO:0000303|PubMed:22921072}; ORFNames=ASPNIDRAFT_188912;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=22921072; DOI=10.1016/j.chembiol.2012.07.004;
RA   Zabala A.O., Xu W., Chooi Y.H., Tang Y.;
RT   "Characterization of a silent azaphilone gene cluster from Aspergillus
RT   niger ATCC 1015 reveals a hydroxylation-mediated pyran-ring formation.";
RL   Chem. Biol. 19:1049-1059(2012).
CC   -!- FUNCTION: Efflux pump that might be required for efficient secretion of
CC       azaphilones (PubMed:22921072). {ECO:0000269|PubMed:22921072}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is under the control of the azaphilone cluster-
CC       specific transcription factor azaR (PubMed:22921072).
CC       {ECO:0000269|PubMed:22921072}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; ACJE01000001; EHA28242.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XMC9; -.
DR   SMR; G3XMC9; -.
DR   EnsemblFungi; EHA28242; EHA28242; ASPNIDRAFT_188912.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1079556; -.
DR   HOGENOM; CLU_001265_54_6_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR01035; TCRTETA.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..468
FT                   /note="Efflux pump azaK"
FT                   /id="PRO_0000437627"
FT   TRANSMEM        43..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   468 AA;  50044 MW;  69AB21927FE542E3 CRC64;
     MTVHPPAVAD ETSPLLPSQD GPGHNGIVPA ATKPKELQSS MSQVALLCCA RAIDPLAFFT
     IFPFVNQMIA DTAGIDEADV GFYSGIIESL FSVTQMMLMI PWARAADRMG RKPVLILSLA
     GLSVSSALFG FSRTLGQMVF FRCLAGTFGG TVVTVRVMIS ENSTPDTQAR AFSYFSLANT
     IGTVIGPLLG GALCRPGGVF RHYPYALPTV AAGAFGVTVT VACLMFVNET RKPADHTPHE
     TASPTWTSAK ILRSQGVLPV LYIHGHSMML AFAYTAVSPV FYFTSPRLGG YGFSPFYISL
     FLGGSGIAQT IWLVLVYPPL HKRLGTGNIL RGLCFVWIIF LAATVGASVL HRHCEMVAFW
     ILAPLALVLG SSVAMQLTAM QLALDSVSPS PAALGTLNAM SLAIISFLRA VAPAMFTSMY
     ASTLKLSSPG FYTFWLVLGG LVLVLAFTLR WLPEQVEKAP RKLGRSSA
 
 
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