ID A2RBK8_ASPNC Unreviewed; 442 AA.
AC A2RBK8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Contig An19c0010, genomic contig {ECO:0000313|EMBL:CAK47346.1};
DE EC=1.14.18.1 {ECO:0000313|EMBL:CAK47346.1};
GN ORFNames=An19g00230 {ECO:0000313|EMBL:CAK47346.1};
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:CAK47346.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47346.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270415; CAK47346.1; -; Genomic_DNA.
DR EnsemblFungi; CAK47346; CAK47346; An19g00230.
DR VEuPathDB; FungiDB:An19g00230; -.
DR HOGENOM; CLU_035914_2_0_1; -.
DR Proteomes; UP000006706; Chromosome 4ER.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF141; N-ACETYL-6-HYDROXYTRYPTOPHAN OXIDASE IVOB-RELATED; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:CAK47346.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 359..370
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 442 AA; 48799 MW; 08E12460C2D4D9FC CRC64;
MSSHISGDGV AIQFPALFCE NCMLLTAEGI EFTCPLWLGH LSLECSSHTK QGDQVCPQIN
TAPSWLSRGP ATESFLLGAK TEWIVHKKVV VPPLLAVAHN IDPPVGYNLA SNTLNMMLSA
LWLLPAIRLV STSATPTSDA ATTLDPGLFS GGCTPEKMTI RKEWRNMTKV EQQSYLQGVN
CLMDLPAQTG LEATTNRFSD LQALHRALTN TPVGDIIHSV RYFLHTYETX LKEQCGYTGP
MAWWNEAYDT DSGNMFRSEM WDADAFGGNG TEPDGCVTDG AFAYYTEHIG PQNQNTVFCM
NRSWGNFEAI MNTTGAAVAH CNTFDSYDEY FACIAATPHR GGHWAVGGVM EDVKTSPGDP
LFYLHHGYID RLWYRWQMHD PANRLWDMGG PAINESANVE PASGWPQTTL NYTLTTFNIM
PDVTVADVMN PVGGYLCYNY EA
//
