ID A0A1V6PRI1_9EURO Unreviewed; 537 AA.
AC A0A1V6PRI1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=PENANT_c047G10993 {ECO:0000313|EMBL:OQD79619.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD79619.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD79619.1}.
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DR EMBL; MDYN01000047; OQD79619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PRI1; -.
DR STRING; 416450.A0A1V6PRI1; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00457; PEBP; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 3.90.280.10; PEBP-like; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR008914; PEBP.
DR InterPro; IPR036610; PEBP-like_sf.
DR InterPro; IPR049556; PhiB.
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; PF01161; PBP; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF49777; PEBP-like; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 271..288
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 460..471
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 537 AA; 60281 MW; 141905694575ABC2 CRC64;
MKAHLSPHIF LSFAYKLFLT PILETYISKM MSYIEYSLSW LFANAKGRDV KLFSKGPAFT
KFPRPTILVE CEEVGPSGSH LDVEHSADGA GRFPTLNWPT ASPEIKQYLL INEDPDAPLP
NPIIHGIYYG IPAMTTTISV HDIEATTEEG TLKGGFRYGK NRRGNVYIPP RPLLGHGPHR
YFFTLVALAE PVDPGRLSLL PTVEEMAREI DGKVVGWGEG ELTPAERIEY TDAVLCMQTQ
PQHLPREEFP GVRNRFDDFV ATHINYTLNV HYSGLFLPWH RHFLWLWETA LQDECGYNGQ
LPYWNWPYWA DNLAASPLFD CSDSSLSGDG EYNPDEQSIQ GGSVTLPRGS GGGCVRCGPF
KNMELHLGPF SRNIASFTEI PAPGFEYNPR CFNRSLNNFV STNYNNETIV DRLLASTDII
DFQTVMDHWP ANAEGVLGVH GGGHFSLGSS LQDLFASPQD PAFMLHHGMI DRLWGQWQAR
DERHRRFALN GTSTILNPPD GIPVTLDTNM EFGVLDQPRS VRDAMNPTRA GYCYSYT
//
