ID A0A163HMT0_DIDRA Unreviewed; 653 AA.
AC A0A163HMT0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=ST47_g3503 {ECO:0000313|EMBL:KZM25369.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25369.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM25369.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM25369.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:57924; EC=1.14.18.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC ChEBI:CHEBI:58315; EC=1.14.18.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001038};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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:KZM25369.1}.
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DR EMBL; JYNV01000129; KZM25369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163HMT0; -.
DR STRING; 5454.A0A163HMT0; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
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; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF32; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 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:UP000076837};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..653
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007843002"
FT DOMAIN 137..155
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 344..355
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 653 AA; 72583 MW; 08D8B746C683CA58 CRC64;
MAIIAFAQAF QLLLVIGLLC SLTDSKTLVS HPRRHAVTSI QTLSRRQNAT ADFYPILGVV
GLGINTTYAR LEIRELQRKP DLFNVYLLGL QRWQNTSQDD KLSYFQVAGI HGRPFSPWDG
VPGRTQPPEG YKEGYCHHSS NLFPTWHRPF LALVEERVHH HASEVIAEFP EGDLKTRMTS
ALPALRLPYW DAAAVPPIGT GSYPWSVQRK TIEVELPDGS GSVKTTISNP LYSYTFHPLP
GKDMFGKLPW TQWHTTIRYP SDRTAAAQSQ DSKIASQLDL NLVNLRQRTY QMMAMQKDYH
NISNNMVSLG GVLDSLESVH DTIHNTVGSS GPGHMTNAAY SAFDPIFWLL HANVDRMTTI
WQALNPDSWV TNHSNPTATF TSEAGAYADE NTPLHPFHRN QAGDFWTSAS VRDHTIFGYT
YPELIGLSGN VTLVRRVNQL YGDNATSQFS WKIGDGAPLP APGTEYLHHE RRSVSSPQRG
KYQHQYFANI RVQKSESEGG FKVFVFVGPT LVSNTGSTYD ATAWMRDPSF VGFTGFQSTN
GRGGGYLVNA AIKHDANGVV ALTRALEDRV WTGQLSSLDE DAVGQYLHDN MSWRITTAEH
RIIAPEDTPG FEIDVSYARI KPPTADSFPE MQDGGYKHLV RATSGRAGGV QDG
//
