ID A0A179UUW6_BLAGS Unreviewed; 852 AA.
AC A0A179UUW6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=BDBG_07330 {ECO:0000313|EMBL:OAT11915.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT11915.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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 -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; GG657465; OAT11915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179UUW6; -.
DR STRING; 559298.A0A179UUW6; -.
DR VEuPathDB; FungiDB:BDBG_07330; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.310.20; -; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR InterPro; IPR041640; Tyrosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF76; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51304; GALECTIN; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038}.
FT DOMAIN 692..843
FT /note="Galectin"
FT /evidence="ECO:0000259|PROSITE:PS51304"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 96265 MW; 86FAEDC353E0AABF CRC64;
MENSSMLRQI FGGPSRSSSL SNLSSPTSRD IGTPSNMAGT NYKPPEYLSK RPYEYYAITG
IKAGTVPEKK KAPIRQEIDE WSNNKANADQ VDLFVMAWRN LMNMSPRERG SFFQVAGIHG
QPYVPYDEPD TNMEDTKDKG YCTHNNILFP IWHRPYLVLL EQLLYENMIT EIIPKFSKDR
QAELKEAADS WRLPFWDWAT NHRVPFLAKY PTTTIPTPNG KRERVDNPLY QFKMSTNEPF
LSEGVGQVFD PWAGEDGKGM YFNFGPCIGT SRSPDIEDSQ NPESETWKNG VVNNNQVGIA
LKSPGWMGGG KYGAASEMVY RLLTHPLDYP SFATTFRAKG QDDISKDINL EYIHNNVHGW
VGGNFTGHMS EIPVATFDPL FWLHHCNIDR MWAIWQALNP DKWFETADKN TFFQEAIGLA
DTITPQTKLR PFHSDKKGTC WTPEGARDVL NFGYTYPELQ TWDSKYNSGG TYNRELHVTD
IRKTINEKYG ASRTELLENP ALGDKTDDGV KSNDFAFSVR YKKYALGGNP FKIKIYLAPG
DGKPRTPESD YVTEVYNFSF PAIIGGKEVC SNCTSVEATE SKATSYLSIT YVLVQCVKRG
ILASLEEAVV TKFLQKNLYW RLYQRGRELD RFAMEKIELE VLGSFNNAQH HKDATILSGF
EGFRDIPSLA GGPDGALDPK LKQKPKPLPT NPPAPPSAGL HKNSSLDLKV DFTTDGVIIL
DSTSVDLNQI QTDTIDNTQV AFRNGNDIMF LISFRRAEGQ IVFNTNFGGK WGSEERVNLA
GKLKNRQAAI MVHDQGEGFE VSIDFVHVAW FNKRDKRPVK SLRYSVNKNQ KPVLSEVLKV
SVYPSMKKVF SR
//