GenomeNet

Database: UniProt
Entry: A0A0C9SUN8_PAXIN
LinkDB: A0A0C9SUN8_PAXIN
Original site: A0A0C9SUN8_PAXIN 
ID   A0A0C9SUN8_PAXIN        Unreviewed;       675 AA.
AC   A0A0C9SUN8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN   ORFNames=PAXINDRAFT_82401 {ECO:0000313|EMBL:KIJ12874.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ12874.1, ECO:0000313|Proteomes:UP000053647};
RN   [1] {ECO:0000313|EMBL:KIJ12874.1, ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ12874.1,
RC   ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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; KN819359; KIJ12874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9SUN8; -.
DR   HOGENOM; CLU_013691_3_2_1; -.
DR   OrthoDB; 1691870at2759; -.
DR   Proteomes; UP000053647; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF76; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 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   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053647}.
FT   DOMAIN          117..134
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          342..353
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   675 AA;  75690 MW;  97CB66851AD0B08D CRC64;
     MTTVKARDYY PITGRSSTGG TFDRIPVEEL KADHPYQWTL FVLGFAWING TPIPFPGVVQ
     PPLKTSLSLM EIGGIHGRPY REWAGDRRTH DEALADFSGV DKKDTNPSPS RFGVSSHAAI
     TFPSWHRPYV MLIEQAIGDY AENVAQQIEN SNAGEVGLWV KASKELRFPC VLVLHRYWDW
     ADPKVEKEGF PSLFYDNELT VTATGHKTVT VPNPLSFFNF PYIPEDFKDT TRNGVTAHFS
     VWPKTYRHAA DSATPVGSNI ADLQTTLKQQ AEDLRTKVGM LFSFPDGGES SIIYDQFSNT
     RNESRQEDDN TTVGSLEGVH NSIHGAIGGN GHMGNPDYAG FDPFFYFHHS NVDRIISLWE
     WCYTSYWMNN GYTVEGVDYS WNQQYGTYAQ AYNEKLEEDG EFGRLVPWRH PDGSYWTNKE
     TRFLTPDAFP KYYSYKEFLG VKVDKPAANL QQQQEARARI AKFYSVDPQT SAQNTTTLAH
     VPVPGVGEVD LPSDFQSIKG FRLFIILARL PEHAFGRSYN FQVFYKGNNL IGNITVFARE
     DDSPCKACAL RRESASLVRG VISIPPRIVH EIIVNSGIDR TKNTMDITTG LVTKALSGKL
     LDLSGKVLAS AQGGEEVAAV PASHAVSKRV QPVEITLLSS AIAQHANDKN QPVHFFDWNA
     HKGLFPVRRP DYLLF
//
DBGET integrated database retrieval system