ID   N6UF31_DENPD            Unreviewed;       645 AA.
AC   N6UF31;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00498};
DE   Flags: Fragment;
GN   ORFNames=YQE_03214 {ECO:0000313|EMBL:ENN80355.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN80355.1};
RN   [1] {ECO:0000313|EMBL:ENN80355.1, ECO:0000313|Proteomes:UP000019118}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN80355}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) to UniProtKB.
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; APGK01024671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB740558; ENN80355.1; -; Genomic_DNA.
DR   AlphaFoldDB; N6UF31; -.
DR   EnsemblMetazoa; ENN80355; ENN80355; YQE_03214.
DR   HOGENOM; CLU_012213_0_1_1; -.
DR   OMA; YYMHEQI; -.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:tyrosinase activity; IEA:UniProt.
DR   GO; GO:0006582; P:melanin metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR   Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR   InterPro; IPR005203; Hemocyanin_C.
DR   InterPro; IPR037020; Hemocyanin_C_sf.
DR   InterPro; IPR005204; Hemocyanin_N.
DR   InterPro; IPR036697; Hemocyanin_N_sf.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR   PANTHER; PTHR11511:SF4; PHENOLOXIDASE 2-RELATED; 1.
DR   Pfam; PF03723; Hemocyanin_C; 1.
DR   Pfam; PF00372; Hemocyanin_M; 1.
DR   Pfam; PF03722; Hemocyanin_N; 1.
DR   PRINTS; PR00187; HAEMOCYANIN.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR   PROSITE; PS00209; HEMOCYANIN_1; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          361..372
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN80355.1"
SQ   SEQUENCE   645 AA;  74641 MW;  B171057F9A08CFEF CRC64;
     SDKYRPIGTQ VTSRFGEEAN ERISVNRISI PPLGEVLELP RDTNFSLFIP KHRRIAGRLI
     DIFLGVRNVD DLLAVAVYAR DRVNPYLFNY SLSVALLHRA DTQELDIPSI IHSFPDKYVD
     SKVFSQARED ANVVPEGSRT PIEIPKDFTA SDLEEEHRLA YFREDIGLNL HHWHWHLVYP
     FEAARVIVDK NRRGELFYYM HQQVIARYNL ERFSNKMKRV ERFIDWKASI KEAYFPKLDS
     LVASRSWPAR VTGQKLQNIR RDVDGLIIDV DDLTRWRDRI YDAIHSGVVT DRQGKTIPLT
     ENEGIDILGN MVESSILSPN REFYGDMHNS GHILLSYIHD PDHRHLESFG VIGDSATAMR
     DPIFYRWHAF IDDLFQEFKS SLPRYTENQL NNPGVTVQGV EVEVQGSQPN VLQTYWQQSD
     VDLSRGMDFQ PRGAVFVRFT HLQHARFTYK IQVQSNQVRE GTCRIFLAPK FDERGNPWLF
     RDQRLMFIEL DKFKVNLKQG QNTITRNSGD SSVTIPFERT YRDLDTSRPQ GGDQLAQFNF
     CGCGWPDNLL IPKGSAEGLP CQLFVMISNI NDDRINQDAS GQCNDADSYC GIKDKLYPDR
     RSMGYPFDRM PRNGVDSLQQ FLTSNMRVQD VSIQFLNKTF KPRQV
//