ID G4V1F2_NEUT9 Unreviewed; 733 AA.
AC G4V1F2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=NEUTE2DRAFT_117126 {ECO:0000313|EMBL:EGZ67836.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ67836.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ67836.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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 -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; GL891269; EGZ67836.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V1F2; -.
DR STRING; 510952.G4V1F2; -.
DR eggNOG; ENOG502RF2C; Eukaryota.
DR HOGENOM; CLU_013691_2_0_1; -.
DR OMA; FQNPRKW; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..733
FT /note="tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003470317"
FT DOMAIN 296..307
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80331 MW; 00E60E81483FF49D CRC64;
MVTSTLLPLL LLINSFASLA AAQTTPIPVI GVKTGVDSST GQRPIRRNIN DLYARGGPQW
DLYILALSEM QAMNESEELS YFSLAGIHGL PHEVWNGVEQ VEGAPDTGYC PHGETIFAPW
HRPYVALFEQ TLVSHALAIA SRYPPSLLPA YTDAARTLRL PFWDWASDPS LPYAVMNDSI
KVGNTPNSSL ASLSPPNTNG TGGGSGAPSG ATLRCKFEDF AEDNKTVIKR WSEPWVAEEG
MKEVGGQLRD SVYDLFVRPD PRGWGAGGFE DPHNTVHNNA GCGNGTMANI AWSAFDPLFM
LHHANTDRLI ALWQAIYYQN ATFNYSFPSG GQLGTKRGTI LTADSPLKPF HAEFPATIGS
GNATPPSDAG GFFHTSNSVA GLRTFGYTYP ELNTDWQTPD KDKLAAQVRQ AVNKLYGSSD
DGSADDQGQA GVSERNVDSD TLDEEEDDTE NDGGKKTVEN NKITFRRSRS RSRSRSLSAS
SNYKKNEEEA EGTTTTSRDD GKQTEENNKI TFRSSRSLSN SNSSPKKNMK QKRQTYGSQS
PTKNYYYTAE LSVDRSEVPL PCTISLIVNG VVMGRMALLG MPMEGIAKAS MPLARPLKNV
VKIGEQQQGS QSQKRGVDED EKMVGGKRKG RWPSTSRHSN IEKVKPKRGL GHVDMTPKKI
IPFLKGNMTV EIRSNDQTLT DPSTVPSLHL EIQDWEYFPR KNASEFPIFQ NPRKWPMGIR
GPGGHGGYGG RGH
//
