ID A0A2G9H9E5_9LAMI Unreviewed; 415 AA.
AC A0A2G9H9E5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Catechol oxidase {ECO:0000313|EMBL:PIN14147.1};
DE EC=1.10.3.1 {ECO:0000313|EMBL:PIN14147.1};
GN ORFNames=CDL12_13227 {ECO:0000313|EMBL:PIN14147.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN14147.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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:PIN14147.1}.
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DR EMBL; NKXS01002345; PIN14147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9H9E5; -.
DR STRING; 429701.A0A2G9H9E5; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF87; POLYPHENOL OXIDASE CHLOROPLASTIC; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF12142; PPO1_DWL; 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PIN14147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 286..297
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46043 MW; EC31EA8E9F1971C9 CRC64;
MASLHLPCAT TANSAPPRSS SSPFFAKPSH FITHSKRNNR LRVTCADAQN PKDIETSEGK
VDRRNMLLGL GGLYGAANLA STPAASANPI KPAELDKCGC IFKYNTAIDH MRRLPKDDPR
SFMQQANIHC AYCNGAYNQP GQGTLDLQRI LGKLIGDPTF ALPFWNWDNP KGMTIPPMFV
DPKSALYDEK RNQANLPPAV VDLGMTGNTD PLQVVAINLT IMYSEMICGN SDAYDFMGNP
YREGTPVNPG PGASERGSHT AVHVWVGDPR QPSGEDLGNF YSAGRDPLFY CHHGNVDRMW
SLWQYFLPSN KVPDKRITDP DFLNAAFLFY VENAQLVRVT VKDCLDNLRM GYDYERIDLP
WLDYRPPPQT VAARVTRTGK SAPKAETVFP LTLDKIVRIL VPKTKKGKAD QLLVI
//
