ID A0A0A2JAX0_PENEN Unreviewed; 733 AA.
AC A0A0A2JAX0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=tyrosinase {ECO:0000256|ARBA:ARBA00011906};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
GN ORFNames=PEX2_064880 {ECO:0000313|EMBL:KGO51768.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO51768.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO51768.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO51768.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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:KGO51768.1}.
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DR EMBL; JQFZ01000276; KGO51768.1; -; Genomic_DNA.
DR RefSeq; XP_016594651.1; XM_016743759.1.
DR AlphaFoldDB; A0A0A2JAX0; -.
DR STRING; 27334.A0A0A2JAX0; -.
DR GeneID; 27679179; -.
DR HOGENOM; CLU_013691_1_0_1; -.
DR OrthoDB; 1908494at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate 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; 2.
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 Pfam; PF00337; Gal-bind_lectin; 1.
DR Pfam; PF18132; Tyosinase_C; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 4: Predicted;
KW Lectin {ECO:0000313|EMBL:KGO51768.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 574..720
FT /note="Galectin"
FT /evidence="ECO:0000259|PROSITE:PS51304"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 84069 MW; 150B166911038662 CRC64;
MASELSVHEY YQIQARFPTK ESNPDDGVNR KVFVRQDIDE WSGKKSWTPK KDSLTFKWLQ
VVYDIMIKEI IPQFQEAHQS SWREQAESWR LPFWDWARNG RVPDLAKYPT ITVPRPEGGS
VRINNPLFQF RMPTDKPMQS EGVGTENTWE NDTEQEEYKN FGNAIGTSRW PDEEDQNPNS
EGWRHGVVNN RKVADAFNSH EGYNDKNHGP AAEMVYRLLT VPMDYTTFAS TNPTSKDQNV
DEDLNIEYIH NNVNIDRLFA IWQALNPDKW MDNIPTDNTT IRDSFGKEHP VNGNTPLQPF
RRDSEGNYWT PEGIRFPSNL GYSYPELLRW ETRYRQEDGT LNQILFKENI IAIINRLYGV
SRDLALDPKA PIPEGLEAID GGLKIPDFAF SVRFLKYALG GQPFWVKLYL AQEDGIQTPL
TDLIAEVYNF SQKPELDGSS VCGNCTEGQK SRVKSTAYIP ITPVLYKLIR GGRKLKSLTR
DEVLEYIRKR AYWRNEKELP RYEVEKLELE IIGSSNDTKH FTNPATPPAF ENFKKEPTIT
GGADGALDPE LKQAKIDPPA PRPKRPRANL PLHGILRFQQ TLKADSVILL ESSSVDPVKP
DNGIDMTQIS IMDAENDTIF HISIRRAQGQ IIFNAKFGGS WGEEERIDID RRFNSEDGAT
ILIHDQGDGF EVSIDWVHAI WFAKRAHGRT PQSIWYDIGN KEGTSALSED LEVRTYPSMK
ALFLQKHAHE EEK
//
