ID A0A428S8Q3_9HYPO Unreviewed; 614 AA.
AC A0A428S8Q3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Laccase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP52_015977 {ECO:0000313|EMBL:RSL85936.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL85936.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL85936.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL85936.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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:RSL85936.1}.
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DR EMBL; NKCK01000308; RSL85936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428S8Q3; -.
DR STRING; 1325735.A0A428S8Q3; -.
DR Proteomes; UP000287144; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13850; CuRO_1_Abr2_like; 1.
DR CDD; cd13876; CuRO_2_Abr2_like; 1.
DR CDD; cd13898; CuRO_3_Abr2_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF488; LACCASE-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..614
FT /note="Laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019480141"
FT DOMAIN 38..152
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 180..384
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 460..588
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 614 AA; 68572 MW; 953FECF964FE95D7 CRC64;
MASFISYLVF LPLLLHSFFT SVAASGHWKQ TKEFDLKITW EDYAPDGFSR KMLLVNGQSP
GPVLEIDQDD WVVVRVHNYS PENITIHYHG LEMKGSPWSD GVPGVTQLPI EPGCSFTYKF
QATQHGSYWY HSHFKGQIED GLYGPIVIHP RREDPNPFHL ISNDYETVCA LEEAEKRVKP
IVIADFVHLT SNEKWDMTIA AGVEDSCYDS ILFNGKGRVE CIPKEEVEAN LNEVQKAYLS
AVPNGAMTDK ACLPAAALLA LGGGGGNEEA LLPGTFSGCK ETKGQIETIK VSNKHHKSAK
WVAFDIVGAI NFVTGVFSID GHELWVYAMD GSYIEPQKVQ AITVTNGDRY SVFVKVEKSG
DFKMRFNANS APQLITGHAI LSVEGYGKAQ EAEAYINLVG LPVSEDVVFF EQHKAYPFPP
DPISPTADLT FNLSMKIDGA TYLWALNDTR LMSDELDVQK PTLFNPMPYV NNNVTISTKL
NQWVDLVFVA SMVPQPPHPI HKHGTKMYQI GSGTGVFRWN SVEEAMKEIP DQFNIVNPPR
RDAFTSLPAE KDVTWVVVRY HATNPGPWLL HCHINNHMVG GMMMVIQDGV DHWPTVPEEY
APGRQGTRGK KWHH
//
