ID A0A2C5Z7T9_9HYPO Unreviewed; 610 AA.
AC A0A2C5Z7T9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Laccase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD80_2520 {ECO:0000313|EMBL:PHH75241.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH75241.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH75241.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH75241.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
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:PHH75241.1}.
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DR EMBL; NJES01000227; PHH75241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Z7T9; -.
DR STRING; 2004952.A0A2C5Z7T9; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13854; CuRO_1_MaLCC_like; 1.
DR CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR CDD; cd13901; CuRO_3_MaLCC_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; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; PLASTOCYANIN-LIKE DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..610
FT /note="Laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013038984"
FT DOMAIN 122..232
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 244..388
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 451..576
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 32..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67908 MW; 8EA6B09DAD82F86B CRC64;
MAPFTRAICA LLASLPGGTW KNPFCVPGVE TQPGKLAQTS PPSSVEEPAQ SSPPGTIGRY
HDEDEDENHL ILPGIVETCA GNTPTTRHKW CKHSIDTDYT RSSPTTGVVR EYWLEATDVI
LAPDGVSRAL TVINGTVPGP TLYADWGDIV RVHFTNSLHT SHNGSSIHFH GIKQNHTVMS
DGVPSITECP LAPGKTRTYE WKAEQYGSSW YHSHFELQAW QGIFGGLIIN GPATADYDED
LGSIFLNDWG HEGPVPMDDK ATIFRGPPIM DSGLINGTNT FGNLGRRYNI AFEAGKSYRL
RFINAAIDSH FKFMLDNHEM TVIASDFIPL EPYVTKIVDI AIGQRYDVII KANQQQVADN
FWLRAIPQLP CSLNKNAHNI RAIVHYGKQP SEPTTTGYPF LDKCQDEKEL TPWFARDARE
PNMTIPIVAS LKIVGDRVKW SVNGTIFTSD WSNPTLLQVI DQVPSFKPST LVVEVPDAEQ
AFYMVLYNLT PFPHPIHLHG HDFAIISQGP GLLFAEEAIN AFTRTNPPRR DTATLPALGH
LVLAIRTTNP GAWLMHCHIG WHTSEGFGLQ ILERAKDIPA LLDTERLRRE CQDWKEYQSR
FSIEQSDSGI
//