ID A0A093V1A3_TALMA Unreviewed; 585 AA.
AC A0A093V1A3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Laccase-2 {ECO:0000313|EMBL:KFX46327.1};
GN ORFNames=GQ26_0190700 {ECO:0000313|EMBL:KFX46327.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX46327.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX46327.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX46327.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX46327.1}.
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DR EMBL; JPOX01000019; KFX46327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V1A3; -.
DR SMR; A0A093V1A3; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_3_1_1; -.
DR Proteomes; UP000029285; 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; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF145; LCC1; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..585
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001888810"
FT DOMAIN 73..188
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 201..353
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 437..549
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 585 AA; 64788 MW; C3B7736F76BD585D CRC64;
MQLVILISLL SVAGLCSCDS ESISGLSPWG TLPSPNLPSW IDFIGVNQWN TNAHQNVVPS
TGKIRKYNFD IRREYAAPDG VNKSVILIND QYPGPLIEAD WGDIITVTVT NNIDVGTEEG
VTLHWHGLTQ KNTPWMDGVP GVTQCPIVPG GSFTYTFQAD QFGSSWYHSH YSAQYNDGLF
GPIVIHGPVQ SGYNYDFDLG PIMISEYTHT SYYESLEMLF EYPPAFPNVD NNLINGKGAF
DCQSNCDEGP SLAKFKFTSG KKHRLRLINT GMTANQKFSI DGHELTVIAN DFVPVQPYKT
NVVTLGVGQR TDVIVEATGN PSGVYWMRSD IDMDCLNMTS TIPNATAIIY YEHANLSAIP
TTTATPWTSN ECRNDPLEST VPYYPQTPPT YPAITQELLI ELKPNASGAF LMYVNNVSTR
VNYDNSVLLD AKAGIPSSSL DPELSIYDFG SNSSVRMVIY NTWGQQHPMH LHGHNFWVLA
EGKGTWDGTV TNPNNPQRRD THLMMPGSTD TPSYIVLEWE LNNPGVWPMH CHMSTHASGG
LIINTLEQPS SIQKQLKIPR AIPETCINWA FFAGHDYIDQ IDSGV
//
