ID A0A2N6NV46_BEABA Unreviewed; 566 AA.
AC A0A2N6NV46;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Laccase-2 {ECO:0000313|EMBL:PMB71139.1};
GN Name=lcc2_3 {ECO:0000313|EMBL:PMB71139.1};
GN ORFNames=BM221_003606 {ECO:0000313|EMBL:PMB71139.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB71139.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB71139.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB71139.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB71139.1}.
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DR EMBL; MRVG01000003; PMB71139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NV46; -.
DR OMA; DWYDGNV; -.
DR Proteomes; UP000235728; 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:UP000235728};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015002279"
FT DOMAIN 67..183
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 194..326
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 407..531
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 566 AA; 62437 MW; 66C05C85552E41F7 CRC64;
MLKLRSLVAA LLLSAISASP TSNLYPRDAC AGNTATTRSQ WCNYSVDTDY TTQIPDTGVT
REYWLEITDV VVSPDGFTRP AIAINGSIPG PTLVADWGDT VVVHVSNKLT TSTNGTSIHF
HGIRQRHSNQ ADGVVSITQC PTAVGETETY RWRAEQYGTT WYHSHFAVQA WEGVYGAIVI
NGPATANYDE DLGPLILSDW SRQTADQLAY YSKRHLLPPF QDSGLINGVN VNPNGAGGKR
HTVKFEAGKS YRLRLLNTAL DTHFKFSIDN HRLTVIAVDL VPIEPYTTNV IDIAIAQRYD
VIVTADQGRR ADNFWIRAVP QLPCSLNKNP DKIRGIVYYG NAPSTPSTGS YLYLPSCSDE
SEHRTIVPHV KKSPKDLANA QKSFQSVALA LQNNFYAWTL NSTSTEVDWR NPTLTQVLNG
QTTFERNDGV IELPNANVVF YLVIHSLLPI PHPVHLHGHD FFVLAQGTGV YLPGITKLNS
NNPLRRDTAI LPGTGYLVLG FETDNPGTWL LHCHIGFHVT QGFALQFIER RSEIPGITDA
GALNKTCADW RAYQDANGIH QDDSGV
//