ID A0A1V8V7G0_9PEZI Unreviewed; 709 AA.
AC A0A1V8V7G0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=B0A51_00763 {ECO:0000313|EMBL:OQO31612.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO31612.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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:OQO31612.1}.
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DR EMBL; NAEU01000019; OQO31612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8V7G0; -.
DR STRING; 1974281.A0A1V8V7G0; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05811; CBM20_glucoamylase; 1.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
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 InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR11709:SF87; LACCASE; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..709
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012822491"
FT DOMAIN 36..143
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 136..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 77632 MW; 1CD54A5FF7390E4B CRC64;
MLSSNVLSGI VTLASFVSAS AFVHRDAHER VFARQSSSCI QVSVTFNELK STAWGESVSV
VGSIAQLGNW DTSKAIFMTA TGYTASNPQW VATVNIPPGT SFQYKYIKFN TDGSVQWELD
PNHSYTVPNS CTTNPSIKDT WQSSTPTSTT STKASTSTAT PTPTCTNGPT TRNCWQGTFS
IDTDFDTNWP TTGRTVSYDF DIRNTTMSPD GHARQVLAIN NQYPGPTIYA NWGDMISVTV
HNNMPNNGTS IHWHGLRQWH KGSQDGVPGV NECPLAPGQS KTYTFQATQY GTSWYHSHWS
SQYGDGVLGP IVIYGPATAN YDIDVGPLPI TDWYYPTVAQ TAARTMHVNA GPPKADSALI
NGSMVIQGAG SYSRTTLQPG KRHRLRLINT AVDNHFMVSL DNHVMQVITN DFVPIVPYNT
THLFLGIGQR YDVIITANQA SSNYWFRAEV QVAAGCGDNW NNGNLNAIFS YAGQSGTPTT
SGTSYTQRCT DETGLTPYWN SYVPDGQVAS QVTQLNTWLN QTTNTDGSLT LYWNVNGSSM
NADWAKPTYS YIYSSTSNWP SRANVLTLPT EAKWTYWVLQ SQPGNPYNVA VPHPIHLHGH
DFYILGTGFD TWNTGKIAGL DYTNPTRRDT AMMPAGGWLA IAFQTDNPGA WMLHCHIAWH
ADEGLAVQFL EAPSQVAGFD PKPSNFDSQC AAWNSYASTA AYKKGDSGI
//
