ID A0A166S8S2_9AGAM Unreviewed; 531 AA.
AC A0A166S8S2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=FIBSPDRAFT_1039133 {ECO:0000313|EMBL:KZP29155.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP29155.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP29155.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP29155.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KV417500; KZP29155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166S8S2; -.
DR STRING; 436010.A0A166S8S2; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13856; CuRO_1_Tv-LCC_like; 1.
DR CDD; cd13903; CuRO_3_Tv-LCC_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; 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.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..531
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007879451"
FT DOMAIN 36..153
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 165..315
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 381..503
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 531 AA; 57860 MW; BF44A4771641AEE0 CRC64;
MPHYAIQTTV ITCLGLVAAA LAAIGPTTNL NIVNAVVAPD GFPRSTVLAD GQFPGPLIRG
NKGDKFSINV FNALTDKTME RSTSIHWHGI FQQGGTNYED GAASVTQCPI VPKNGYQYDF
SVPDQAGTFW YHSHVGLQYC DGLRGPFVVY DPEDPHQSLY DVDDESTVIT LADWYHLPAN
KVPVPFNADS TLINGLGRYQ GGPKDSPLSV VNVTQGLRYR FRLVSMACNI RYNFTIDDHQ
MTIIEVDGVN VEPLVVDSIQ IFSGQRYSFV LEAKQNVNNY RIRAEPREIL PVFGDGAPTG
FRGGINSAIL RYAGAPAEEP TSHQSPSVIP LLETNLHPLE NPGAPGGHHK GGADVELTLN
LAQVVKPTGN VFTINGVTFE PPSVPVLLQI LSGSTKATDL LPKGSVYTLP SNKVIELHIP
GHGIAGSPHP FHLHGHTFDV IRSAGNSTYN YANPVRRDVV STGNTSDNVT IRFVTDNSGP
WMLHCHINFH LNTGMAVVLV EDVEEIAIEA VPKDWKALCP KYEHFNSPFQ E
//
