ID A0A164PLH1_9AGAM Unreviewed; 487 AA.
AC A0A164PLH1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Laccase 1 {ECO:0000313|EMBL:KZS88848.1};
DE Flags: Fragment;
GN ORFNames=SISNIDRAFT_417497 {ECO:0000313|EMBL:KZS88848.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS88848.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS88848.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS88848.1,
RC ECO:0000313|Proteomes:UP000076722};
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 -!- 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; KV419432; KZS88848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164PLH1; -.
DR SMR; A0A164PLH1; -.
DR STRING; 1314777.A0A164PLH1; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000076722; 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 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:SF218; FI03373P-RELATED; 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; 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:UP000076722}.
FT DOMAIN 3..107
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 120..273
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 329..457
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZS88848.1"
SQ SEQUENCE 487 AA; 53950 MW; BD558CE9CF1B3368 CRC64;
SRFILTNGSF PGPLISAQKG DRLLVISSIS YDFRMTHIPQ HWHGIFQQRT SGSDGTAEVT
QCPISPFQSF EYQFETGQQS GTYWYHSHLG TQYCDGLIGP LVIYDPKDPH ASLYDVDDAS
TIITIGDWTH LPANEAFANK SILQPSPDST LINGKGLYMG GPTKTSMIPV IGPVQYGKRY
RFRIINVSCN SFFNISFDRH PMNVIEADGT EIVPRSVDAL TIFPGQRYSV VVLDPKNPGS
YWFRTRPTPD IVDWNPTTAD PAVNNAIFRY EGARNTVPLT TIAPTPTTVL REFDMVPGGT
GLPTRKITVP LRLNGTVWTV GNGSFFGTPV PVLMQILTGM IPAQQVLGDD NVVTIDYNQT
IDLTLTNDCD TNQNTTPCDI ADNHPIHLHG HEFAVIQAAG QSKPNYINPP RRDTVAIYNN
DVIIRFNTLN PGPWIFHCHI DWHLSQGMAL VFAEAPNRVI SGPDSVILPP GWSNLCTIYN
KLPPDEQ
//
