ID A0A427Y3J8_9TREE Unreviewed; 576 AA.
AC A0A427Y3J8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Laccase, multicopper oxidase, benzenediol:oxygen oxidorectuctase {ECO:0000313|EMBL:RSH85652.1};
GN Name=LCC2_1 {ECO:0000313|EMBL:RSH85652.1};
GN ORFNames=EHS25_003792 {ECO:0000313|EMBL:RSH85652.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH85652.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH85652.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH85652.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:RSH85652.1}.
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DR EMBL; RSCD01000019; RSH85652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427Y3J8; -.
DR STRING; 1890683.A0A427Y3J8; -.
DR Proteomes; UP000279259; 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; cd13857; CuRO_1_Diphenol_Ox; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 4.
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; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF414; 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; 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:UP000279259};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..576
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019270297"
FT DOMAIN 106..214
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 228..367
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 509..550
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 576 AA; 62165 MW; C61EBFE16B8DE1B7 CRC64;
MRASALAFAL ITLINIPDLA AAVYMPATLK YDRMIAQGPT TRQPGRMAKS LLLKTRISSA
TATSSGSAVT ATYDSSIFTL NSSFVITDVP SRHGRYASVR STQLTPAPDG YERTLYAVNG
QFPGPLIEAN EGDTVIVHVT NNLAMGQSIH WHGMLMNGTQ YMDGVPGFSQ CPIPAGGSFT
YNFTITNQYG SYWWHSHYGN TVADGLVGGL IVHSVNDPLK LGQDYDEERV LMLADWVDVL
SDTVVAELAG GGFDGSRVPP QGDAILVNGI SVARINSSCE VPIPPEIQVP VNKRIRFRVL
NHGSHLLLRL SIDQHPFQVV EVDDTPVYGP DLHELPIAVG QRYSIVVNTT EGTVGDVFWL
RANAAVASFR YVEDGVTPTT QQPTTQAWTD LAAANSECDD LDETNSLTPR VAMYPPESAL
DTHVLSSAFG TFVNVTGQSN TGFGFNNVSY QNQINDPLLA QVERGQSINS SLIANVAFDG
IGGGDIIVNN LDAGIVHPYH LHGRSFFLIQ GGSWAVLRII TDTPGVWPLH CHIGWHLAQG
KMAAIVVQPD AVERIAQPWD WSNLCAGKDA GAWGPD
//
