ID A0A3E2HG08_SCYLI Unreviewed; 523 AA.
AC A0A3E2HG08;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Multicopper oxidase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g4366 {ECO:0000313|EMBL:RFU31991.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU31991.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU31991.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU31991.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU31991.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCSJ02000064; RFU31991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HG08; -.
DR STRING; 5539.A0A3E2HG08; -.
DR OMA; YGAIYIH; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13876; CuRO_2_Abr2_like; 1.
DR CDD; cd13898; CuRO_3_Abr2_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:SF488; LACCASE-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; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 3..72
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 101..300
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 392..500
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU31991.1"
FT NON_TER 523
FT /evidence="ECO:0000313|EMBL:RFU31991.1"
SQ SEQUENCE 523 AA; 57074 MW; 68E86B42467691B5 CRC64;
MPFGTTLHSH GIQQQGTPWS DGVPGLSQTL IPSGGSFTYK WTATHYGTYW YHGHSKGQLM
DGFYGPIYIR PAPGVATPFG LISSDSGQKA AMKKAFNNPN MMMITDWSHF TSQEIRDISV
SANIDPFCMD SILINGKGSV NCQDVAFLQT LIPPPLVPLL NGLPYSDKGC MPLESPVGQT
NTTHSLELVP SSMWNNCTAT KSPNEVIQAD PRTGWVNLNW ISSSSVDELT VSIDGHSMWV
YAVDGLFIKP QPVQAMTFPH GSRYSTLIKL DQAPGDYTIR VASSGLNQKV SGFGTLSYDN
GHRKPINVKP FIDYGGVNTT ASVIFFNAAL ASPFISSPPA QTADVTHFLA LNRVADAWVW
SLNGSSFGPP LELRKPLLFD PTSAIPNLSI LSNNGTWIDL IMVLGGLQPS HPIHKHSNKG
YLIGQGVGQF NYSSVVEAMK EIPQFFNLVD PPLVDTYYTP PTLGAGSWQI IRYQVVNPGA
FFLHCHINPH LEGGMGIALM DGIDKWPKIP REYALNPKIV IEP
//