ID A0A423VAH5_9PEZI Unreviewed; 688 AA.
AC A0A423VAH5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROV87902.1};
GN ORFNames=VMCG_10276 {ECO:0000313|EMBL:ROV87902.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV87902.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV87902.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV87902.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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:ROV87902.1}.
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; LKEA01000086; ROV87902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VAH5; -.
DR STRING; 356882.A0A423VAH5; -.
DR Proteomes; UP000283895; 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; cd13854; CuRO_1_MaLCC_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:SF71; LACCASE; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT DOMAIN 139..248
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 336..424
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 555..635
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 688 AA; 78076 MW; 8F8A6DB6982586B7 CRC64;
MRLTERAWAA VVEFVAWINP TVLNSFGELG GLQRPLVDSL EWSVGPTDLY PGAFTPPKPH
IGDGNLGDPI FKPPTGDDKF QCDYRKMKGW QPCSSPSNRE CWLRHPDGRE YNVMTNYEVD
SPIGVQRNYT LVINDGWIDA DGRNFTEAKL FNNTYPGPWI QACWGDTVNV KVVNRMKHNG
TSIHWHGIRQ NQTSHMDGVN GVTQCPISPG DSYTYSFRAV QYGSSWYHSH YSVQYADGLL
GPLTIHGPDT ADFDEPKQPI LMTDWVWEWV QYMLTKPPND GIGHDSAFSS IYLQNPNLKN
PSILLNGRGN VTRFDSKNPP PDSPIPEEFV LHFEKRHIGQ NGKAKRYMLR LINTSFRSTF
VFSIDNHALK VIDTDFVPIE PYYNTSIRVG IGQRYRVIVE ARPEEDDDES NPIPEDGNFW
IRTFVADECG QPGQLGYERT GIVRYNSNSK SDPTSRPWPN ISLACSDEPY DSLRPKFPWF
VGSAANGEER FTLKSNFTSG GQPFPLAKFA LDPESATGFT PLQINYSQPM IQHLDDFSGK
WPSQWVVIPE DFNSSSWIHL HGHDFAILQQ SDQSYSLDRV NLTLNNPPRR DVVLLPKNGF
IIIAFKSDNP GTWLMHCHIA FHASEGLALQ ILERQPDANR LFNSPSSPIT KEVERVCDNW
NQWYGDCKNW WSGCDGSHIF QCQDDSGI
//
